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Human Metabolome Database Version 2.5

 

Showing metabocard for Beta-D-Glucose (HMDB00516)

Legend: metabolite field enzyme field

Version 2.5
Creation Date 2005-11-16 15:48:42
Update Date 2009-05-05 20:58:02
Accession Number HMDB00516
Secondary Accession Numbers HMDB03340
Common Name Beta-D-Glucose
Description A glucoside is a glycoside that is derived from glucose. Glucosides are common in plants, but rare in animals. Glucose is produced when a glucoside is hydrolysed by purely chemical means, or decomposed by fermentation or enzymes. This group contains a benzene and also an ethylene group, being derived from styrolene. Coniferin, C16H22O8, occurs in the cambium of conifer wood. Emulsin converts it into glucose and coniferyl alcohol, while oxidation gives glycovanillin, which yields with emulsin glucose and vanillin. Syringin, which occurs in the bark of Syringe vulgaris, is a methoxyconiferin. Phloridzus occurs in the root-bark of various fruit trees; it hydrolyses to glucose and phloretin, which is the phloroglucin ester of paraoxyhydratropic acid. It is related to the pentosides naringin, C21HEOi1, which hydrolyses to rhamnose and naringenin, the phioroglucin ester of para-oxycinnamic acid, and hesperidin, which hydrolyses to rhamnose and hesperetin, the phloroglucin ester of meta-oxy-para-methoxycinnamic acid or isoferulic acid, C10H10O4. A primary source of energy for living organisms. It is naturally occurring and is found in fruits and other parts of plants in its free state. It is used therapeutically in fluid and nutrient replacement. Classification of the glucosides is a matter of some difficulty. One based on the chemical constitution of the non-glucose part of the molecules has been proposed that frames four groups: (I) ethylene derivatives, (2) benzene derivatives, (3) styrolene derivatives, (4) anthracene derivatives. A group may also be made to include the cyanogenetic glucosides, i.e. those containing prussic acid. Other classifications follow a botanical classification, which has several advantages; in particular, plants of allied genera contain similar compounds. In this article the chemical classification will be followed, and only the more important compounds will be discussed here.
Synonyms
  1. b-D-Glucopyranose
  2. b-Dextrose
  3. b-Glucose
  4. beta-Dextrose
  5. beta-Glucose
  6. beta-delta-Glucopyranose
  7. beta-D-Glucopyranose
  8. beta-D-Glucose
Chemical IUPAC Name (2R,3R,4S,5R,6R)-6-(hydroxymethyl)oxane-2,3,4,5-tetrol
Chemical Formula C6H12O6
Chemical Structure Structure
Chemical Taxonomy
Kingdom
  • Organic
Super Class
  • Carbohydrates and Carbohydrate conjugates
Class
  • Carbohydrates
Sub Class
  • Monosaccharides
Family
  • Mammalian Metabolite
Species
  • hemiacetal
  • primary alcohol
  • secondary alcohol
  • 1,2-diol
  • heterocyclic compound
Biofunction
—
Application
—
Source
  • Endogenous
Average Molecular Weight 180.156
Monoisotopic Molecular Weight 180.063385
Isomeric SMILES OC[C@H]1O[C@@H](O)[C@H](O)[C@@H](O)[C@@H]1O
Canonical SMILES OCC1OC(O)C(O)C(O)C1O
KEGG Compound ID C00221 Link Image
BioCyc ID Not Available
BiGG ID Not Available
Wikipedia Link Not Available
NuGOwiki Link HMDB00516 Link Image
Metagene Link HMDB00516 Link Image
METLIN ID 3755 Link Image
PubChem Compound 64689 Link Image
PubChem Substance 834527 Link Image
ChEBI ID Not Available
CAS Registry Number 492-61-5
InChI Identifier InChI=1/C6H12O6/c7-1-2-3(8)4(9)5(10)6(11)12-2/h2-11H,1H2/t2-,3-,4+,5-,6-/m1/s1
Synthesis Reference Wenck, Helmut; Kinedt, Claudia; Bader, Hans Joachim. Production of b-D-glucose. Praxis der Naturwissenschaften, Chemie (1986), 35(4), 23.
Melting Point (Experimental) Not Available
Experimental Water Solubility Not Available Source: PhysProp
Predicted Water Solubility 782.0 mg/mL [Predicted by ALOGPS] Calculated using ALOGPS
Physiological Charge 0
State Solid
Experimental LogP/Hydrophobicity -3.24 [SANGSTER (1994)] Source: PhysProp
Predicted LogP/Hydrophobicity -2.57 [Predicted by ALOGPS]; -2.3 [Predicted by PubChem via XLOGP] Calculated using ALOGPS
Material Safety Data Sheet (MSDS) Not Available
MOL File Show
SDF File Show
PDB File Show
2D Structure
3D Structure
Experimental PDB ID Not Available
Experimental 1H NMR Spectrum Not Available
Experimental 13C NMR Spectrum Not Available
Experimental 13C HSQC Spectrum Not Available
Predicted 1H NMR Spectrum Show Image
Show Peaklist
Predicted 13C NMR Spectrum Show Image
Show Peaklist
Mass Spectrum Not Available
Simplified TOCSY Spectrum Not Available
BMRB Spectrum Not Available
Cellular Location
  • Cytoplasm
Biofluid Location Not Available
Tissue Location Not Available
Concentrations (Normal) Not Available
Concentrations (Abnormal) Not Available
Associated Disorders Not Available
OMIM ID Not Available
Pathways
Name SMPDB Link KEGG Link
Gluconeogenesis SMP00128 Link Image map00010 Link Image
Glycolysis SMP00040 Link Image map00010 Link Image
Trehalose Degradation SMP00467 Link Image
General References Not Available
Metabolic Enzymes
  1. Glucokinase
  2. Hexokinase-3
  3. Hexokinase-2
  4. Hexokinase-1
  5. GDH/6PGL endoplasmic bifunctional protein precursor [Includes: Glucose 1-dehydrogenase
  6. Lactase-phlorizin hydrolase precursor
  7. Beta-galactosidase precursor
  8. Glucosylceramidase precursor
  9. Glucokinase regulatory protein
  10. Cytosolic beta-glucosidase
  11. Maltase-glucoamylase, intestinal [Includes: Maltase
  12. Aldose 1-epimerase
  13. cDNA FLJ78173, highly similar to Homo sapiens hexokinase 1 (HK1) mRNA
  14. Putative uncharacterized protein LOC130589 (Galactose mutarotase) (Aldose 1-epimerase) (cDNA FLJ75695, highly similar to Homo sapiens galactose mutarotase (aldose 1-epimerase) (GALM), mRNA)
Enzyme 1 [top]
Enzyme 1 ID 5442
Enzyme 1 Name Glucokinase
Enzyme 1 Synonyms
  1. Hexokinase-4
  2. Hexokinase type IV
  3. HK IV
  4. HK4
  5. Hexokinase-D
Enzyme 1 Gene Name GCK
Enzyme 1 Protein Sequence >Glucokinase 
MLDDRARMEAAKKEKVEQILAEFQLQEEDLKKVMRRMQKEMDRGLRLETHEEASVKMLPT
YVRSTPEGSEVGDFLSLDLGGTNFRVMLVKVGEGEEGQWSVKTKHQMYSIPEDAMTGTAE
MLFDYISECISDFLDKHQMKHKKLPLGFTFSFPVRHEDIDKGILLNWTKGFKASGAEGNN
VVGLLRDAIKRRGDFEMDVVAMVNDTVATMISCYYEDHQCEVGMIVGTGCNACYMEEMQN
VELVEGDEGRMCVNTEWGAFGDSGELDEFLLEYDRLVDESSANPGQQLYEKLIGGKYMGE
LVRLVLLRLVDENLLFHGEASEQLRTRGAFETRFVSQVESDTGDRKQIYNILSTLGLRPS
TTDCDIVRRACESVSTRAAHMCSAGLAGVINRMRESRSEDVMRITVGVDGSVYKLHPSFK
ERFHASVRRLTPSCEITFIESEEGSGRGAALVSAVACKKACMLGQ
Enzyme 1 Number of Residues 465
Enzyme 1 Molecular Weight 52192
Enzyme 1 Theoretical pI 4.85
Enzyme 1 GO Classification
Function
  • ATP binding
  • adenyl nucleotide binding
  • binding
  • catalytic activity
  • hexokinase activity
  • nucleotide binding
  • phosphotransferase activity, alcohol group as acceptor
  • purine nucleotide binding
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • alcohol metabolism
  • cellular metabolism
  • glucose catabolism
  • glucose metabolism
  • glycolysis
  • hexose metabolism
  • metabolism
  • monosaccharide metabolism
  • physiological process
Component
—
Enzyme 1 General Function Not Available
Enzyme 1 Specific Function Catalyzes the initial step in utilization of glucose by the beta-cell and liver at physiological glucose concentration. Glucokinase has a high Km for glucose, and so it is effective only when glucose is abundant. The role of GCK is to provide G6P for the synthesis of glycogen. Pancreatic glucokinase plays an important role in modulating insulin secretion. Hepatic glucokinase helps to facilitate the uptake and conversion of glucose by acting as an insulin-sensitive determinant of hepatic glucose usage
Enzyme 1 Pathways
Enzyme 1 Reactions
  • ATP + D-glucose = ADP + D-glucose 6-phosphate
Enzyme 1 Pfam Domain Function
Enzyme 1 Signals
  • None
Enzyme 1 Transmembrane Regions
  • None
Enzyme 1 Essentiality Not Available
Enzyme 1 GenBank ID Protein 179427 Link Image
Enzyme 1 UniProtKB/Swiss-Prot ID P35557 Link Image
Enzyme 1 UniProtKB/Swiss-Prot Entry Name HXK4_HUMAN Link Image
Enzyme 1 PDB ID 1V4T Link Image
Enzyme 1 PDB File Show
Enzyme 1 3D Structure
Enzyme 1 Cellular Location Not Available
Enzyme 1 Gene Sequence >1398 bp 
ATGCTGGACGACAGAGCCAGGATGGAGGCCGCCAAGAAGGAGAAGGTAGAGCAGATCCTG
GCAGAGTTCCAGCTGCAGGAGGAGGACCTGAAGAAGGTGATGAGACGGATGCAGAAGGAG
ATGGACCGCGGCCTGAGGCTGGAGACCCATGAAGAGGCCAGTGTGAAGATGCTGCCCACC
TACGTGCGCTCCACCCCAGAAGGCTCAGAAGTCGGGGACTTCCTCTCCCTGGACCTGGGT
GGCACTAACTTCAGGGTGATGCTGGTGAAGGTGGGAGAAGGTGAGGAGGGGCAGTGGAGC
GTGAAGACCAAACACCAGATGTACTCCATCCCCGAGGACGCCATGACCGGCACTGCTGAG
ATGCTCTTCGACTACATCTCTGAGTGCATCTCCGACTTCCTGGACAAGCATCAGATGAAA
CACAAGAAGCTGCCCCTGGGCTTCACCTTCTCCTTTCCTGTGAGGCACGAAGACATCGAT
AAGGGCATCCTTCTCAACTGGACCAAGGGCTTCAAGGCCTCAGGAGCAGAAGGGAACAAT
GTCGTGGGGCTTCTGCGAGACGCTATCAAACGGAGAGGGGACTTTGAAATGGATGTGGTG
GCAATGGTGAATGACACGGTGGCCACGATGATCTCCTGCTACTACGAAGACCATCAGTGC
GAGGTCGGCATGATCGTGGGCACGGGCTGCAATGCCTGCTACATGGAGGAGATGCAGAAT
GTGGAGCTGGTGGAGGGGGACGAGGGCCGCATGTGCGTCAATACCGAGTGGGGCGCCTTC
GGGGACTCCGGCGAGCTGGACGAGTTCCTGCTGGAGTATGACCGCCTGGTGGACGAGAGC
TCTGCAAACCCCGGTCAGCAGCTGTATGAGAAGCTCATAGGTGGCAAGTACATGGGCGAG
CTGGTGCGGCTTGTGCTGCTCAGGCTCGTGGACGAAAACCTGCTCTTCCACGGGGAGGCC
TCCGAGCAGCTGCGCACACGCGGAGCCTTCGAGACGCGCTTCGTGTCGCAGGTGGAGAGC
GACACGGGCGACCGCAAGCAGATCTACAACATCCTGAGCACGCTGGGGCTGCGACCCTCG
ACCACCGACTGCGACATCGTGCGCCGCGCCTGCGAGAGCGTGTCTACGCGCGCTGCGCAC
ATGTGCTCGGCGGGGCTGGCGGGCGTCATCAACCGCATGCGCGAGAGCCGCAGCGAGGAC
GTAATGCGCATCACTGTGGGCGTGGATGGCTCCGTGTACAAGCTGCACCCCAGCTTCAAG
GAGCGGTTCCATGCCAGCGTGCGCAGGCTGACGCCCAGCTGCGAGATCACCTTCATCGAG
TCGGAGGAGGGCAGTGGCCGGGGCGCGGCCCTGGTCTCGGCGGTGGCCTGTAAGAAGGCC
TGTATGCTGGGCCAGTGA
Enzyme 1 GenBank Gene ID M88011 Link Image
Enzyme 1 GeneCard ID GCK Link Image
Enzyme 1 GenAtlas ID GCK Link Image
Enzyme 1 HGNC ID HGNC:4195 Link Image
Enzyme 1 Chromosome Location 7
Enzyme 1 Locus 7p15.3-p15.1
Enzyme 1 SNPs SNPJam Report Link Image
Enzyme 1 General References
  1. Tanizawa Y, Matsutani A, Chiu KC, Permutt MA: Human glucokinase gene: isolation, structural characterization, and identification of a microsatellite repeat polymorphism. Mol Endocrinol. 1992 Jul;6(7):1070-81. [PubMed Link Image]
  2. Tanizawa Y, Koranyi LI, Welling CM, Permutt MA: Human liver glucokinase gene: cloning and sequence determination of two alternatively spliced cDNAs. Proc Natl Acad Sci U S A. 1991 Aug 15;88(16):7294-7. [PubMed Link Image]
  3. Nishi S, Stoffel M, Xiang K, Shows TB, Bell GI, Takeda J: Human pancreatic beta-cell glucokinase: cDNA sequence and localization of the polymorphic gene to chromosome 7, band p 13. Diabetologia. 1992 Aug;35(8):743-7. [PubMed Link Image]
  4. Koranyi LI, Tanizawa Y, Welling CM, Rabin DU, Permutt MA: Human islet glucokinase gene. Isolation and sequence analysis of full-length cDNA. Diabetes. 1992 Jul;41(7):807-11. [PubMed Link Image]
  5. Stoffel M, Froguel P, Takeda J, Zouali H, Vionnet N, Nishi S, Weber IT, Harrison RW, Pilkis SJ, Lesage S, et al.: Human glucokinase gene: isolation, characterization, and identification of two missense mutations linked to early-onset non-insulin-dependent (type 2) diabetes mellitus. Proc Natl Acad Sci U S A. 1992 Aug 15;89(16):7698-702. [PubMed Link Image]
  6. Sakura H, Eto K, Kadowaki H, Simokawa K, Ueno H, Koda N, Fukushima Y, Akanuma Y, Yazaki Y, Kadowaki T: Structure of the human glucokinase gene and identification of a missense mutation in a Japanese patient with early-onset non-insulin-dependent diabetes mellitus. J Clin Endocrinol Metab. 1992 Dec;75(6):1571-3. [PubMed Link Image]
  7. St Charles R, Harrison RW, Bell GI, Pilkis SJ, Weber IT: Molecular model of human beta-cell glucokinase built by analogy to the crystal structure of yeast hexokinase B. Diabetes. 1994 Jun;43(6):784-91. [PubMed Link Image]
  8. Stoffel M, Patel P, Lo YM, Hattersley AT, Lucassen AM, Page R, Bell JI, Bell GI, Turner RC, Wainscoat JS: Missense glucokinase mutation in maturity-onset diabetes of the young and mutation screening in late-onset diabetes. Nat Genet. 1992 Oct;2(2):153-6. [PubMed Link Image]
  9. Chiu KC, Tanizawa Y, Permutt MA: Glucokinase gene variants in the common form of NIDDM. Diabetes. 1993 Apr;42(4):579-82. [PubMed Link Image]
  10. Stoffel M, Bell KL, Blackburn CL, Powell KL, Seo TS, Takeda J, Vionnet N, Xiang KS, Gidh-Jain M, Pilkis SJ, et al.: Identification of glucokinase mutations in subjects with gestational diabetes mellitus. Diabetes. 1993 Jun;42(6):937-40. [PubMed Link Image]
  11. Takeda J, Gidh-Jain M, Xu LZ, Froguel P, Velho G, Vaxillaire M, Cohen D, Shimada F, Makino H, Nishi S, et al.: Structure/function studies of human beta-cell glucokinase. Enzymatic properties of a sequence polymorphism, mutations associated with diabetes, and other site-directed mutants. J Biol Chem. 1993 Jul 15;268(20):15200-4. [PubMed Link Image]
  12. Gidh-Jain M, Takeda J, Xu LZ, Lange AJ, Vionnet N, Stoffel M, Froguel P, Velho G, Sun F, Cohen D, et al.: Glucokinase mutations associated with non-insulin-dependent (type 2) diabetes mellitus have decreased enzymatic activity: implications for structure/function relationships. Proc Natl Acad Sci U S A. 1993 Mar 1;90(5):1932-6. [PubMed Link Image]
  13. Hager J, Blanche H, Sun F, Vaxillaire NV, Poller W, Cohen D, Czernichow P, Velho G, Robert JJ, Cohen N, et al.: Six mutations in the glucokinase gene identified in MODY by using a nonradioactive sensitive screening technique. Diabetes. 1994 May;43(5):730-3. [PubMed Link Image]
  14. Velho G, Blanche H, Vaxillaire M, Bellanne-Chantelot C, Pardini VC, Timsit J, Passa P, Deschamps I, Robert JJ, Weber IT, Marotta D, Pilkis SJ, Lipkind GM, Bell GI, Froguel P: Identification of 14 new glucokinase mutations and description of the clinical profile of 42 MODY-2 families. Diabetologia. 1997 Feb;40(2):217-24. [PubMed Link Image]
  15. Hattersley AT, Beards F, Ballantyne E, Appleton M, Harvey R, Ellard S: Mutations in the glucokinase gene of the fetus result in reduced birth weight. Nat Genet. 1998 Jul;19(3):268-70. [PubMed Link Image]
  16. Glaser B, Kesavan P, Heyman M, Davis E, Cuesta A, Buchs A, Stanley CA, Thornton PS, Permutt MA, Matschinsky FM, Herold KC: Familial hyperinsulinism caused by an activating glucokinase mutation. N Engl J Med. 1998 Jan 22;338(4):226-30. [PubMed Link Image]
  17. Ng MC, Cockburn BN, Lindner TH, Yeung VT, Chow CC, So WY, Li JK, Lo YM, Lee ZS, Cockram CS, Critchley JA, Bell GI, Chan JC: Molecular genetics of diabetes mellitus in Chinese subjects: identification of mutations in glucokinase and hepatocyte nuclear factor-1alpha genes in patients with early-onset type 2 diabetes mellitus/MODY. Diabet Med. 1999 Nov;16(11):956-63. [PubMed Link Image]
  18. Nam JH, Lee HC, Kim YH, Cha BS, Song YD, Lim SK, Kim KR, Huh KB: Identification of glucokinase mutation in subjects with post-renal transplantation diabetes mellitus. Diabetes Res Clin Pract. 2000 Dec;50(3):169-76. [PubMed Link Image]
  19. Njolstad PR, Sovik O, Cuesta-Munoz A, Bjorkhaug L, Massa O, Barbetti F, Undlien DE, Shiota C, Magnuson MA, Molven A, Matschinsky FM, Bell GI: Neonatal diabetes mellitus due to complete glucokinase deficiency. N Engl J Med. 2001 May 24;344(21):1588-92. [PubMed Link Image]
Enzyme 1 Metabolite References Not Available
Enzyme 2 [top]
Enzyme 2 ID 5444
Enzyme 2 Name Hexokinase-3
Enzyme 2 Synonyms
  1. Hexokinase type III
  2. HK III
Enzyme 2 Gene Name HK3
Enzyme 2 Protein Sequence >Hexokinase-3 
MDSIGSSGLRQGEETLSCSEEGLPGPSDSSELVQECLQQFKVTRAQLQQIQASLLGSMEQ
ALRGQASPAPAVRMLPTYVGSTPHGTEQGDFVVLELGATGASLRVLWVTLTGIEGHRVEP
RSQEFVIPQEVMLGAGQQLFDFAAHCLSEFLDAQPVNKQGLQLGFSFSFPCHQTGLDRST
LISWTKGFRCSGVEGQDVVQLLRDAIRRQGAYNIDVVAVVNDTVGTMMGCEPGVRPCEVG
LVVDTGTNACYMEEARHVAVLDEDRGRVCVSVEWGSLSDDGALGPVLTTFDHTLDHESLN
PGAQRFEKMIGGLYLGELVRLVLAHLARCGVLFGGCTSPALLSQGSILLEHVAEMEDPST
GAARVHAILQDLGLSPGASDVELVQHVCAAVCTRAAQLCAAALAAVLSCLQHSREQQTLQ
VAVATGGRVCERHPRFCSVLQGTVMLLAPECDVSLIPSVDGGGRGVAMVTAVAARLAAHR
RLLEETLAPFRLNHDQLAAVQAQMRKAMAKGLRGEASSLRMLPTFVRATPDGSERGDFLA
LDLGGTNFRVLLVRVTTGVQITSEIYSIPETVAQGSGQQLFDHIVDCIVDFQQKQGLSGQ
SLPLGFTFSFPCRQLGLDQGILLNWTKGFKASDCEGQDVVSLLREAITRRQAVELNVVAI
VNDTVGTMMSCGYEDPRCEIGLIVGTGTNACYMEELRNVAGVPGDSGRMCINMEWGAFGD
DGSLAMLSTRFDASVDQASINPGKQRFEKMISGMYLGEIVRHILLHLTSLGVLFRGQQIQ
RLQTRDIFKTKFLSEIESDSLALRQVRAILEDLGLPLTSDDALMVLEVCQAVSQRAAQLC
GAGVAAVVEKIRGNRGLEELAVSVGVDGTLYKLHPRFSSLVAATVRELAPRCVVTFLQSE
DGSGKGAALVTAVACRLAQLTRV
Enzyme 2 Number of Residues 923
Enzyme 2 Molecular Weight 98921
Enzyme 2 Theoretical pI 5.11
Enzyme 2 GO Classification
Function
  • ATP binding
  • adenyl nucleotide binding
  • binding
  • catalytic activity
  • hexokinase activity
  • nucleotide binding
  • phosphotransferase activity, alcohol group as acceptor
  • purine nucleotide binding
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • alcohol metabolism
  • cellular metabolism
  • glucose catabolism
  • glucose metabolism
  • glycolysis
  • hexose metabolism
  • metabolism
  • monosaccharide metabolism
  • physiological process
Component
—
Enzyme 2 General Function Not Available
Enzyme 2 Specific Function ATP + D-hexose = ADP + D-hexose 6-phosphate
Enzyme 2 Pathways
Enzyme 2 Reactions
  • ATP + D-hexose = ADP + D-hexose 6-phosphate
Enzyme 2 Pfam Domain Function
Enzyme 2 Signals
  • None
Enzyme 2 Transmembrane Regions
  • None
Enzyme 2 Essentiality Not Available
Enzyme 2 GenBank ID Protein 1255788 Link Image
Enzyme 2 UniProtKB/Swiss-Prot ID P52790 Link Image
Enzyme 2 UniProtKB/Swiss-Prot Entry Name HXK3_HUMAN Link Image
Enzyme 2 PDB ID Not Available
Enzyme 2 Cellular Location Not Available
Enzyme 2 Gene Sequence >2772 bp 
ATGGACTCCATTGGGTCTTCAGGGTTGCGGCAGGGGGAAGAAACCCTGAGTTGCTCTGAG
GAGGGCTTGCCCGGGCCCTCAGACAGCTCAGAGCTGGTGCAGGAGTGCCTGCAGCAGTTC
AAGGTGACAAGGGCACAGCTACAGCAGATCCAAGCCAGCCTCTTGGGTTCCATGGAGCAG
GCGCTGAGGGGACAGGCCAGCCCTGCCCCTGCGGTCCGGATGCTGCCTACATACGTGGGG
TCCACCCCACATGGCACTGAGCAAGGAGACTTCGTGGTGCTGGAGCTGGGGGCCACAGGG
GCCTCACTGCGTGTTTTGTGGGTGACTCTAACTGGCATTGAGGGGCATAGGGTGGAGCCC
AGAAGCCAGGAGTTTGTGATCCCCCAAGAGGTGATGCTGGGTGCTGGCCAGCAGCTCTTT
GACTTTGCTGCCCACTGCCTGTCTGAGTTCCTGGATGCGCAGCCTGTGAACAAACAGGGT
CTGCAGCTTGGCTTCAGCTTCTCTTTCCCTTGTCACCAGACGGGCTTGGACAGGAGCACC
CTCATTTCCTGGACCAAAGGTTTTAGGTGCAGTGGTGTGGAAGGCCAGGATGTGGTCCAG
CTGCTGAGAGATGCCATTCGGAGGCAGGGGGCCTACAACATCGACGTGGTTGCTGTGGTG
AACGACACAGTGGGCACCATGATGGGCTGTGAGCCGGGGGTCAGGCCGTGTGAGGTTGGG
CTAGTTGTAGACACGGGCACCAACGCGTGTTACATGGAGGAGGCACGGCATGTGGCAGTG
CTGGACGAAGACCGGGGCCGCGTCTGCGTCAGCGTCGAGTGGGGCTCCTTAAGCGATGAT
GGGGCGCTGGGACCAGTGCTGACCACCTTCGACCATACCCTGGACCATGAGTCCCTGAAT
CCTGGTGCTCAGAGGTTTGAGAAGATGATCGGAGGCCTGTACCTGGGTGAGCTGGTGCGG
CTGGTGCTGGCTCACTTGGCCCGGTGTGGGGTCCTCTTTGGTGGCTGCACCTCCCCTGCC
CTGCTGAGCCAAGGCAGCATCCTCCTGGAACACGTGGCTGAGATGGAGGACCCCTCTACT
GGGGCAGCCCGTGTCCATGCTATCCTGCAGGACTTGGGCCTGAGCCCTGGGGCTTCGGAT
GTTGAGCTTGTGCAGCACGTCTGTGCGGCCGTGTGCACGCGGGCTGCCCAGCTCTGTGCT
GCCGCCCTGGCCGCTGTTCTCTCCTGCCTCCAGCACAGCCGGGAGCAACAAACACTCCAG
GTTGCTGTGGCCACCGGAGGCCGAGTGTGTGAGCGGCACCCCAGGTTCTGCAGCGTCCTG
CAGGGGACAGTGATGCTCCTGGCCCCGGAATGCGATGTCTCCTTAATCCCCTCTGTGGAT
GGTGGTGGCCGGGGAGTGGCGATGGTGACTGCTGTGGCTGCCCGTCTGGCTGCCCACCGG
CGCCTGCTGGAGGAGACCCTGGCCCCATTCCGGTTGAACCATGATCAACTGGCTGCGGTT
CAGGCACAGATGCGGAAGGCCATGGCCAAGGGGCTCCGAGGGGAGGCCTCCTCCCTTCGC
ATGCTGCCCACTTTCGTCCGGGCCACCCCTGACGGCAGCGAGCGAGGGGATTTCCTGGCC
CTGGACCTCGGGGGCACGAACTTCCGTGTCCTCCTGGTACGTGTGACCACAGGCGTGCAG
ATCACCAGCGAGATCTACTCCATTCCCGAGACTGTGGCCCAGGGTTCTGGGCAGCAGCTC
TTTGACCACATCGTGGACTGCATCGTGGACTTCCAGCAGAAGCAGGGCCTGAGCGGGCAG
AGCCTCCCACTGGGTTTTACCTTCTCCTTCCCATGTAGGCAGCTTGGCCTAGACCAGGGC
ATCCTCCTGAACTGGACCAAGGGTTTCAAGGCATCAGACTGCGAGGGCCAAGATGTCGTG
AGTCTGTTGCGGGAAGCCATCACTCGCAGACAGGCAGTGGAGCTGAATGTGGTTGCCATT
GTCAATGACACGGTGGGGACCATGATGTCCTGTGGCTATGAGGACCCCCGTTGCGAGATA
GGCCTCATTGTCGGAACCGGCACCAATGCCTGCTACATGGAGGAGCTCCGGAATGTGGCG
GGCGTGCCTGGGGACTCAGGCCGCATGTGCATCAACATGGAGTGGGGCGCCTTTGGGGAC
GATGGCTCTCTGGCCATGCTCAGCACCCGCTTTGATGCAAGTGTGGACCAGGCGTCCATC
AACCCCGGCAAGCAGAGGTTTGAAAAGATGATCAGCGGCATGTACCTGGGGGAGATCGTC
CGCCACATCCTTTTACATTTAACCAGCCTTGGCGTTCTCTTCCGGGGCCAGCAGATCCAG
CGCCTTCAGACCAGGGACATCTTCAAGACCAAGTTCCTCTCTGAGATCGAAAGTGACAGC
CTGGCCCTGCGGCAGGTCCGAGCCATCCTAGAGGATCTGGGGCTACCCCTGACCTCAGAT
GACGCCCTGATGGTGCTAGAGGTGTGCCAGGCTGTGTCCCAGAGGGCTGCCCAGCTCTGT
GGGGCGGGTGTAGCTGCCGTGGTGGAGAAGATCCGGGGGAACCGGGGCCTGGAAGAGCTG
GCAGTGTCTGTGGGGGTGGATGGAACGCTCTACAAGCTGCACCCGCGCTTCTCCAGCCTG
GTGGCGGCCACAGTGCGGGAGCTGGCCCCTCGCTGTGTGGTCACGTTCCTGCAGTCAGAG
GATGGGTCCGGCAAAGGTGCGGCCCTGGTCACCGCTGTTGCCTGCCGCCTTGCGCAGTTG
ACTCGTGTCTGA
Enzyme 2 GenBank Gene ID U51333 Link Image
Enzyme 2 GeneCard ID HK3 Link Image
Enzyme 2 GenAtlas ID HK3 Link Image
Enzyme 2 HGNC ID HGNC:4925 Link Image
Enzyme 2 Chromosome Location 5
Enzyme 2 Locus 5q35.2
Enzyme 2 SNPs SNPJam Report Link Image
Enzyme 2 General References
  1. Furuta H, Nishi S, Le Beau MM, Fernald AA, Yano H, Bell GI: Sequence of human hexokinase III cDNA and assignment of the human hexokinase III gene (HK3) to chromosome band 5q35.2 by fluorescence in situ hybridization. Genomics. 1996 Aug 15;36(1):206-9. [PubMed Link Image]
  2. Palma F, Agostini D, Mason P, Dacha M, Piccoli G, Biagiarelli B, Fiorani M, Stocchi V: Purification and characterization of the carboxyl-domain of human hexokinase type III expressed as fusion protein. Mol Cell Biochem. 1996 Feb 9;155(1):23-9. [PubMed Link Image]
Enzyme 2 Metabolite References Not Available
Enzyme 3 [top]
Enzyme 3 ID 5445
Enzyme 3 Name Hexokinase-2
Enzyme 3 Synonyms
  1. Hexokinase type II
  2. HK II
  3. Muscle form hexokinase
Enzyme 3 Gene Name HK2
Enzyme 3 Protein Sequence >Hexokinase-2 
MIASHLLAYFFTELNHDQVQKVDQYLYHMRLSDETLLEISKRFRKEMEKGLGATTHPTAA
VKMLPTFVRSTPDGTEHGEFLALDLGGTNFRVLWVKVTDNGLQKVEMENQIYAIPEDIMR
GSGTQLFDHIAECLANFMDKLQIKDKKLPLGFTFSFPCHQTKLDESFLVSWTKGFKSSGV
EGRDVVALIRKAIQRRGDFDIDIVAVVNDTVGTMMTCGYDDHNCEIGLIVGTGSNACYME
EMRHIDMVEGDEGRMCINMEWGAFGDDGSLNDIRTEFDQEIDMGSLNPGKQLFEKMISGM
YMGELVRLILVKMAKEELLFGGKLSPELLNTGRFETKDISDIEGEKDGIRKAREVLMRLG
LDPTQEDCVATHRICQIVSTRSASLCAATLAAVLQRIKENKGEERLRSTIGVDGSVYKKH
PHFAKRLHKTVRRLVPGCDVRFLRSEDGSGKGAAMVTAVAYRLADQHRARQKTLEHLQLS
HDQLLEVKRRMKVEMERGLSKETHASAPVKMLPTYVCATPDGTEKGDFLALDLGGTNFRV
LLVRVRNGKWGGVEMHNKIYAIPQEVMHGTGDELFDHIVQCIADFLEYMGMKGVSLPLGF
TFSFPCQQNSLDESILLKWTKGFKASGCEGEDVVTLLKEAIHRREEFDLDVVAVVNDTVG
TMMTCGFEDPHCEVGLIVGTGSNACYMEEMRNVELVEGEEGRMCVNMEWGAFGDNGCLDD
FRTEFDVAVDELSLNPGKQRFEKMISGMYLGEIVRNILIDFTKRGLLFRGRISERLKTRG
IFETKFLSQIESDCLALLQVRAILQHLGLESTCDDSIIVKEVCTVVARRAAQLCGAGMAA
VVDRIRENRGLDALKVTVGVDGTLYKLHPHFAKVMHETVKDLAPKCDVSFLQSEDGSGKG
AALITAVACRIREAGQR
Enzyme 3 Number of Residues 917
Enzyme 3 Molecular Weight 102381
Enzyme 3 Theoretical pI 5.93
Enzyme 3 GO Classification
Function
  • ATP binding
  • adenyl nucleotide binding
  • binding
  • catalytic activity
  • hexokinase activity
  • nucleotide binding
  • phosphotransferase activity, alcohol group as acceptor
  • purine nucleotide binding
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • alcohol metabolism
  • cellular metabolism
  • glucose catabolism
  • glucose metabolism
  • glycolysis
  • hexose metabolism
  • metabolism
  • monosaccharide metabolism
  • physiological process
Component
—
Enzyme 3 General Function Not Available
Enzyme 3 Specific Function ATP + D-hexose = ADP + D-hexose 6-phosphate
Enzyme 3 Pathways
Enzyme 3 Reactions
  • ATP + D-hexose = ADP + D-hexose 6-phosphate
Enzyme 3 Pfam Domain Function
Enzyme 3 Signals
  • None
Enzyme 3 Transmembrane Regions
  • None
Enzyme 3 Essentiality Not Available
Enzyme 3 GenBank ID Protein 587202 Link Image
Enzyme 3 UniProtKB/Swiss-Prot ID P52789 Link Image
Enzyme 3 UniProtKB/Swiss-Prot Entry Name HXK2_HUMAN Link Image
Enzyme 3 PDB ID Not Available
Enzyme 3 Cellular Location Not Available
Enzyme 3 Gene Sequence >2754 bp 
ATGATTGCCTCGCATCTGCTTGCCTACTTCTTCACGGAGCTCAACCATGACCAAGTGCAG
AAGGTTGACCAGTATCTCTACCACATGCGCCTCTCTGATGAGACCCTCTTGGAGATCTCT
AAGCGGTTCCGCAAGGAGATGGAGAAAGGGCTTGGAGCCACCACTCACCCTACTGCAGCA
GTGAAGATGCTGCCCACCTTTGTGAGGTCCACTCCAGATGGGACAGAACACGGAGAGTTC
CTGGCTCTGGATCTTGGAGGGACCAACTTCCGTGTGCTTTGGGTGAAAGTAACGGACAAT
GGGCTCCAGAAGGTGGAGATGGAGAATCAGATCTATGCCATCCCTGAGGACATCATGCGA
GGCAGTGGCACCCAGCTGTTTGACCACATTGCCGAATGCCTGGCTAACTTCATGGATAAG
CTACAAATCAAAGACAAGAAGCTCCCACTGGGTTTTACCTTCTCGTTCCCCTGCCACCAG
ACTAAACTAGACGAGAGTTTCCTGGTCTCATGGACCAAGGGATTCAAGTCCAGTGGAGTG
GAAGGCAGAGACGTTGTGGCTCTGATCCGGAAGGCCATCCAGAGGAGAGGGGACTTTGAT
ATCGACATTGTGGCTGTGGTGAATGACACAGTTGGGACCATGATGACCTGTGGTTATGAT
GACCACAACTGTGAGATTGGTCTCATTGTGGGCACGGGCAGCAACGCCTGCTACATGGAA
GAGATGCGCCACATCGACATGGTGGAAGGCGATGAGGGGCGGATGTGTATCAATATGGAG
TGGGGGGCCTTCGGGGACGATGGCTCGCTCAACGACATTCGCACTGAGTTTGACCAGGAG
ATTGACATGGGCTCACTGAACCCGGGAAAGCAACTGTTTGAGAAGATGATCAGTGGGATG
TACATGGGGGAGCTGGTGAGGCTTATCCTGGTGAAGATGGCCAAGGAGGAGCTGCTCTTT
GGGGGGAAGCTCAGCCCAGAGCTTCTCAACACCGGTCGCTTTGAGACCAAAGACATCTCA
GACATTGAAGGGGAGAAGGATGGCATCCGGAAGGCCCGTGAGGTCCTGATGCGGTTGGGC
CTGGACCCGACTCAGGAGGACTGCGTGGCCACTCACCGGATCTGCCAGATCGTGTCCACA
CGCTCCGCCAGCCTGTGCGCAGCCACCCTGGCCGCCGTGCTGCAGCGCATCAAGGAGAAC
AAAGGCGAGGAGCGGCTGCGCTCTACTATTGGGGTCGACGGTTCCGTCTACAAGAAACAC
CCCCATTTTGCCAAGCGTCTACATAAGACCGTGCGGCGGCTGGTGCCCGGCTGCGATGTC
CGCTTCCTCCGCTCCGAGGATGGCAGTGGCAAAGGTGCAGCCATGGTGACAGCAGTGGCT
TACCGGCTGGCCGATCAACACCGTGCCCGCCAGAAGACATTAGAGCATCTGCAGCTGAGC
CATGACCAGCTGCTGGAGGTCAAGAGGAGGATGAAGGTAGAAATGGAGCGAGGTCTGAGC
AAGGAGACTCATGCCAGTGCCCCCGTCAAGATGCTGCCCACCTACGTGTGTGCTACCCCG
GACGGCACAGAGAAAGGGGACTTCTTGGCCTTGGACCTTGGAGGAACAAATTTCCGGGTC
CTGCTGGTCCGTGTTCGGAATGGGAAGTGGGGTGGAGTGGAGATGCACAACAAGATCTAC
GCCATCCCGCAGGAGGTCATGCACGGCACCGGGGACGAGCTCTTTGACCACATTGTCCAG
TGCATCGCGGACTTCCTCGAGTACATGGGCATGAAGGGCGTGTCCCTGCCTCTGGGTTTT
ACCTTCTCCTTCCCCTGCCAGCAGAACAGCCTGGACGAGAGCATCCTCCTCAAGTGGACA
AAAGGCTTCAAGGCATCTGGCTGCGAGGGCGAGGACGTGGTGACCCTGCTGAAGGAAGCG
ATCCACCGGCGAGAGGAGTTTGACCTGGATGTGGTTGCTGTGGTGAACGACACAGTCGGA
ACTATGATGACCTGTGGCTTTGAAGACCCTCACTGTGAAGTTGGCCTCATTGTTGGCACG
GGCAGCAATGCCTGCTACATGGAGGAGATGCGCAACGTGGAACTGGTGGAAGGAGAAGAG
GGGCGGATGTGTGTGAACATGGAATGGGGGGCCTTCGGGGACAATGGATGCCTAGATGAC
TTCCGCACAGAATTTGATGTGGCTGTGGATGAGCTTTCACTCAACCCCGGCAAGCAGAGG
TTCGAGAAAATGATCAGTGGAATGTACCTGGGTGAGATTGTCCGTAACATTCTCATCGAT
TTCACCAAGCGTGGACTACTCTTCCGAGGCCGCATCTCAGAGCGGCTCAAGACAAGGGGC
ATCTTTGAAACCAAGTTCTTGTCTCAGATTGAGAGTGACTGCCTGGCCCTGCTGCAAGTC
CGAGCCACCCTGCAACACTTAGGGCTTGAGAGCACCTGTGACGACAGCATCATTGTTAAG
GAGGTGTGCACTGTGGTGGCCCGGCGGGCAGCCCAGCTCTGTGGCGCAGGCATGGCCGCT
GTGGTGGACAGGATACGAGAAAACCGTGGGCTGGACGCTCTCAAAGTGACAGTGGGTGTG
GATGGGACCCTCTACAAGCTACATCCTCACTTTGCCAAAGTCATGCATGAGACAGTGAAG
GACCTGGCTCCGAAATGTGATGTGTCTTTCCTGCAGTCAGAGGATGGCAGCGGGAAGGGG
GCGGCGCTCATCACTGCTGTGGCCTGCCGCATCCGTGAGGCTGGACAGCGATAG
Enzyme 3 GenBank Gene ID Z46376 Link Image
Enzyme 3 GeneCard ID HK2 Link Image
Enzyme 3 GenAtlas ID HK2 Link Image
Enzyme 3 HGNC ID HGNC:4923 Link Image
Enzyme 3 Chromosome Location 2
Enzyme 3 Locus 2p13
Enzyme 3 SNPs SNPJam Report Link Image
Enzyme 3 General References
  1. Lehto M, Huang X, Davis EM, Le Beau MM, Laurila E, Eriksson KF, Bell GI, Groop L: Human hexokinase II gene: exon-intron organization, mutation screening in NIDDM, and its relationship to muscle hexokinase activity. Diabetologia. 1995 Dec;38(12):1466-74. [PubMed Link Image]
  2. Deeb SS, Malkki M, Laakso M: Human hexokinase II: sequence and homology to other hexokinases. Biochem Biophys Res Commun. 1993 Nov 30;197(1):68-74. [PubMed Link Image]
  3. Shinohara Y, Yamamoto K, Kogure K, Ichihara J, Terada H: Steady state transcript levels of the type II hexokinase and type 1 glucose transporter in human tumor cell lines. Cancer Lett. 1994 Jul 15;82(1):27-32. [PubMed Link Image]
  4. Laakso M, Malkki M, Deeb SS: Amino acid substitutions in hexokinase II among patients with NIDDM. Diabetes. 1995 Mar;44(3):330-4. [PubMed Link Image]
  5. Vidal-Puig A, Printz RL, Stratton IM, Granner DK, Moller DE: Analysis of the hexokinase II gene in subjects with insulin resistance and NIDDM and detection of a Gln142-->His substitution. Diabetes. 1995 Mar;44(3):340-6. [PubMed Link Image]
  6. Echwald SM, Bjorbaek C, Hansen T, Clausen JO, Vestergaard H, Zierath JR, Printz RL, Granner DK, Pedersen O: Identification of four amino acid substitutions in hexokinase II and studies of relationships to NIDDM, glucose effectiveness, and insulin sensitivity. Diabetes. 1995 Mar;44(3):347-53. [PubMed Link Image]
Enzyme 3 Metabolite References Not Available
Enzyme 4 [top]
Enzyme 4 ID 5447
Enzyme 4 Name Hexokinase-1
Enzyme 4 Synonyms
  1. Hexokinase type I
  2. HK I
  3. Brain form hexokinase
Enzyme 4 Gene Name HK1
Enzyme 4 Protein Sequence >Hexokinase-1 
MIAAQLLAYYFTELKDDQVKKIDKYLYAMRLSDETLIDIMTRFRKEMKNGLSRDFNPTAT
VKMLPTFVRSIPDGSEKGDFIALDLGGSSFRILRVQVNHEKNQNVHMESEVYDTPENIVH
GSGSQLFDHVAECLGDFMEKRKIKDKKLPVGFTFSFPCQQSKIDEAILITWTKRFKASGV
EGADVVKLLNKAIKKRGDYDANIVAVVNDTVGTMMTCGYDDQHCEVGLIIGTGTNACYME
ELRHIDLVEGDEGRMCINTEWGAFGDDGSLEDIRTEFDREIDRGSLNPGKQLFEKMVSGM
YLGELVRLILVKMAKEGLLFEGRITPELLTRGKFNTSDVSAIEKNKEGLHNAKEILTRLG
VEPSDDDCVSVQHVCTIVSFRSANLVAATLGAILNRLRDNKGTPRLRTTVGVDGSLYKTH
PQYSRRFHKTLRRLVPDSDVRFLLSESGSGKGAAMVTAVAYRLAEQHRQIEETLAHFHLT
KDMLLEVKKRMRAEMELGLRKQTHNNAVVKMLPSFVRRTPDGTENGDFLALDLGGTNFRV
LLVKIRSGKKRTVEMHNKIYAIPIEIMQGTGEELFDHIVSCISDFLDYMGIKGPRMPLGF
TFSFPCQQTSLDAGILITWTKGFKATDCVGHDVVTLLRDAIKRREEFDLDVVAVVNDTVG
TMMTCAYEEPTCEVGLIVGTGSNACYMEEMKNVEMVEGDQGQMCINMEWGAFGDNGCLDD
IRTHYDRLVDEYSLNAGKQRYEKMISGMYLGEIVRNILIDFTKKGFLFRGQISETLKTRG
IFETKFLSQIESDRLALLQVRAILQQLGLNSTCDDSILVKTVCGVVSRRAAQLCGAGMAA
VVDKIRENRGLDRLNVTVGVDGTLYKLHPHFSRIMHQTVKELSPKCNVSFLLSEDGSGKG
AALITAVGVRLRTEASS
Enzyme 4 Number of Residues 917
Enzyme 4 Molecular Weight 102487
Enzyme 4 Theoretical pI 6.78
Enzyme 4 GO Classification
Function
  • ATP binding
  • adenyl nucleotide binding
  • binding
  • catalytic activity
  • hexokinase activity
  • nucleotide binding
  • phosphotransferase activity, alcohol group as acceptor
  • purine nucleotide binding
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • alcohol metabolism
  • cellular metabolism
  • glucose catabolism
  • glucose metabolism
  • glycolysis
  • hexose metabolism
  • metabolism
  • monosaccharide metabolism
  • physiological process
Component
—
Enzyme 4 General Function Not Available
Enzyme 4 Specific Function ATP + D-hexose = ADP + D-hexose 6-phosphate
Enzyme 4 Pathways
Enzyme 4 Reactions
  • ATP + D-hexose = ADP + D-hexose 6-phosphate
Enzyme 4 Pfam Domain Function
Enzyme 4 Signals
  • None
Enzyme 4 Transmembrane Regions
  • None
Enzyme 4 Essentiality Not Available
Enzyme 4 GenBank ID Protein 184021 Link Image
Enzyme 4 UniProtKB/Swiss-Prot ID P19367 Link Image
Enzyme 4 UniProtKB/Swiss-Prot Entry Name HXK1_HUMAN Link Image
Enzyme 4 PDB ID 1HKB Link Image
Enzyme 4 PDB File Show
Enzyme 4 3D Structure
Enzyme 4 Cellular Location Not Available
Enzyme 4 Gene Sequence >2754 bp 
ATGATCGCCGCGCAGCTCCTGGCCTATTACTTCACGGAGCTGAAGGATGACCAGGTCAAA
AAGATTGACAAGTATCTGTATGCCATGCGGCTCTCCGATGAAACTCTCATAGATATCATG
ACTCGCTTCAGGAAGGAGATGAAGAATGGCCTCTCCCGGGATTTTAATCCAACAGCCACA
GTCAAGATGTTGCCAACATTCGTAAGGTCCATTCCTGATGGCTCTGAAAAGGGAGATTTC
ATTGCCCTGGATCTTGGTGGGTCTTCCTTTCGAATTCTGCGGGTGCAAGTGAATCATGAG
AAAAACCAGAATGTTCACATGGAGTCCGAGGTTTATGACACCCCAGAGAACATCGTGCAC
GGCAGTGGAAGCCAGCTTTTTGATCATGTTGCTGAGTGCCTGGGAGATTTCATGGAGAAA
AGGAAGATCAAGGACAAGAAGTTACCTGTGGGATTCACGTTTTCTTTTCCTTGCCAACAA
TCCAAAATAGATGAGGCCATCCTGATCACCTGGACAAAGCGATTTAAAGCGAGCGGAGTG
GAAGGAGCAGATGTGGTCAAACTGCTTAACAAAGCCATCAAAAAGCGAGGGGACTATGAT
GCCAACATCGTAGCTGTGGTGAATGACACAGTGGGCACCATGATGACCTGTGGCTATGAC
GACCAGCACTGTGAAGTCGGCCTGATCATCGGCACTGGCACCAATGCTTGCTACATGGAG
GAACTGAGGCACATTGATCTGGTGGAAGGAGACGAGGGGAGGATGTGTATCAATACAGAA
TGGGGAGCCTTTGGAGACGATGGATCATTAGAAGACATCCGGACAGAGTTTGACAGGGAG
ATAGACCGGGGATCCCTCAACCCTGGAAAACAGCTGTTTGAGAAGATGGTCAGTGGCATG
TACTTGGGAGAGCTGGTTCGACTGATCCTAGTCAAGATGGCCAAGGAGGGCCTCTTATTT
GAAGGGCGGATCACCCCGGAGCTGCTCACCCGAGGGAAGTTTAACACCAGTGATGTGTCA
GCCATCGAAAAGAATAAGGAAGGCCTCCACAATGCCAAAGAAATCCTGACCCGCCTGGGA
GTGGAGCCGTCCGATGATGACTGTGTCTCAGTCCAGCACGTTTGCACCATTGTCTCATTT
CGCTCAGCCAACTTGGTGGCTGCCACACTGGGCGCCATCTTGAACCGCCTGCGTGATAAC
AAGGGCACACCCAGGCTGCGGACCACGGTTGGTGTCGACGGATCTCTTTACAAGACGCAC
CCACAGTATTCCCGGCGTTTCCACAAGACTCTAAGGCGCTTGGTGCCAGACTCCGATGTG
CGCTTCCTCCTCTCGGAGAGTGGCAGCGGCAAGGGGGCTGCCATGGTGACGGCGGTGGCC
TACCGCTTGGCCGAGCAGCACCGGCAGATAGAGGAGACCCTGGCTCATTTCCACCTCACC
AAAGACATGCTGCTGGAGGTGAAGAAGAGGATGCGGGCCGAGATGGAGCTGGGGCTGAGG
AAGCAGACGCACAACAATGCCGTGGTTAAGATGCTGCCCTCCTTCGTCCGGAGAACTCCC
GACGGGACCGAGAATGGTGACTTCTTGGCCCTGGATCTTGGAGGAACCAATTTCCGTGTG
CTGCTGGTGAAAATCCGTAGTGGGAAAAAGAGAACGGTGGAAATGCACAACAAGATCTAC
GCCATTCCTATTGAAATCATGCAGGGCACTGGGGAAGAGCTGTTTGATCACATTGTCTCC
TGCATCTCTGACTTCTTGGACTACATGGGGATCAAAGGCCCCAGGATGCCTCTGGGCTTC
ACGTTCTCATTTCCCTGCCAGCAGACGAGTCTGGACGCGGGAATCTTGATCACGTGGACA
AAGGGTTTTAAGGCAACAGACTGCGTGGGCCACGATGTAGTCACCTTACTAAGGGATGCG
ATAAAAAGGAGAGAGGAATTTGACCTGGACGTGGTGGCTGTGGTCAACGACACAGTGGGC
ACCATGATGACCTGTGCTTATGAGGAGCCCACCTGTGAGGTTGGACTCATTGTTGGGACC
GGCAGCAATGCCTGCTACATGGAGGAGATGAAGAACGTGGAGATGGTGGAGGGGGACCAG
GGGCAGATGTGCATCAACATGGAGTGGGGGGCCTTTGGGGACAACGGGTGTCTGGATGAT
ATCAGGACACACTACGACAGACTGGTGAACGAATATTCCCTAAATGCTGGGAAACAAAGG
TATGAGAAGATGATCAGTGGTATGTACCTGGGTGAAATCGTCCGCAACATCTTAATCGAC
TTCACCAAGAAGGGATTCCTCTTCCGAGGGCAGATCTCTGAGACGATGAAGACCCGGGGC
ATCTTTGAGACCAAGTTTCTCTCTCAGATCGAGAGTGACCGATTAGCACTGCTCCAGGTC
CGGGCTATCCTCCAGCAGCTAGGTCTGAATAGCACCTGCGATGACAGTATCCTCGTCAAG
ACAGTGTGCGGGGTGGTGTCCAGGAGGGCCGCACAGCTGTGTGGCGCAGGCATGGCTGCG
GTTGTGGATAAGATCCGCGAGAACAGAGGACTGGACCGTCTGAATGTGACTGTGGGAGTG
GACGGGACACTCTACAAGCTTCATCCACACTTCTCCAGAATCATGCACCAGACGGTGAAG
GAACTGTCACCAAAATGTAACGTGTCCTTCCTCCTGTCTGAGGATGGCAGCGGCAAGGGG
GCCGCCCTCATCACGGCCGTGGGCGTGCGGTTACGCACAGAGGCAAGCAGCTAA
Enzyme 4 GenBank Gene ID M75126 Link Image
Enzyme 4 GeneCard ID HK1 Link Image
Enzyme 4 GenAtlas ID HK1 Link Image
Enzyme 4 HGNC ID HGNC:4922 Link Image
Enzyme 4 Chromosome Location 10
Enzyme 4 Locus 10q22
Enzyme 4 SNPs SNPJam Report Link Image
Enzyme 4 General References
  1. Nishi S, Seino S, Bell GI: Human hexokinase: sequences of amino- and carboxyl-terminal halves are homologous. Biochem Biophys Res Commun. 1988 Dec 30;157(3):937-43. [PubMed Link Image]
  2. Ruzzo A, Andreoni F, Magnani M: Structure of the human hexokinase type I gene and nucleotide sequence of the 5' flanking region. Biochem J. 1998 Apr 15;331 ( Pt 2):607-13. [PubMed Link Image]
  3. Magnani M, Bianchi M, Casabianca A, Stocchi V, Daniele A, Altruda F, Ferrone M, Silengo L: A recombinant human 'mini'-hexokinase is catalytically active and regulated by hexose 6-phosphates. Biochem J. 1992 Jul 1;285 ( Pt 1):193-9. [PubMed Link Image]
  4. Magnani M, Serafini G, Bianchi M, Casabianca A, Stocchi V: Human hexokinase type I microheterogeneity is due to different amino-terminal sequences. J Biol Chem. 1991 Jan 5;266(1):502-5. [PubMed Link Image]
  5. Murakami K, Piomelli S: Identification of the cDNA for human red blood cell-specific hexokinase isozyme. Blood. 1997 Feb 1;89(3):762-6. [PubMed Link Image]
  6. Andreoni F, Ruzzo A, Magnani M: Structure of the 5' region of the human hexokinase type I (HKI) gene and identification of an additional testis-specific HKI mRNA. Biochim Biophys Acta. 2000 Sep 7;1493(1-2):19-26. [PubMed Link Image]
  7. Aleshin AE, Zeng C, Fromm HJ, Honzatko RB: Crystallization and preliminary X-ray analysis of human brain hexokinase. FEBS Lett. 1996 Aug 5;391(1-2):9-10. [PubMed Link Image]
  8. Aleshin AE, Zeng C, Bourenkov GP, Bartunik HD, Fromm HJ, Honzatko RB: The mechanism of regulation of hexokinase: new insights from the crystal structure of recombinant human brain hexokinase complexed with glucose and glucose-6-phosphate. Structure. 1998 Jan 15;6(1):39-50. [PubMed Link Image]
  9. Aleshin AE, Zeng C, Bartunik HD, Fromm HJ, Honzatko RB: Regulation of hexokinase I: crystal structure of recombinant human brain hexokinase complexed with glucose and phosphate. J Mol Biol. 1998 Sep 18;282(2):345-57. [PubMed Link Image]
  10. Rosano C, Sabini E, Rizzi M, Deriu D, Murshudov G, Bianchi M, Serafini G, Magnani M, Bolognesi M: Binding of non-catalytic ATP to human hexokinase I highlights the structural components for enzyme-membrane association control. Structure. 1999 Nov 15;7(11):1427-37. [PubMed Link Image]
  11. Aleshin AE, Kirby C, Liu X, Bourenkov GP, Bartunik HD, Fromm HJ, Honzatko RB: Crystal structures of mutant monomeric hexokinase I reveal multiple ADP binding sites and conformational changes relevant to allosteric regulation. J Mol Biol. 2000 Mar 3;296(4):1001-15. [PubMed Link Image]
  12. Bianchi M, Magnani M: Hexokinase mutations that produce nonspherocytic hemolytic anemia. Blood Cells Mol Dis. 1995;21(1):2-8. [PubMed Link Image]
Enzyme 4 Metabolite References Not Available
Enzyme 5 [top]
Enzyme 5 ID 5565
Enzyme 5 Name GDH/6PGL endoplasmic bifunctional protein precursor [Includes: Glucose 1-dehydrogenase
Enzyme 5 Synonyms
  1. Hexose-6-phosphate dehydrogenase
  2. 6- phosphogluconolactonase
  3. 6PGL]
Enzyme 5 Gene Name H6PD
Enzyme 5 Protein Sequence >GDH/6PGL endoplasmic bifunctional protein precursor [Includes: Glucose 1-dehydrogenase 
MWNMLIVAMCLALLGCLQAQELQGHVSIILLGATGDLAKKYLWQGLFQLYLDEAGRGHSF
SFHGAALTAPKQGQELMAKALESLSCPKDMAPSHCAEHKDQFLQLSQYRQLKTAEDYQAL
NKDIEAQLQHAGLREAGRIFYFSVPPFAYEDIARNINSSCRPGPGAWLRVVLEKPFGHDH
FSAQQLATELGTFFQEEEMYRVDHYLGKQAVAQILPFRDQNRKALDGLWNRHHVERVEII
MKETVDAEGRTSFYEEYGVIRDVLQNHLTEVLTLVAMELPHNVSSAEAVLRHKLQVFQAL
RGLQRGSAVVGQYQSYSEQVRRELQKPDSFHSLTPTFAAVLVHIDNLRWEGVPFILMSGK
ALDERVGYARILFKNQACCVQSEKHWAAAQSQCLPRQLVFHIGHGDLGSPAVLVSRNLFR
PSLPSSWKEMEGPPGLRLFGSPLSDYYAYSPVRERDAHSVLLSHIFHGRKNFFITTENLL
ASWNFWTPLLESLAHKAPRLYPGGAENGRLLDFEFSSGRLFFSQQQPEQLVPGPGPAPMP
SDFQVLRAKYRESPLVSAWSEELISKLANDIEATAVRAVRRFGQFHLALSGGSSPVALFQ
QLATAHYGFPWAHTHLWLVDERCVPLSDPESNFQGLQAHLLQHVRIPYYNIHPMPVHLQQ
RLCAEEDQGAQIYAREISALVANSSFDLVLLGMGADGHTASLFPQSPTGLDGEQLVVLTT
SPSQPHRRMSLSLPLINRAKKVAVLVMGRMKREITTLVSRVGHEPKKWPISGVLPHSGQL
VWYMDYDAFLG
Enzyme 5 Number of Residues 791
Enzyme 5 Molecular Weight 88894
Enzyme 5 Theoretical pI 7.31
Enzyme 5 GO Classification
Function
  • 6-phosphogluconolactonase activity
  • carboxylic ester hydrolase activity
  • catalytic activity
  • glucose-6-phosphate 1-dehydrogenase activity
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • oxidoreductase activity
  • oxidoreductase activity, acting on CH-OH group of donors
  • oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
Process
  • alcohol metabolism
  • carbohydrate metabolism
  • cellular metabolism
  • glucose catabolism
  • glucose metabolism
  • hexose metabolism
  • macromolecule metabolism
  • metabolism
  • monosaccharide metabolism
  • pentose-phosphate shunt
  • physiological process
Component
—
Enzyme 5 General Function Carbohydrate transport and metabolism
Enzyme 5 Specific Function Oxidizes glucose-6-phosphate and glucose, as well as other hexose-6-phosphates
Enzyme 5 Pathways
Enzyme 5 Reactions
  • 6-phospho-D-glucono-1,5-lactone + H2O = 6-phospho-D-gluconate
Enzyme 5 Pfam Domain Function
Enzyme 5 Signals
  • 1-19
Enzyme 5 Transmembrane Regions Not Available
Enzyme 5 Essentiality Not Available
Enzyme 5 GenBank ID Protein 4186038 Link Image
Enzyme 5 UniProtKB/Swiss-Prot ID O95479 Link Image
Enzyme 5 UniProtKB/Swiss-Prot Entry Name G6PE_HUMAN Link Image
Enzyme 5 PDB ID Not Available
Enzyme 5 Cellular Location Not Available
Enzyme 5 Gene Sequence >2376 bp 
ATGTGGAATATGCTCATAGTGGCGATGTGCTTGGCCCTTCTGGGCTGCCTGCAAGCCCAG
GAGCTCCAGGGACATGTCTCCATAATCCTGCTGGGAGCAACTGGGGACCTGGCTAAGAAG
TACTTATGGCAGGGACTGTTCCAGCTGTACCTGGATGAAGCGGGGAGGGGTCACAGTTTT
AGCTTCCATGGAGCTGCTCTGACAGCCCCCAAGCAGGGTCAAGAGCTCATGGCCAAGGCC
CTGGAATCCCTCTCCTGCCCCAAGGACATGGCACCCAGTCACTGTGCAGAGCACAAGGAT
CAGTTCCTGCAGCTGAGCCAGTACCGCCAACTGAAGACGGCCGAGGACTATCAGGCCCTG
AACAAGGACATCGAGGCACAGCTCCAGCACGCAGGCCTCCGGGAGGCTGGCAGGATCTTC
TACTTCTCAGTGCCACCCTTCGCCTATGAAGACATTGCCCGCAACATCAACAGTAGCTGC
CGGCCAGGCCCGGGCGCCTGGCTGCGGGTTGTCCTTGAGAAACCCTTTGGCCATGACCAC
TTCTCAGCCCAGCAGCTGGCCACAGAACTCGGGACCTTTTTCCAGGAGGAGGAGATGTAC
CGGGTGGACCATTACTTAGGCAAGCAGGCTGTGGCGCAGATCCTGCCTTTCCGAGACCAG
AACCGCAAGGCTTTGGACGGCCTCTGGAACCGGCACCATGTGGAGCGGGTGGAGATCATC
ATGAAAGAGACCGTGGATGCTGAAGGCCGCACCAGCTTCTATGAGGAGTACGGTGTCATT
CGCGACGTCCTCCAGAACCATCTGACGGAGGTCCTCACCCTCGTGGCCATGGAGCTGCCC
CACAATGTCAGCAGTGCGGAGGCTGTGCTGCGGCACAAGCTTCAGGTCTTCCAGGCGCTG
CGGGGCCTGCAGAGGGGCAGTGCCGTCGTGGGCCAGTACCAGTCTTACAGTGAGCAGGTG
CGCAGAGAGCTGCAGAAGCCAGACAGCTTCCACAGCCTGACGCCGACCTTCGCAGGTGTC
CTAGTGCACATTGACAACCTTCGCTGGGAGGGCGTGCCTTTCATCCTGATGTCTGGCAAA
GCCTTGGACGAGAGAGTGGGCTACGCTCGGATCTTGTTCAAGAACCAGGCCTGCTGTGTG
CAGAGCGAAAAGCACTGGGCCGCGGCGCAGAGCCAGTGCCTGCCCCGGCAGCTCGTCTTC
CACATCGGCCATGGCGACCTGGGCAGCCCTGCCGTGCTGGTCAGCAGGAACCTGTTCAGG
CCCTCCCTGCCCTCCAGCTGGAAGGAAATGGAGGGACCACCTGGGCTCCGCCTTTTCGGC
AGCCCTCTGTCCGATTACTACGCCTACAGCCCTGTGCGGGAGCGGGACGCCCACTCCGTC
CTCTTATCCCATATCTTCCATGGCCGGAAGAATTTCTTCATCACCACAGAGAACTTGCTG
GCCTCCTGGAACTTCTGGACCCCTCTGCTGGAGAGCCTGGCCCATAAGGCCCCACGCCTC
TACCCTGGAGGAGCTGAGAATGGCCGTCTGTTGGACTTTGAGTTCAGTAGCGGCCGGTTG
TTCTTTTCCCAGCAGCAGCCGGAGCAGCTGGTGCCAGGGCCAGGGCCGGCCCCAATGCCC
AGTGACTTCCAGGTCCTCAGGGCCAAGTACCGAGAGAGCCCGCTGGTCTCCGCCTGGTCC
GAGGAGCTGATCTCTAAGCTGGCTAATGACATCGAGGCCACCGCTGTGCGAGCCGTGCGG
CGCTTTGGCCAGTTCCACCTGGCACTGTCGGGGGGCTCGAGCCCCGTGGCCCTGTTCCAG
CAGCTGGCCACGGCGCACTATGGCTTCCCCTGGGCCCACACGCACCTGTGGCTGGTTGAC
GAGCGCTGCGTCCCACTCTCAGACCCGGAGTCCAACTTCCAGGGCCTGCAGGCCCACCTG
CTGCAGCACGTCCGGATCCCCTACTACAACATCCACCCCATGCCTGTGCACCTGCAGCAG
CGGCTCTGCGCCGAGGAGGACCAGGGCGCCCAGATCTATGCCAGGGAGATCTCAGCCCTG
GTGGCCAACAGCAGCTTCGACCTGGTGCTGCTGGGCATGGGTGCCGACGGGCACACAGCC
TCCCTCTTCCCACAGTCACCCACTGGCCTGGATGGCGAGCAGCTGGTCGTGCTGACCACG
AGCCCCTCCCAGCCACACCGCCGCATGAGCCTTAGCCTGCCTCTCATCAACCGCGCCAAG
AAGGTGGCAGTCCTGGTCATGGGCAGGATGAAGCGTGAGATCACCACGCTGGTGAGCCGG
GTGGGCCATGAGCCCAAGAAGTGGCCCATCTCGGGTGTCCTGCCGCACTCCGGCCAGCTG
GTGTGGTACATGGACTACGACGCCTTCCTGGGATGA
Enzyme 5 GenBank Gene ID AJ012590 Link Image
Enzyme 5 GeneCard ID H6PD Link Image
Enzyme 5 GenAtlas ID H6PD Link Image
Enzyme 5 HGNC ID HGNC:4795 Link Image
Enzyme 5 Chromosome Location 1
Enzyme 5 Locus 1p36
Enzyme 5 SNPs SNPJam Report Link Image
Enzyme 5 General References
  1. Mason PJ, Stevens D, Diez A, Knight SW, Scopes DA, Vulliamy TJ: Human hexose-6-phosphate dehydrogenase (glucose 1-dehydrogenase) encoded at 1p36: coding sequence and expression. Blood Cells Mol Dis. 1999 Feb;25(1):30-7. [PubMed Link Image]
Enzyme 5 Metabolite References Not Available
Enzyme 6 [top]
Enzyme 6 ID 5601
Enzyme 6 Name Lactase-phlorizin hydrolase precursor
Enzyme 6 Synonyms
  1. Lactase-glycosylceramidase[Includes: Lactase
Enzyme 6 Gene Name LCT
Enzyme 6 Protein Sequence >Lactase-phlorizin hydrolase precursor 
MELSWHVVFIALLSFSCWGSDWESDRNFISTAGPLTNDLLHNLSGLLGDQSSNFVAGDKD
MYVCHQPLPTFLPEYFSSLHASQITHYKVFLSWAQLLPAGSTQNPDEKTVQCYRRLLKAL
KTARLQPMVILHHQTLPASTLRRTEAFADLFADYATFAFHSFGDLVGIWFTFSDLEEVIK
ELPHQESRASQLQTLSDAHRKAYEIYHESYAFQGGKLSVVLRAEDIPELLLEPPISALAQ
DTVDFLSLDLSYECQNEASLRQKLSKLQTIEPKVKVFIFNLKLPDCPSTMKNPASLLFSL
FEAINKDQVLTIGFDINEFLSCSSSSKKSMSCSLTGSLALQPDQQQDHETTDSSPASAYQ
RVWEAFANQSRAERDAFLQDTFPEGFLWGASTGAFNVEGGWAEGGRGVSIWDPRRPLNTT
EGQATLEVASDSYHKVASDVALLCGLRAQVYKFSISWSRIFPMGHGSSPSLPGVAYYNKL
IDRLQDAGIEPMATLFHWDLPQALQDHGGWQNESVVDAFLDYAAFCFSTFGDRVKLWVTF
HEPWVMSYAGYGTGQHPPGISDPGVASFKVAHLVLKAHARTWHHYNSHHRPQQQGHVGIV
LNSDWAEPLSPERPEDLRASERFLHFMLGWFAHPVFVDGDYPATLRTQIQQMNRQCSHPV
AQLPEFTEAEKQLLKGSADFLGLSHYTSRLISNAPQNTCIPSYDTIGGFSQHVNHVWPQT
SSSWIRVVPWGIRRLLQFVSLEYTRGKVPIYLAGNGMPIGESENLFDDSLRVDYFNQYIN
EVLKAIKEDSVDVRSYIARSLIDGFEGPSGYSQRFGLHHVNFSDSSKSRTPRKSAYFFTS
IIEKNGFLTKGAKRLLPPNTVNLPSKVRAFTFPSEVPSKAKVVWEKFSSQPKFERDLFYH
GTFRDDFLWGVSSSAYQIEGAWDADGKGPSIWDNFTHTPGSNVKDNATGDIACDSYHQLD
ADLNMLRALKVKAYRFSISWSRIFPTGRNSSINSHGVDYYNRLINGLVASNIFPMVTLFH
WDLPQALQDIGGWENPALIDLFDSYADFCFQTFGDRVKFWMTFNEPMYLAWLGYGSGEFP
PGVKDPGWAPYRIAHTVIKAHARVYHTYDEKYRQEQKGVISLSLSTHWAEPKSPGVPRDV
EAADRMLQFSLGWFAHPIFRNGDYPDTMKWKVGNRSELQHLATSRLPSFTEEEKRFIRAT
ADVFCLNTYYSRIVQHKTPRLNPPSYEDDQEMAEEEDPSWPSTAMNRAAPWGTRRLLNWI
KEEYGDIPIYITENGVGLTNPNTEDTDRIFYHKTYINEALKAYRLDGIDLRGYVAWSLMD
NFEWLNGYTVKFGLYHVDFNNTNRPRTARASARYYTEVITNNGMPLAREDEFLYGRFPEG
FIWSAASAAYQIEGAWRADGKGLSIWDTFSHTPLRVENDAIGDVACDSYHKIAEDLVTLQ
NLGVSHYRFSISWSRILPDGTTRYINEAGLNYYVRLIDTLLAASIQPQVTIYHWDLPQTL
QDVGGWENETIVQRFKEYADVLFQRLGDKVKFWITLNEPFVIAYQGYGYGTAAPGVSNRP
GTAPYIVGHNLIKAHAEAWHLYNDVYRASQGGVISITISSDWAEPRDPSNQEDVEAARRY
VQFMGGWFAHPIFKNGDYNEVMKTRIRDRSLAAGLNKSRLPEFTESEKRRINGTYDFFGF
NHYTTVLAYNLNYATAISSFDADRGVASIADRSWPDSGSFWLKMTPFGFRRILNWLKEEY
NDPPIYVTENGVSQREETDLNDTARIYYLRTYINEALKAVQDKVDLRGYTVWSAMDNFEW
ATGFSERFGLHFVNYSDPSLPRIPKASAKFYASVVRCNGFPDPATGPHACLHQPDAGPTI
SPVRQEEVQFLGLMLGTTEAQTALYVLFSLVLLGVCGLAFLSYKYCKRSKQGKTQRSQQE
LSPVSSF
Enzyme 6 Number of Residues 1927
Enzyme 6 Molecular Weight 218604
Enzyme 6 Theoretical pI 6.30
Enzyme 6 GO Classification
Function
  • catalytic activity
  • glucosidase activity
  • hydrolase activity
  • hydrolase activity, acting on glycosyl bonds
  • hydrolase activity, hydrolyzing O-glycosyl compounds
Process
  • carbohydrate metabolism
  • macromolecule metabolism
  • metabolism
  • physiological process
Component
—
Enzyme 6 General Function Carbohydrate transport and metabolism
Enzyme 6 Specific Function LPH splits lactose in the small intestine
Enzyme 6 Pathways
Enzyme 6 Reactions
  • lactose + H2O = D-galactose + D-glucose
Enzyme 6 Pfam Domain Function
Enzyme 6 Signals
  • 1-19
Enzyme 6 Transmembrane Regions
  • 1883-1901
Enzyme 6 Essentiality Not Available
Enzyme 6 GenBank ID Protein 34400 Link Image
Enzyme 6 UniProtKB/Swiss-Prot ID P09848 Link Image
Enzyme 6 UniProtKB/Swiss-Prot Entry Name LPH_HUMAN Link Image
Enzyme 6 PDB ID Not Available
Enzyme 6 Cellular Location Not Available
Enzyme 6 Gene Sequence >5784 bp 
ATGGAGCTGTCTTGGCATGTAGTCTTTATTGCCCTGCTAAGTTTTTCATGCTGGGGGTCA
GACTGGGAGTCTGATAGAAATTTCATTTCCACCGCTGGTCCTCTAACCAATGACTTGCTG
CACAACCTGAGTGGTCTCCTGGGAGACCAGAGTTCTAACTTTGTAGCAGGGGACAAAGAC
ATGTATGTTTGTCACCAGCCACTGCCCACTTTCCTGCCAGAATACTTCAGCAGTCTCCAT
GCCAGTCAGATCACCCATTATAAGGTATTTCTGTCATGGGCACAGCTCCTCCCAGCAGGA
AGCACCCAGAATCCAGACGAGAAAACAGTGCAGTGCTACCGGCGACTCCTCAAGGCCCTC
AAGACTGCACGGCTTCAGCCCATGGTCATCCTGCACCACCAGACCCTCCCTGCCAGCACC
CTCCGGAGAACCGAAGCCTTTGCTGACCTCTTCGCCGACTATGCCACATTCGCCTTCCAC
TCCTTCGGGGACCTAGTTGGGATCTGGTTCACCTTCAGTGACTTGGAGGAAGTGATCAAG
GAGCTTCCCCACCAGGAATCAAGAGCGTCACAACTCCAGACCCTCAGTGATGCCCACAGA
AAAGCCTATGAGATTTACCACGAAAGCTATGCTTTTCAGGGCGGAAAACTCTCTGTTGTC
CTGCGAGCTGAAGATATCCCGGAGCTCCTGCTAGAACCACCCATATCTGCGCTTGCCCAG
GACACGGTCGATTTCCTCTCTCTTGATTTGTCTTATGAATGCCAAAATGAGGCAAGTCTG
CGGCAGAAGCTGAGTAAATTGCAGACCATTGAGCCAAAAGTGAAAGTTTTCATCTTCAAC
CTAAAACTCCCAGACTGCCCCTCCACCATGAAGAACCCAGCCAGTCTGCTCTTCAGCCTT
TTTGAAGCCATAAATAAAGACCAAGTGCTCACCATTGGGTTTGATATTAATGAGTTTCTG
AGTTGTTCATCAAGTTCCAAGAAAAGCATGTCTTGTTCTCTGACTGGCAGCCTGGCCCTT
CAGCCTGACCAGCAGCAGGACCACGAGACCACGGACTCCTCTCCTGCCTCTGCCTATCAG
AGAGTCTGGGAAGCATTTGCCAATCAGTCCAGAGCGGAAAGGGATGCCTTCCTGCAGGAT
ACTTTCCCTGAAGGCTTCCTCTGGGGTGCCTCCACAGGAGCCTTTAACGTGGAAGGAGGC
TGGGCCGAGGGTGGGAGAGGGGTGAGCATCTGGGATCCACGCAGGCCCCTGAACACCACT
GAGGGCCAAGCGACGCTGGAGGTGGCCAGCGACAGTTACCACAAGGTAGCCTCTGACGTC
GCCCTGCTTTGCGGCCTCCGGGCTCAGGTGTACAAGTTCTCCATCTCCTGGTCCCGGATC
TTCCCCATGGGGCACGGGAGCAGCCCCAGCCTCCCAGGCGTTGCCTACTACAACAAGCTG
ATTGACAGGCTACAGGATGCGGGCATCGAGCCCATGGCCACGCTGTTCCACTGGGACCTG
CCTCAGGCCCTGCAGGATCATGGTGGATGGCAGAATGAGAGCGTGGTGGATGCCTTCCTG
GACTATGCGGCCTTCTGCTTCTCCACATTTGGGGACCGTGTGAAGCTGTGGGTGACCTTC
CATGAGCCGTGGGTGATGAGCTACGCAGGCTATGGCACCGGCCAGCACCCTCCCGGCATC
TCTGACCCAGGAGTGGCCTCTTTTAAGGTGGCTCACTTGGTCCTCAAGGCTCATGCCAGA
ACTTGGCACCACTACAACAGCCATCATCGCCCACAGCAGCAGGGGCACGTGGGCATTGTG
CTGAACTCAGACTGGGCAGAACCCCTGTCTCCAGAGAGGCCTGAGGACCTGAGAGCCTCT
GAGCGCTTCTTGCACTTCATGCTGGGCTGGTTTGCACACCCCGTCTTTGTGGATGGAGAC
TACCCAGCCACCCTGAGGACCCAGATCCAACAGATGAACAGACAGTGCTCCCATCCTGTG
GCTCAACTCCCCGAGTTCACAGAGGCAGAGAAGCAGCTCCTGAAAGGCTCTGCTGATTTT
CTGGGTCTGTCGCATTACACCTCCCGCCTCATCAGCAACGCCCCACAAAACACCTGCATC
CCTAGCTATGATACCATTGGAGGCTTCTCCCAACACGTGAACCATGTGTGGCCCCAGACC
TCATCCTCTTGGATTCGTGTGGTGCCCTGGGGGATAAGGAGGCTGTTGCAGTTTGTATCC
CTGGAATACACAAGAGGAAAAGTTCCAATATACCTTGCCGGGAATGGCATGCCCATAGGG
GAAAGTGAAAATCTCTTTGATGATTCCTTAAGAGTAGACTACTTCAATCAATATATCAAT
GAGGTGCTCAAGGCTATCAAGGAAGACTCTGTGGATGTTCGTTCCTACATTGCTCGTTCC
CTCATTGATGGCTTCGAAGGCCCTTCTGGTTACAGCCAGCGGTTTGGCCTGCACCACGTC
AACTTCAGCGACAGCAGCAAGTCAAGGACTCCCAGGAAATCTGCCTACTTTTTCACTAGC
ATCATAGAAAAGAACGGTTTCCTCACCAAGGGGGCAAAAAGACTGCTACCACCTAATACA
GTAAACCTCCCCTCCAAAGTCAGAGCCTTCACTTTTCCATCTGAGGTGCCCTCCAAGGCT
AAAGTCGTTTGGGAAAAGTTCTCCAGCCAACCCAAGTTCGAAAGAGATTTGTTCTACCAC
GGGACGTTTCGGGATGACTTTCTGTGGGGCGTGTCCTCTTCCGCTTATCAGATTGAAGGC
GCGTGGGATGCCGATGGCAAAGGCCCCAGCATCTGGGATAACTTTACCCACACACCAGGG
AGCAATGTGAAAGACAATGCCACTGGAGACATCGCCTGTGACAGCTATCACCAGCTGGAT
GCCGATCTGAATATGCTCCGAGCTTTGAAGGTGAAGGCCTACCGCTTCTCTATCTCCTGG
TCTCGGATTTTCCCAACTGGGAGAAACAGCTCTATCAACAGTCATGGGGTTGATTATTAC
AACAGGCTGATCAATGGCTTGGTGGCAAGCAACATCTTTCCCATGGTGACATTGTTCCAT
TGGGACCTGCCCCAGGCCCTCCAGGATATCGGAGGCTGGGAGAATCCTGCCTTGATTGAC
TTGTTTGACAGCTACGCAGACTTTTGTTTCCAGACCTTTGGTGATAGAGTCAAGTTTTGG
ATGACTTTTAATGAGCCCATGTACCTGGCATGGCTAGGTTATGGCTCAGGGGAATTTCCC
CCAGGGGTGAAGGACCCAGGCTGGGCACCATATAGGATAGCCCACACCGTCATCAAAGCC
CATGCCAGAGTCTATCACACGTACGATGAGAAATACAGGCAGGAGCAGAAGGGGGTCATC
TCGCTGAGCCTCAGTACACACTGGGCAGAGCCCAAGTCACCAGGGGTCCCCAGAGATGTG
GAAGCCGCTGACCGAATGCTGCAGTTCTCCCTGGGCTGGTTTGCTCACCCCATTTTTAGA
AACGGAGACTATCCTGACACCATGAAGTGGAAAGTGGGGAACAGGAGTGAACTGCAGCAC
TTAGCCACCTCCCGCCTGCCAAGCTTCACTGAGGAAGAGAAGAGGTTCATCAGGGCGACG
GCCGACGTCTTCTGCCTCAACACGTACTACTCCAGAATCGTGCAGCACAAAACACCCAGG
CTAAACCCACCCTCCTACGAAGACGACCAGGAGATGGCTGAGGAGGAGGACCCTTCGTGG
CCTTCCACGGCAATGAACAGAGCTGCGCCCTGGGGGACGCGAAGGCTGCTGAACTGGATC
AAGGAAGAGTATGGTGACATCCCCATTTACATCACCGAAAACGGAGTGGGGCTGACCAAT
CCGAACACGGAGGATACTGATAGGATATTTTACCACAAAACCTACATCAATGAGGCTTTG
AAAGCCTACAGGCTCGATGGTATAGACCTTCGAGGGTATGTCGCCTGGTCTCTGATGGAC
AACTTTGAGTGGCTAAATGGCTACACGGTCAAGTTTGGACTGTACCATGTTGATTTCAAC
AACACGAACAGGCCTCGCACAGCAAGAGCCTCCGCCAGGTACTACACAGAGGTCATTACC
AACAACGGCATGCCACTGGCCAGGGAGGATGAGTTTCTGTACGGACGGTTTCCTGAGGGC
TTCATCTGGAGTGCAGCTTCTGCTGCATATCAGATTGAAGGTGCGTGGAGAGCAGATGGC
AAAGGACTCAGCATTTGGGACACGTTTTCTCACACACCACTGAGGGTTGAGAACGATGCC
ATTGGAGACGTGGCCTGTGACAGTTATCACAAGATTGCTGAGGATCTGGTCACCCTGCAG
AACCTGGGTGTGTCCCACTACCGTTTTTCCATCTCCTGGTCTCGCATCCTCCCTGATGGA
ACCACCAGGTACATCAATGAAGCGGGCCTGAACTACTACGTGAGGCTCATCGATACACTG
CTGGCCGCCAGCATCCAGCCCCAGGTGACCATTTACCACTGGGACCTACCACAGACGCTC
CAAGATGTAGGAGGCTGGGAGAATGAGACCATCGTGCAGCGGTTTAAGGAGTATGCAGAT
GTGCTCTTCCAGAGGCTGGGAGACAAGGTGAAGTTTTGGATCACGTTGAATGAGCCCTTT
GTCATTGCTTACCAGGGCTATGGCTACGGAACAGCAGCTCCAGGAGTCTCCAATAGGCCT
GGCACTGCCCCCTACATTGTTGGCCACAATCTAATAAAGGCTCATGCTGAGGCCTGGCAT
CTGTACAACGATGTGTACCGCGCCAGTCAAGGTGGCGTGATTTCCATCACCATCAGCAGT
GACTGGGCTGAACCCAGAGATCCCTCTAACCAGGAGGATGTGGAGGCAGCCAGGAGATAT
GTTCAGTTCATGGGAGGCTGGTTTGCACATCCTATTTTCAAGAATGGAGATTACAATGAG
GTGATGAAGACGCGGATCCGTGACAGGAGCTTGGCTGCAGGCCTCAACAAGTCTCGGCTG
CCAGAATTTACAGAGAGTGAGAAGAGGAGGATCAACGGCACCTATGACTTTTTTGGGTTC
AATCACTACACCACTGTCCTCGCCTACAACCTCAACTATGCCACTGCCATCTCTTCTTTT
GATGCAGACAGAGGAGTTGCTTCCATCGCAGATCGCTCGTGGCCAGACTCTGGCTCCTTC
TGGCTGAAGATGACGCCTTTTGGCTTCAGGAGGATCCTGAACTGGTTAAAGGAGGAATAC
AATGACCCTCCAATTTATGTCACAGAGAATGGAGTGTCCCAGCGGGAAGAAACAGACCTC
AATGACACTGCAAGGATCTACTACCTTCGGACTTACATCAATGAGGCCCTCAAAGCTGTG
CAGGACAAGGTGGACCTTCGAGGATACACAGTTTGGAGTGCGATGGACAATTTTGAGTGG
GCCACAGGCTTTTCAGAGAGATTTGGTCTGCATTTTGTGAACTACAGTGACCCTTCTCTG
CCAAGGATCCCCAAAGCATCAGCGAAGTTCTACGCCTCTGTGGTCCGATGCAATGGCTTC
CCTGACCCCGCTACAGGGCCTCACGCTTGTCTCCACCAGCCAGATGCTGGACCCACCATC
AGCCCCGTGAGACAGGAGGAGGTGCAGTTCCTGGGGCTAATGCTCGGCACCACAGAAGCA
CAGACAGCTTTGTACGTTCTCTTTTCTCTTGTGCTTCTTGGAGTCTGTGGCTTGGCATTT
CTGTCATACAAGTACTGCAAGCGCTCTAAGCAAGGGAAAACACAACGAAGCCAACAGGAA
TTGAGCCCGGTGTCTTCATTCTGA
Enzyme 6 GenBank Gene ID X07994 Link Image
Enzyme 6 GeneCard ID LCT Link Image
Enzyme 6 GenAtlas ID LCT Link Image
Enzyme 6 HGNC ID HGNC:6530 Link Image
Enzyme 6 Chromosome Location Not Available
Enzyme 6 Locus Not Available
Enzyme 6 SNPs SNPJam Report Link Image
Enzyme 6 General References
  1. Mantei N, Villa M, Enzler T, Wacker H, Boll W, James P, Hunziker W, Semenza G: Complete primary structure of human and rabbit lactase-phlorizin hydrolase: implications for biosynthesis, membrane anchoring and evolution of the enzyme. EMBO J. 1988 Sep;7(9):2705-13. [PubMed Link Image]
  2. Boll W, Wagner P, Mantei N: Structure of the chromosomal gene and cDNAs coding for lactase-phlorizin hydrolase in humans with adult-type hypolactasia or persistence of lactase. Am J Hum Genet. 1991 May;48(5):889-902. [PubMed Link Image]
Enzyme 6 Metabolite References Not Available
Enzyme 7 [top]
Enzyme 7 ID 6124
Enzyme 7 Name Beta-galactosidase precursor
Enzyme 7 Synonyms
  1. Lactase
  2. Acid beta- galactosidase
Enzyme 7 Gene Name GLB1
Enzyme 7 Protein Sequence >Beta-galactosidase precursor 
MPGFLVRILLLLLVLLLLGPTRGLRNATQRMFEIDYSRDSFLKDGQPFRYISGSIHYSRV
PRFYWKDRLLKMKMAGLNAIQTYVPWNFHEPWPGQYQFSEDHDVEYFLRLAHELGLLVIL
RPGPYICAEWEMGGLPAWLLEKESILLRSSDPDYLAAVDKWLGVLLPKMKPLLYQNGGPV
ITVQVENEYGSYFACDFDYLRFLQKRFRHHLGDDVVLFTTDGAHKTFLKCGALQGLYTTV
DFGTGSNITDAFLSQRKCEPKGPLINSEFYTGWLDHWGQPHSTIKTEAVASSLYDILARG
ASVNLYMFIGGTNFAYWNGANSPYAAQPTSYDYDAPLSEAGDLTEKYFALRNIIQKFEKV
PEGPIPPSTPKFAYGKVTLEKLKTVGAALDILCPSGPIKSLYPLTFIQVKQHYGFVLYRT
TLPQDCSNPAPLSSPLNGVHDRAYVAVDGIPQGVLERNNVITLNITGKAGATLDLLVENM
GRVNYGAYINDFKGLVSNLTLSSNILTDWTIFPLDTEDAVRSHLGGWGHRDSGHHDEAWA
HNSSNYTLPAFYMGNFSIPSGIPDLPQDTFIQFPGWTKGQVWINGFNLGRYWPARGPQLT
LFVPQHILMTSAPNTITVLELEWAPCSSDDPELCAVTFVDRPVIGSSVTYDHPSKPVEKR
LMPPPPQKNKDSWLDHV
Enzyme 7 Number of Residues 677
Enzyme 7 Molecular Weight 76092
Enzyme 7 Theoretical pI 6.55
Enzyme 7 GO Classification
Function
  • beta-galactosidase activity
  • catalytic activity
  • galactosidase activity
  • hydrolase activity
  • hydrolase activity, acting on glycosyl bonds
  • hydrolase activity, hydrolyzing O-glycosyl compounds
Process
  • carbohydrate metabolism
  • macromolecule metabolism
  • metabolism
  • physiological process
Component
  • beta-galactosidase complex
  • protein complex
  • unlocalized protein complex
Enzyme 7 General Function Carbohydrate transport and metabolism
Enzyme 7 Specific Function Cleaves beta-linked terminal galactosyl residues from gangliosides, glycoproteins, and glycosaminoglycans
Enzyme 7 Pathways
Enzyme 7 Reactions
  • Hydrolysis of terminal non-reducing beta-D-galactose residues in beta-D-galactosides
Enzyme 7 Pfam Domain Function
Enzyme 7 Signals
  • 1-23
Enzyme 7 Transmembrane Regions Not Available
Enzyme 7 Essentiality Not Available
Enzyme 7 GenBank ID Protein 179401 Link Image
Enzyme 7 UniProtKB/Swiss-Prot ID P16278 Link Image
Enzyme 7 UniProtKB/Swiss-Prot Entry Name BGAL_HUMAN Link Image
Enzyme 7 PDB ID Not Available
Enzyme 7 Cellular Location Not Available
Enzyme 7 Gene Sequence >2034 bp 
ATGCCGGGGTTCCTGGTTCGCATCCTCCTTCTGCTGCTGGTTCTGCTGCTTCTGGGCCCT
ACGCGCGGCTTGCGCAATGCCACCCAGAGGATGTTTGAAATTGACTATAGCCGGGACTCC
TTCCTCAAGGATGGCCAGCCATTTCGCTACATCTCAGGAAGCATTCACTACTCCCGTGTG
CCCCGCTTCTACTGGAAGGACCGGCTGCTGAAGATGAAGATGGCTGGGCTGAACGCCATC
CAGACGTATGTGCCCTGGAACTTTCATGAGCCCTGGCCAGGACAGTACCAGTTTTCTGAG
GACCATGATGTGGAATATTTTCTTCGGCTGGCTCATGAGCTGGGACTGCTGGTTATCCTG
AGGCCCGGGCCCTACATCTGTGCAGAGTGGGAAATGGGAGGATTACCTGCTTGGCTGCTA
GAGAAAGAGTCTATTCTTCTCCGCTCCTCCGACCCAGATTACCTGGCAGCTGTGGACAAG
TGGTTGGGAGTCCTTCTGCCCAAGATGAAGCCTCTCCTCTATCAGAATGGAGGGCCAGTT
ATAACAGTGCAGGTTGAAAATGAATATGGCAGCTACTTTGCCTGTGATTTTGACTACCTG
CGCTTCCTGCAGAAGCGCTTTCGCCACCATCTGGGGGATGATGTGGTTCTGTTTACCACT
GATGGAGCACATAAAACATTCCTGAAATGTGGGGCCCTGCAGGGCCTCTACACCACGGTG
GACTTTGGAACAGGCAGCAACATCACAGATGCTTTCCTAAGCCAGAGGAAGTGTGAGCCC
AAAGGACCCTTGATCAATTCTGAATTCTATACTGGCTGGCTAGATCACTGGGGCCAACCT
CACTCCACAATCAAGACCGAAGCAGTGGCTTCCTCCCTCTATGATATACTTGCCCGTGGG
GCGAGTGTGAACTTGTACATGTTTATAGGTGGGACCAATTTTGCCTATTGGAATGGGGCC
AACTCACCCTATGCAGCACAGCCCACCAGCTACGACTATGATGCCCCACTGAGTGAGGCT
GGGGACCTCACTGAGAAGTATTTTGCTCTGCGAAACATCATCCAGAAGTTTGAAAAAGTA
CCAGAAGGTCCTATCCCTCCATCTACACCAAAGTTTGCATATGGAAAGGTCACTTTGGAA
AAGTTAAAGACAGTGGGAGCAGCTCTGGACATTCTGTGTCCCTCTGGGCCCATCAAAAGC
CTTTATCCCTTGACATTTATCCAGGTGAAACAGCATTATGGGTTTGTGCTGTACCGGACA
ACACTTCCTCAAGATTGCAGCAACCCAGCACCTCTCTCTTCACCCCTCAATGGAGTCCAC
GATCGAGCATATGTTGCTGTGGATGGGATCCCCCAGGGAGTCCTTGAGCGAAACAATGTG
ATCACTCTGAACATAACAGGGAAAGCTGGAGCCACTCTGGACCTTCTGGTAGAGAACATG
GGACGTGTGAACTATGGTGCATATATCAACGATTTTAAGGGTTTGGTTTCTAACCTGACT
CTCAGTTCCAATATCCTCACGGACTGGACGATCTTTCCACTGGACACTGAGGATGCAGTG
CGCAGCCACCTGGGGGGCTGGGGACACCGTGACAGTGGCCACCATGATGAAGCCTGGGCC
CACAACTCATCCAACTACACGCTCCCGGCCTTTTATATGGGGAACTTCTCCATTCCCAGT
GGGATCCCAGACTTGCCCCAGGACACCTTTATCCAGTTTCCTGGATGGACCAAGGGCCAG
GTCTGGATTAATGGCTTTAACCTTGGCCGCTATTGGCCAGCCCGGGGCCCTCAGTTGACC
TTGTTTGTGCCCCAGCACATCCTGATGACCTCGGCCCCAAACACCATCACCGTGCTGGAA
CTGGAGTGGGCACCCTGCAGCAGTGATGATCCAGAACTATGTGCTGTGACGTTCGTGGAC
AGGCCAGTTATTGGCTCATCTGTGACCTACGATCATCCCTCCAAACCTGTTGAAAAAAGA
CTCATGCCCCCACCCCCGCAAAAAAACAAAGATTCATGGCTGGACCATGTATGA
Enzyme 7 GenBank Gene ID M27507 Link Image
Enzyme 7 GeneCard ID GLB1 Link Image
Enzyme 7 GenAtlas ID GLB1 Link Image
Enzyme 7 HGNC ID HGNC:4298 Link Image
Enzyme 7 Chromosome Location 3
Enzyme 7 Locus 3p21.33
Enzyme 7 SNPs SNPJam Report Link Image
Enzyme 7 General References
  1. Morreau H, Galjart NJ, Gillemans N, Willemsen R, van der Horst GT, d'Azzo A: Alternative splicing of beta-galactosidase mRNA generates the classic lysosomal enzyme and a beta-galactosidase-related protein. J Biol Chem. 1989 Dec 5;264(34):20655-63. [PubMed Link Image]
  2. Yamamoto Y, Hake CA, Martin BM, Kretz KA, Ahern-Rindell AJ, Naylor SL, Mudd M, O'Brien JS: Isolation, characterization, and mapping of a human acid beta-galactosidase cDNA. DNA Cell Biol. 1990 Mar;9(2):119-27. [PubMed Link Image]
  3. Oshima A, Tsuji A, Nagao Y, Sakuraba H, Suzuki Y: Cloning, sequencing, and expression of cDNA for human beta-galactosidase. Biochem Biophys Res Commun. 1988 Nov 30;157(1):238-44. [PubMed Link Image]
  4. Hinek A, Zhang S, Smith AC, Callahan JW: Impaired elastic-fiber assembly by fibroblasts from patients with either Morquio B disease or infantile GM1-gangliosidosis is linked to deficiency in the 67-kD spliced variant of beta-galactosidase. Am J Hum Genet. 2000 Jul;67(1):23-36. Epub 2000 Jun 6. [PubMed Link Image]
  5. Callahan JW: Molecular basis of GM1 gangliosidosis and Morquio disease, type B. Structure-function studies of lysosomal beta-galactosidase and the non-lysosomal beta-galactosidase-like protein. Biochim Biophys Acta. 1999 Oct 8;1455(2-3):85-103. [PubMed Link Image]
  6. Oshima A, Yoshida K, Shimmoto M, Fukuhara Y, Sakuraba H, Suzuki Y: Human beta-galactosidase gene mutations in morquio B disease. Am J Hum Genet. 1991 Nov;49(5):1091-3. [PubMed Link Image]
  7. Nishimoto J, Nanba E, Inui K, Okada S, Suzuki K: GM1-gangliosidosis (genetic beta-galactosidase deficiency): identification of four mutations in different clinical phenotypes among Japanese patients. Am J Hum Genet. 1991 Sep;49(3):566-74. [PubMed Link Image]
  8. Yoshida K, Oshima A, Shimmoto M, Fukuhara Y, Sakuraba H, Yanagisawa N, Suzuki Y: Human beta-galactosidase gene mutations in GM1-gangliosidosis: a common mutation among Japanese adult/chronic cases. Am J Hum Genet. 1991 Aug;49(2):435-42. [PubMed Link Image]
  9. Mosna G, Fattore S, Tubiello G, Brocca S, Trubia M, Gianazza E, Gatti R, Danesino C, Minelli A, Piantanida M: A homozygous missense arginine to histidine substitution at position 482 of the beta-galactosidase in an Italian infantile GM1-gangliosidosis patient. Hum Genet. 1992 Nov;90(3):247-50. [PubMed Link Image]
  10. Boustany RM, Qian WH, Suzuki K: Mutations in acid beta-galactosidase cause GM1-gangliosidosis in American patients. Am J Hum Genet. 1993 Oct;53(4):881-8. [PubMed Link Image]
  11. Chakraborty S, Rafi MA, Wenger DA: Mutations in the lysosomal beta-galactosidase gene that cause the adult form of GM1 gangliosidosis. Am J Hum Genet. 1994 Jun;54(6):1004-13. [PubMed Link Image]
  12. Ishii N, Oohira T, Oshima A, Sakuraba H, Endo F, Matsuda I, Sukegawa K, Orii T, Suzuki Y: Clinical and molecular analysis of a Japanese boy with Morquio B disease. Clin Genet. 1995 Aug;48(2):103-8. [PubMed Link Image]
  13. Kaye EM, Shalish C, Livermore J, Taylor HA, Stevenson RE, Breakefield XO: beta-Galactosidase gene mutations in patients with slowly progressive GM1 gangliosidosis. J Child Neurol. 1997 Jun;12(4):242-7. [PubMed Link Image]
  14. Bagshaw RD, Zhang S, Hinek A, Skomorowski MA, Whelan D, Clarke JT, Callahan JW: Novel mutations (Asn 484 Lys, Thr 500 Ala, Gly 438 Glu) in Morquio B disease. Biochim Biophys Acta. 2002 Dec 12;1588(3):247-53. [PubMed Link Image]
  15. Silva CM, Severini MH, Sopelsa A, Coelho JC, Zaha A, d'Azzo A, Giugliani R: Six novel beta-galactosidase gene mutations in Brazilian patients with GM1-gangliosidosis. Hum Mutat. 1999;13(5):401-9. [PubMed Link Image]
  16. Zhang S, Bagshaw R, Hilson W, Oho Y, Hinek A, Clarke JT, Callahan JW: Characterization of beta-galactosidase mutations Asp332-->Asn and Arg148-->Ser, and a polymorphism, Ser532-->Gly, in a case of GM1 gangliosidosis. Biochem J. 2000 Jun 15;348 Pt 3:621-32. [PubMed Link Image]
  17. Morrone A, Bardelli T, Donati MA, Giorgi M, Di Rocco M, Gatti R, Parini R, Ricci R, Taddeucci G, D'Azzo A, Zammarchi E: beta-galactosidase gene mutations affecting the lysosomal enzyme and the elastin-binding protein in GM1-gangliosidosis patients with cardiac involvement. Hum Mutat. 2000;15(4):354-66. [PubMed Link Image]
  18. Paschke E, Milos I, Kreimer-Erlacher H, Hoefler G, Beck M, Hoeltzenbein M, Kleijer W, Levade T, Michelakakis H, Radeva B: Mutation analyses in 17 patients with deficiency in acid beta-galactosidase: three novel point mutations and high correlation of mutation W273L with Morquio disease type B. Hum Genet. 2001 Aug;109(2):159-66. [PubMed Link Image]
Enzyme 7 Metabolite References Not Available
Enzyme 8 [top]
Enzyme 8 ID 7152
Enzyme 8 Name Glucosylceramidase precursor
Enzyme 8 Synonyms
  1. Beta-glucocerebrosidase
  2. Acid beta-glucosidase
  3. D-glucosyl-N-acylsphingosine glucohydrolase
  4. Alglucerase
  5. Imiglucerase
Enzyme 8 Gene Name GBA
Enzyme 8 Protein Sequence >Glucosylceramidase precursor 
MEFSSPSREECPKPLSRVSIMAGSLTGLLLLQAVSWASGARPCIPKSFGYSSVVCVCNAT
YCDSFDPPTFPALGTFSRYESTRSGRRMELSMGPIQANHTGTGLLLTLQPEQKFQKVKGF
GGAMTDAAALNILALSPPAQNLLLKSYFSEEGIGYNIIRVPMASCDFSIRTYTYADTPDD
FQLHNFSLPEEDTKLKIPLIHRALQLAQRPVSLLASPWTSPTWLKTNGAVNGKGSLKGQP
GDIYHQTWARYFVKFLDAYAEHKLQFWAVTAENEPSAGLLSGYPFQCLGFTPEHQRDFIA
RDLGPTLANSTHHNVRLLMLDDQRLLLPHWAKVVLTDPEAAKYVHGIAVHWYLDFLAPAK
ATLGETHRLFPNTMLFASEACVGSKFWEQSVRLGSWDRGMQYSHSIITNLLYHVVGWTDW
NLALNPEGGPNWVRNFVDSPIIVDITKDTFYKQPMFYHLGHFSKFIPEGSQRVGLVASQK
NDLDAVALMHPDGSAVVVVLNRSSKDVPLTIKDPAVGFLETISPGYSIHTYLWRRQ
Enzyme 8 Number of Residues 536
Enzyme 8 Molecular Weight 59717
Enzyme 8 Theoretical pI 7.66
Enzyme 8 GO Classification
Function
  • catalytic activity
  • glucosylceramidase activity
  • hydrolase activity
  • hydrolase activity, acting on glycosyl bonds
  • hydrolase activity, hydrolyzing O-glycosyl compounds
Process
  • cell organization and biogenesis
  • cellular lipid metabolism
  • cellular physiological process
  • lipid metabolism
  • lysosome organization and biogenesis
  • membrane lipid metabolism
  • metabolism
  • organelle organization and biogenesis
  • physiological process
  • primary metabolism
  • sphingolipid metabolism
  • vacuole organization and biogenesis
Component
  • intracellular membrane-bound organelle
  • lysosome
  • lytic vacuole
  • membrane-bound organelle
  • organelle
  • vacuole
Enzyme 8 General Function Not Available
Enzyme 8 Specific Function D-glucosyl-N-acylsphingosine + H(2)O = D- glucose + N-acylsphingosine
Enzyme 8 Pathways
Enzyme 8 Reactions
  • D-glucosyl-N-acylsphingosine + H2O = D-glucose + N-acylsphingosine
Enzyme 8 Pfam Domain Function
Enzyme 8 Signals
  • 21-39
Enzyme 8 Transmembrane Regions Not Available
Enzyme 8 Essentiality Not Available
Enzyme 8 GenBank ID Protein 183008 Link Image
Enzyme 8 UniProtKB/Swiss-Prot ID P04062 Link Image
Enzyme 8 UniProtKB/Swiss-Prot Entry Name GLCM_HUMAN Link Image
Enzyme 8 PDB ID 1Y7V Link Image
Enzyme 8 PDB File Show
Enzyme 8 3D Structure
Enzyme 8 Cellular Location Not Available
Enzyme 8 Gene Sequence >1551 bp 
ATGGCTGGCAGCCTCACAGGTTTGCTTCTACTTCAGGCAGTGTCGTGGGCATCAGGTGCC
CGCCCCTGCATCCCTAAAAGCTTCGGCTACAGCTCGGTGGTGTGTGTCTGCAATGCCACA
TACTGTGACTCCTTTGACCCCCCGACCTTTCCTGCCCTTGGTACCTTCAGCCGCTATGAG
AGTACACGCAGTGGGCGACGGATGGAGCTGAGTATGGGGCCCATCCAGGCTAATCACACG
GGCACAGGCCTGCTACTGACCCTGCAGCCAGAACAGAAGTTCCAGAAAGTGAAGGGATTT
GGAGGGGCCATGACAGATGCTGCTGCTCTCAACATCCTTGCCCTGTCACCCCCTGCCCAA
AATTTGCTACTTAAATCGTACTTCTCTGAAGAAGGAATCGGATATAACATCATCCGGGTA
CCCATGGCCAGCTGTGACTTCTCCATCCGCACCTACACCTATGCAGACACCCCTGATGAT
TTCCAGTTGCACAACTTCAGCCTCCCAGAGGAAGATACCAAGCTCAAGATACCCCTGATT
CACCGAGCCCTGCAGTTGGCCCAGCGTCCCGTTTCACTCCTTGCCAGCCCCTGGACATCA
CCCACTTGGCTCAAGACCAATGGAGCGGTGAATGGGAAGGGGTCACTCAAGGGACAGCCC
GGAGACATCTACCACCAGACCTGGGCCAGATACTTTGTGAAGTTCCTGGATGCCTATGCT
GAGCACAAGTTACAGTTCTGGGCAGTGACAGCTGAAAATGAGCCTTCTGCTGGGCTGTTG
AGTGGATACCCCTTCCAGTGCCTGGGCTTCACCCCTGAACATCAGCGAGACTTCATTGCC
CGTGACCTAGGTCCTACCCTCGCCAACAGTACTCACCACAATGTCCGCCTACTCATGCTG
GATGACCAACGCTTGCTGCTGCCCCACTGGGCAAAGGTGGTACTGACAGACCCAGAAGCA
GCTAAATATGTTCATGGCATTGCTGTACATTGGTACCTGGACTTTCTGGCTCCAGCCAAA
GCCACCCTAGGGGAGACACACCGCCTGTTCCCCAACACCATGCTCTTTGCCTCAGAGGCC
TGTGTGGGCTCCAAGTTCTGGGAGCAGAGTGTGCGGCTAGGCTCCTGGGATCGAGGGATG
CAGTACAGCCACAGCATCATCACGAACCTCCTGTACCATGTGGTCGGCTGGACCGACTGG
AACCTTGCCCTGAACCCCGAAGGAGGACCCAATTGGGTGCGTAACTTTGTCGACAGTCCC
ATCATTGTAGACATCACCAAGGACACGTTTTACAAACAGCCCATGTTCTACCACCTTGGC
CACTTCAGCAAGTTCATTCCTGAGGGCTCCCAGAGAGTGGGGCTGGTTGCCAGTCAGAAG
AACGACCTGGACGCAGTGGCACTGATGCATCCCGATGGCTCTGCTGTTGTGGTCGTGCTA
AACCGCTCCTCTAAGGATGTGCCTCTTACCATCAAGGATCCTGCTGTGGGCTTCCTGGAG
ACAATCTCACCTGGCTACTCCATTCACACCTACCTGTGGCATCGCCAGTGA
Enzyme 8 GenBank Gene ID M16328 Link Image
Enzyme 8 GeneCard ID GBA Link Image
Enzyme 8 GenAtlas ID GBA Link Image
Enzyme 8 HGNC ID HGNC:4177 Link Image
Enzyme 8 Chromosome Location 1
Enzyme 8 Locus 1q21
Enzyme 8 SNPs SNPJam Report Link Image
Enzyme 8 General References
  1. Sorge J, West C, Westwood B, Beutler E: Molecular cloning and nucleotide sequence of human glucocerebrosidase cDNA. Proc Natl Acad Sci U S A. 1985 Nov;82(21):7289-93. [PubMed Link Image]
  2. Tsuji S, Choudary PV, Martin BM, Winfield S, Barranger JA, Ginns EI: Nucleotide sequence of cDNA containing the complete coding sequence for human lysosomal glucocerebrosidase. J Biol Chem. 1986 Jan 5;261(1):50-3. [PubMed Link Image]
  3. Horowitz M, Wilder S, Horowitz Z, Reiner O, Gelbart T, Beutler E: The human glucocerebrosidase gene and pseudogene: structure and evolution. Genomics. 1989 Jan;4(1):87-96. [PubMed Link Image]
  4. Beutler E, West C, Gelbart T: Polymorphisms in the human glucocerebrosidase gene. Genomics. 1992 Apr;12(4):795-800. [PubMed Link Image]
  5. Imai K, Nakamura M, Yamada M, Asano A, Yokoyama S, Tsuji S, Ginns EI: A novel transcript from a pseudogene for human glucocerebrosidase in non-Gaucher disease cells. Gene. 1993 Dec 22;136(1-2):365-8. [PubMed Link Image]
  6. Winfield SL, Tayebi N, Martin BM, Ginns EI, Sidransky E: Identification of three additional genes contiguous to the glucocerebrosidase locus on chromosome 1q21: implications for Gaucher disease. Genome Res. 1997 Oct;7(10):1020-6. [PubMed Link Image]
  7. Reiner O, Wigderson M, Horowitz M: Structural analysis of the human glucocerebrosidase genes. DNA. 1988 Mar;7(2):107-16. [PubMed Link Image]
  8. Sorge JA, West C, Kuhl W, Treger L, Beutler E: The human glucocerebrosidase gene has two functional ATG initiator codons. Am J Hum Genet. 1987 Dec;41(6):1016-24. [PubMed Link Image]
  9. Ginns EI, Choudary PV, Martin BM, Winfield S, Stubblefield B, Mayor J, Merkle-Lehman D, Murray GJ, Bowers LA, Barranger JA: Isolation of cDNA clones for human beta-glucocerebrosidase using the lambda gt11 expression system. Biochem Biophys Res Commun. 1984 Sep 17;123(2):574-80. [PubMed Link Image]
  10. Tsuji S, Martin BM, Barranger JA, Stubblefield BK, LaMarca ME, Ginns EI: Genetic heterogeneity in type 1 Gaucher disease: multiple genotypes in Ashkenazic and non-Ashkenazic individuals. Proc Natl Acad Sci U S A. 1988 Apr;85(7):2349-52. [PubMed Link Image]
  11. Dinur T, Osiecki KM, Legler G, Gatt S, Desnick RJ, Grabowski GA: Human acid beta-glucosidase: isolation and amino acid sequence of a peptide containing the catalytic site. Proc Natl Acad Sci U S A. 1986 Mar;83(6):1660-4. [PubMed Link Image]
  12. Zhang H, Li XJ, Martin DB, Aebersold R: Identification and quantification of N-linked glycoproteins using hydrazide chemistry, stable isotope labeling and mass spectrometry. Nat Biotechnol. 2003 Jun;21(6):660-6. Epub 2003 May 18. [PubMed Link Image]
  13. Horowitz M, Zimran A: Mutations causing Gaucher disease. Hum Mutat. 1994;3(1):1-11. [PubMed Link Image]
  14. Beutler E, Gelbart T: Glucocerebrosidase (Gaucher disease). Hum Mutat. 1996;8(3):207-13. [PubMed Link Image]
  15. Tayebi N, Stone DL, Sidransky E: Type 2 gaucher disease: an expanding phenotype. Mol Genet Metab. 1999 Oct;68(2):209-19. [PubMed Link Image]
  16. Stone DL, Tayebi N, Orvisky E, Stubblefield B, Madike V, Sidransky E: Glucocerebrosidase gene mutations in patients with type 2 Gaucher disease. Hum Mutat. 2000;15(2):181-8. [PubMed Link Image]
  17. Beutler E, Gelbart T: Gaucher disease associated with a unique KpnI restriction site: identification of the amino-acid substitution. Ann Hum Genet. 1990 May;54(Pt 2):149-53. [PubMed Link Image]
  18. Hong CM, Ohashi T, Yu XJ, Weiler S, Barranger JA: Sequence of two alleles responsible for Gaucher disease. DNA Cell Biol. 1990 May;9(4):233-41. [PubMed Link Image]
  19. Beutler E, Gelbart T, West C: Identification of six new Gaucher disease mutations. Genomics. 1993 Jan;15(1):203-5. [PubMed Link Image]
  20. Choy FY, Wei C, Applegarth DA, McGillivray BC: DNA analysis of an uncommon missense mutation in a Gaucher disease patient of Jewish-Polish-Russian descent. Am J Med Genet. 1994 Jun 1;51(2):156-60. [PubMed Link Image]
  21. Beutler E, Gelbart T: Two new Gaucher disease mutations. Hum Genet. 1994 Feb;93(2):209-10. [PubMed Link Image]
  22. Tuteja R, Tuteja N, Lilliu F, Bembi B, Galanello R, Cao A, Baralle FE: Y418C: a novel mutation in exon 9 of the glucocerebrosidase gene of a patient with Gaucher disease creates a new Bgl I site. Hum Genet. 1994 Sep;94(3):314-5. [PubMed Link Image]
  23. Beutler E, Demina A, Gelbart T: Glucocerebrosidase mutations in Gaucher disease. Mol Med. 1994 Nov;1(1):82-92. [PubMed Link Image]
  24. Cormand B, Vilageliu L, Burguera JM, Balcells S, Gonzalez-Duarte R, Grinberg D, Chabas A: Gaucher disease in Spanish patients: analysis of eight mutations. Hum Mutat. 1995;5(4):303-9. [PubMed Link Image]
  25. Choy FY, Wei C: Identification of a new mutation (P178S) in an African-American patient with type 2 Gaucher disease. Hum Mutat. 1995;5(4):345-7. [PubMed Link Image]
  26. Morar B, Lane AB: The molecular characterization of Gaucher disease in South Africa. Clin Genet. 1996 Aug;50(2):78-84. [PubMed Link Image]
  27. Kim JW, Liou BB, Lai MY, Ponce E, Grabowski GA: Gaucher disease: identification of three new mutations in the Korean and Chinese (Taiwanese) populations. Hum Mutat. 1996;7(3):214-8. [PubMed Link Image]
  28. Cormand B, Vilageliu L, Balcells S, Gonzalez-Duarte R, Chabas A, Grinberg D: Two novel (1098insA and Y313H) and one rare (R359Q) mutations detected in exon 8 of the beta-glucocerebrosidase gene in Gaucher's disease patients. Hum Mutat. 1996;7(3):272-4. [PubMed Link Image]
  29. Amaral O, Pinto E, Fortuna M, Lacerda L, Sa Miranda MC: Type 1 Gaucher disease: identification of N396T and prevalence of glucocerebrosidase mutations in the Portuguese. Hum Mutat. 1996;8(3):280-1. [PubMed Link Image]
  30. Seeman PJ, Finckh U, Hoppner J, Lakner V, Liebisch I, Grau G, Rolfs A: Two new missense mutations in a non-Jewish Caucasian family with type 3 Gaucher disease. Neurology. 1996 Apr;46(4):1102-7. [PubMed Link Image]
  31. Cormand B, Grinberg D, Gort L, Fiumara A, Barone R, Vilageliu L, Chabas A: Two new mild homozygous mutations in Gaucher disease patients: clinical signs and biochemical analyses. Am J Med Genet. 1997 Jun 27;70(4):437-43. [PubMed Link Image]
  32. Choy FY, Humphries ML, Shi H: Identification of two novel and four uncommon missense mutations among chinese Gaucher disease patients. Am J Med Genet. 1997 Aug 8;71(2):172-8. [PubMed Link Image]
  33. Hatton CE, Cooper A, Whitehouse C, Wraith JE: Mutation analysis in 46 British and Irish patients with Gaucher's disease. Arch Dis Child. 1997 Jul;77(1):17-22. [PubMed Link Image]
  34. Grace ME, Desnick RJ, Pastores GM: Identification and expression of acid beta-glucosidase mutations causing severe type 1 and neurologic type 2 Gaucher disease in non-Jewish patients. J Clin Invest. 1997 May 15;99(10):2530-7. [PubMed Link Image]
  35. Ida H, Rennert OM, Kawame H, Maekawa K, Eto Y: Mutation prevalence among 47 unrelated Japanese patients with Gaucher disease: identification of four novel mutations. J Inherit Metab Dis. 1997 Mar;20(1):67-73. [PubMed Link Image]
  36. Uyama E, Uchino M, Ida H, Eto Y, Owada M: D409H/D409H genotype in Gaucher-like disease. J Med Genet. 1997 Feb;34(2):175. [PubMed Link Image]
  37. Demina A, Beutler E: Six new Gaucher disease mutations. Acta Haematol. 1998;99(2):80-2. [PubMed Link Image]
  38. Germain DP, Puech JP, Caillaud C, Kahn A, Poenaru L: Exhaustive screening of the acid beta-glucosidase gene, by fluorescence-assisted mismatch analysis using universal primers: mutation profile and genotype/phenotype correlations in Gaucher disease. Am J Hum Genet. 1998 Aug;63(2):415-27. [PubMed Link Image]
  39. Choy FY, Humphries ML, Ben-Yoseph Y: Gaucher type 2 disease: identification of a novel transversion mutation in a French-Irish patient. Am J Med Genet. 1998 Jun 16;78(1):92-3. [PubMed Link Image]
  40. Beutler E, Gelbart T: Hematologically important mutations: Gaucher disease. Blood Cells Mol Dis. 1998 Mar;24(1):2-8. [PubMed Link Image]
  41. Sinclair G, Choy FY, Humphries L: A novel complex allele and two new point mutations in type 2 (acute neuronopathic) Gaucher disease. Blood Cells Mol Dis. 1998 Dec;24(4):420-7. [PubMed Link Image]
  42. Parenti G, Filocamo M, Titomanlio L, Rizzolo G, Silvestro E, Perretti A, Gatti R, Andria G: A novel mutation of the beta-glucocerebrosidase gene associated with neurologic manifestations in three sibs. Clin Genet. 1998 Apr;53(4):281-5. [PubMed Link Image]
  43. Cormand B, Grinberg D, Gort L, Chabas A, Vilageliu L: Molecular analysis and clinical findings in the Spanish Gaucher disease population: putative haplotype of the N370S ancestral chromosome. Hum Mutat. 1998;11(4):295-305. [PubMed Link Image]
  44. Wasserstein MP, Martignetti JA, Zeitlin R, Lumerman H, Solomon M, Grace ME, Desnick RJ: Type 1 Gaucher disease presenting with extensive mandibular lytic lesions: identification and expression of a novel acid beta-glucosidase mutation. Am J Med Genet. 1999 Jun 4;84(4):334-9. [PubMed Link Image]
  45. Choy FY, Wong K, Shi HP: Glucocerebrosidase mutations among Chinese neuronopathic and non-neuronopathic Gaucher disease patients. Am J Med Genet. 1999 Jun 11;84(5):484-6. [PubMed Link Image]
  46. Hodanov inverted question mark K, Hrebicek M, Cervenkov inverted question mark M, Mr inverted question markzov inverted question mark L, Veprekov inverted question mark L, Zemen J: Analysis of the beta-glucocerebrosidase gene in Czech and Slovak Gaucher patients: mutation profile and description of six novel mutant alleles. Blood Cells Mol Dis. 1999 Oct-Dec;25(5-6):287-98. [PubMed Link Image]
  47. Stone DL, van Diggelen OP, de Klerk JB, Gaillard JL, Niermeijer MF, Willemsen R, Tayebi N, Sidransky E: Is the perinatal lethal form of Gaucher disease more common than classic type 2 Gaucher disease? Eur J Hum Genet. 1999 May-Jun;7(4):505-9. [PubMed Link Image]
  48. Sarria AJ, Giraldo P, Perez-Calvo JI, Pocovi M: Detection of three rare (G377S, T134P and 1451delAC), and two novel mutations (G195W and Rec[1263del55;1342G>C]] in Spanish Gaucher disease patients. Mutation in brief no. 251. Online. Hum Mutat. 1999;14(1):88. [PubMed Link Image]
Enzyme 8 Metabolite References Not Available
Enzyme 9 [top]
Enzyme 9 ID 8417
Enzyme 9 Name Glucokinase regulatory protein
Enzyme 9 Synonyms
  1. Glucokinase regulator
Enzyme 9 Gene Name GCKR
Enzyme 9 Protein Sequence >Glucokinase regulatory protein 
MPGTKRFQHVIETPEPGKWELSGYEAAVPITEKSNPLTQDLDKADAENIVRLLGQCDAEI
FQEEGQALSTYQRLYSESILTTMVQVAGKVQEVLKEPDGGLVVLSGGGTSGRMAFLMSVS
FNQLMKGLGQKPLYTYLIAGGDRSVVASREGTEDSALHGIEELKKVAAGKKRVIVIGISV
GLSAPFVAGQMDCCMNNTAVFLPVLVGFNPVSMARNDPIEDWSSTFRQVAERMQKMQEKQ
KAFVLNPAIGPEGLSGSSRMKGGSATKILLETLLLAAHKTVDQGIAASQRCLLEILRTFE
RAHQVTYSQSPKIATLMKSVSTSLEKKGHVYLVGWQTLGIIAIMDGVECIHTFGADFRDV
RGFLIGDHSDMFNQKAELTNQGPQFTFSQEDFLTSILPSLTEIDTVVFIFTLDDNLTEVQ
TIVEQVKEKTNHIQALAHSTVGQTLPIPLKKLFPSIISITWPLLFFEYEGNFIQKFQREL
STKWVLNTVSTGAHVLLGKILQNHMLDLRISNSKLFWRALAMLQRFSGQSKARCIESLLR
AIHFPQPLSDDIRAAPISCHVQVAHEKEQVIPIALLSLLFRCSITEAQAHLAAAPSVCEA
VRSALAGPGQKRTADPLEILEPDVQ
Enzyme 9 Number of Residues 625
Enzyme 9 Molecular Weight 68686
Enzyme 9 Theoretical pI 6.68
Enzyme 9 GO Classification
Function
  • enzyme regulator activity
Process
—
Component
—
Enzyme 9 General Function Not Available
Enzyme 9 Specific Function Inhibits glucokinase by forming an inactive complex with this enzyme
Enzyme 9 Pathways Not Available
Enzyme 9 Reactions Not Available
Enzyme 9 Pfam Domain Function Not Available
Enzyme 9 Signals
  • None
Enzyme 9 Transmembrane Regions
  • None
Enzyme 9 Essentiality Not Available
Enzyme 9 GenBank ID Protein 683572 Link Image
Enzyme 9 UniProtKB/Swiss-Prot ID Q14397 Link Image
Enzyme 9 UniProtKB/Swiss-Prot Entry Name GCKR_HUMAN Link Image
Enzyme 9 PDB ID Not Available
Enzyme 9 Cellular Location Not Available
Enzyme 9 Gene Sequence >1878 bp 
ATGCCAGGCACAAAACGGTTTCAACATGTCATTGAGACCCCGGAGCCTGGCAAGTGGGAG
TTGTCTGGGTACGAGGCAGCTGTGCCAATCACGGAGAAGTCAAACCCACTGACCCAGGAT
CTAGACAAAGCAGATGCTGAGAACATTGTTCGACTGCTAGGGCAATGTGATGCTGAGATC
TTCCAGGAGGAGGGGCAAGCCCTGTCCACATACCAGAGACTCTACAGCGAATCCATTCTG
ACCACCATGGTACAGGTGGCTGGGAAAGTTCAGGAAGTGCTGAAGGAGCCAGATGGGGGG
CTGGTTGTGCTGAGTGGAGGGGGCACCTCTGGCCGGATGGCATTCCTCATGTCGGTGTCC
TTTAATCAGCTGATGAAAGGTCTGGGACAGAAACCTCTTTACACCTACCTCATTGCAGGT
GGTGACAGGTCTGTGGTGGCCTCTAGGGAGGGGACAGAAGATAGTGCCTTGCACGGGATT
GAGGAACTGAAGAAGGTGGCTGCCGGGAAGAAGAGAGTGATTGTCATTGGCATTTCTGTG
GGACTCTCTGCTCCCTTTGTGGCAGGCCAGATGGACTGCTGCATGAACAACACAGCTGTC
TTCTTGCCAGTCCTGGTTGGCTTCAATCCAGTGAGCATGGCCAGAAATGACCCCATTGAA
GACTGGAGTTCAACATTCCGACAAGTAGCAGAGCGGATGCAGAAAATGCAGGAGAAACAG
AAAGCTTTTGTGCTCAATCCTGCCATCGGGCCCGAGGGTCTCAGCGGCTCCTCCCGGATG
AAAGGTGGAAGTGCCACCAAGATTCTGCTGGAAACCCTGTTATTAGCAGCCCATAAGACT
GTGGACCAGGGCATTGCAGCATCTCAAAGATGCCTCCTGGAAATCTTGCGGACATTTGAG
CGAGCTCATCAGGTGACCTACAGCCAAAGCCCCAAGATTGCCACCCTGATGAAGAGTGTC
AGCACCAGTCTGGAGAAGAAAGGCCACGTGTACCTGGTTGGCTGGCAGACCCTGGGTATC
ATTGCCATCATGGATGGAGTAGAGTGCATCCACACCTTTGGTGCTGATTTCCGAGATGTC
CGTGGCTTTCTCATTGGTGATCACAGTGACATGTTTAACCAGAAGGCTGAGCTCACCAAC
CAGGGTCCCCAGTTCACCTTCTCCCAGGAGGACTTCCCGACTTCCATCCTTCCCTCTCTC
ACGGAAATCGATACTGTGGTCTTCATTTTCACCCTGGATGACAACCTCACGGAGGTGCAG
ACTATAGTGGAGCAGGTGAAAGAGAAGACCAACCACATCCAGGCCCTGGCACACAGCACC
GTGGGTCAGACCTTGCCGATCCCTCTGAAGAAGCTCTTTCCCTCCATCATCAGCATCACA
TGGCCACTGCTTTTCTTTGAATATGAAGGGAACTTCATCCAGAAGTTCCAGCGTGAGCTA
AGCACCAAATGGGTGCTGAATACAGTGAGTACAGGTGCTCATGTGCTTCTTGGTAAGATC
CTACAAAACCACATGTTGGACCTTCGGATTAGCAACTCCAAGCTCTTCTGGCGGGCGCTG
GCCATGCTGCAGCGGTTCTCTGGACAGTCCAAGGCTCGATGCATCGAGAGCCTCCTCCGA
GCGATCCACTTTCCCCAGCCACTGTCAGATGATATTCGGGCTGCTCCCATCTCCTGCCGT
GTCCAGGTTGCACATGAGAAGGAACAGGTGATACCCATCGCCTTGCTGAGCCTCCTATTC
CGGTGCTCGATCACTGAGGCTCAGGCACACCTGGCTGCAGCTCCTTCTGTCTGTGAGGCT
GTCAGGAGTGCTCTTGCTGGGCCAGGTCAGAAGCGCACTGCGGACCCCCTCGAGATCCTA
GAGCCTGACGTTCAGTGA
Enzyme 9 GenBank Gene ID Z48475 Link Image
Enzyme 9 GeneCard ID GCKR Link Image
Enzyme 9 GenAtlas ID GCKR Link Image
Enzyme 9 HGNC ID HGNC:4196 Link Image
Enzyme 9 Chromosome Location 2
Enzyme 9 Locus 2p23
Enzyme 9 SNPs SNPJam Report Link Image
Enzyme 9 General References
  1. Warner JP, Leek JP, Intody S, Markham AF, Bonthron DT: Human glucokinase regulatory protein (GCKR): cDNA and genomic cloning, complete primary structure, and chromosomal localization. Mamm Genome. 1995 Aug;6(8):532-6. [PubMed Link Image]
  2. Hayward BE, Dunlop N, Intody S, Leek JP, Markham AF, Warner JP, Bonthron DT: Organization of the human glucokinase regulator gene GCKR. Genomics. 1998 Apr 1;49(1):137-42. [PubMed Link Image]
Enzyme 9 Metabolite References Not Available
Enzyme 10 [top]
Enzyme 10 ID 8593
Enzyme 10 Name Cytosolic beta-glucosidase
Enzyme 10 Synonyms
  1. Cytosolic beta-glucosidase- like protein 1
Enzyme 10 Gene Name GBA3
Enzyme 10 Protein Sequence >Cytosolic beta-glucosidase 
MAFPAGFGWAAATAAYQVEGGWDADGKGPCVWDTFTHQGGERVFKNQTGDVACGSYTLWE
EDLKCIKQLGLTHYRFSLSWSRLLPDGTTGFINQKGIDYYNKIIDDLLKNGVTPIVTLYH
FDLPQTLEDQGGWLSEAIIESFDKYAQFCFSTFGDRVKQWITINEANVLSVMSYDLGMFP
PGIPHFGTGGYQAAHNLIKAHARSWHSYDSLFRKKQKGMVSLSLFAVWLEPADPNSVSDQ
EAAKRAITFHLDLFAKPIFIDGDYPEVVKSQIASMSQKQGYPSSRLPEFTEEEKKMIKGT
ADFFAVQYYTTRLIKYQENKKGELGILQDAEIEFFPDPSWKNVDWIYVVPWGVCKLLKYI
KDTYNNPVIYITENGFPQSDPAPLDDTQRWEYFRQTFQELFKAIQLDKVNLQVYCAWSLL
DNFEWNQGYSSRFGLFHVDFEDPARPRVPYTSAKEYAKIIRNNGLEAHL
Enzyme 10 Number of Residues 469
Enzyme 10 Molecular Weight 53696
Enzyme 10 Theoretical pI 5.33
Enzyme 10 GO Classification
Function
  • catalytic activity
  • glucosidase activity
  • hydrolase activity
  • hydrolase activity, acting on glycosyl bonds
  • hydrolase activity, hydrolyzing O-glycosyl compounds
Process
  • carbohydrate metabolism
  • macromolecule metabolism
  • metabolism
  • physiological process
Component
—
Enzyme 10 General Function Carbohydrate transport and metabolism
Enzyme 10 Specific Function Glycosidase probably involved in the intestinal absorption and metabolism of dietary flavonoid glycosides. Able to hydrolyze a broad variety of glycosides including phytoestrogens, flavonols, flavones, flavanones and cyanogens
Enzyme 10 Pathways
  • Cyanoamino acid metabolism (map00460 Link Image)
  • Starch and Sucrose Metabolism (map00500 Link Image)
  • Stilbene, coumarine and lignin biosynthesis (map00940 Link Image)
Enzyme 10 Reactions
  • Hydrolysis of terminal, non-reducing beta-D-glucose residues with release of beta-D-glucose
Enzyme 10 Pfam Domain Function
Enzyme 10 Signals Not Available
Enzyme 10 Transmembrane Regions Not Available
Enzyme 10 Essentiality Not Available
Enzyme 10 GenBank ID Protein 11559218 Link Image
Enzyme 10 UniProtKB/Swiss-Prot ID Q9H227 Link Image
Enzyme 10 UniProtKB/Swiss-Prot Entry Name GBA3_HUMAN Link Image
Enzyme 10 PDB ID Not Available
Enzyme 10 Cellular Location Not Available
Enzyme 10 Gene Sequence >1410 bp 
ATGGCTTTCCCTGCAGGATTTGGATGGGCGGCAGCCACTGCAGCTTATCAAGTAGAAGGA
GGCTGGGATGCAGATGGAAAAGGCCCTTGTGTCTGGGACACATTTACTCATCAGGGAGGA
GAGAGAGTTTTCAAGAACCAGACTGGCGATGTAGCTTGTGGCAGCTACACTCTGTGGGAG
GAAGATTTGAAATGTATCAAACAGCTTGGATTGACTCATTACCGCTTCTCTCTTTCCTGG
TCACGTCTGTTACCTGATGGGACGACAGGTTTCATCAACCAGAAAGGAATTGATTATTAC
AACAAGATCATCGATGATTTGTTAAAAAATGGGGTTACTCCCATTGTGACCCTCTACCAC
TTTGATTTGCCTCAGACTTTAGAAGACCAAGGAGGTTGGTTGTCAGAGGCAATCATTGAA
TCCTTTGACAAATATGCTCAGTTTTGCTTCAGTACCTTTGGGGATCGTGTCAAGCAGTGG
ATCACCATAAATGAAGCTAATGTTCTTTCTGTGATGTCATATGACTTAGGTATGTTTCCT
CCGGGTATCCCTCACTTTGGGACTGGAGGTTATCAGGCAGCTCATAATTTGATTAAGGCT
CATGCCAGATCCTGGCACAGCTATGATTCCTTATTTCGAAAAAAGCAGAAAGGTATGGTG
TCTCTATCACTTTTTGCGGTCTGGTTGGAACCAGCAGATCCCAACTCAGTGTCTGACCAG
GAAGCTGCTAAAAGAGCCATCACTTTCCATCTGGATTTATTTGCTAAACCCATATTCATC
GATGGTGATTATCCTGAAGTTGTCAAGTCTCAGATTGCCTCCATGAGTCAAAAGCAAGGC
TATCCATCATCGAGGCTTCCAGAATTCACTGAAGAAGAGAAGAAAATGATCAAAGGCACT
GCTGATTTTTTTGCTGTGCAATATTATACAACTCGCTTAATCAAGTACCAGGAGAACAAG
AAAGGAGAACTAGGTATTCTCCAGGATGCGGAAATTGAATTTTTTCCAGATCCATCTTGG
AAAAATGTGGATTGGATCTACGTGGTACCATGGGGAGTATGTAAACTACTGAAATATATT
AAGGATACATATAATAACCCTGTAATTTACATCACTGAGAATGGGTTTCCCCAGAGTGAC
CCAGCGCCTCTTGATGACACTCAACGCTGGGAGTATTTCAGACAAACATTTCAGGAACTG
TTCAAAGCTATCCAACTTGATAAAGTCAATCTTCAAGTATATTGTGCATGGTCTCTTCTG
GATAACTTTGAGTGGAACCAGGGATACAGCAGCCGGTTTGGTCTCTTCCACGTTGATTTT
GAAGACCCAGCTAGACCCCGAGTCCCTTACACATCGGCCAAGGAATATGCCAAGATCATC
CGAAACAATGGCCTTGAAGCACATCTGTAG
Enzyme 10 GenBank Gene ID AB017913 Link Image
Enzyme 10 GeneCard ID GBA3 Link Image
Enzyme 10 GenAtlas ID GBA3 Link Image
Enzyme 10 HGNC ID HGNC:19069 Link Image
Enzyme 10 Chromosome Location 4
Enzyme 10 Locus 4p15.31
Enzyme 10 SNPs SNPJam Report Link Image
Enzyme 10 General References
  1. Yahata K, Mori K, Arai H, Koide S, Ogawa Y, Mukoyama M, Sugawara A, Ozaki S, Tanaka I, Nabeshima Y, Nakao K: Molecular cloning and expression of a novel klotho-related protein. J Mol Med. 2000;78(7):389-94. [PubMed Link Image]
  2. de Graaf M, van Veen IC, van der Meulen-Muileman IH, Gerritsen WR, Pinedo HM, Haisma HJ: Cloning and characterization of human liver cytosolic beta-glycosidase. Biochem J. 2001 Jun 15;356(Pt 3):907-10. [PubMed Link Image]
Enzyme 10 Metabolite References Not Available
Enzyme 11 [top]
Enzyme 11 ID 8603
Enzyme 11 Name Maltase-glucoamylase, intestinal [Includes: Maltase
Enzyme 11 Synonyms
  1. Alpha-glucosidase
  2. Glucoamylase
  3. Glucan 1,4-alpha- glucosidase]
Enzyme 11 Gene Name MGAM
Enzyme 11 Protein Sequence >Maltase-glucoamylase, intestinal [Includes: Maltase 
MARKKLKKFTTLEIVLSVLLLVLFIISIVLIVLLAKESLKSTAPDPGTTGTPDPGTTGTP
DPGTTGTTHARTTGPPDPGTTGTTPVSAECPVVNELERINCIPDQPPTKATCDQRGCCWN
PQGAVSVPWCYYSKNHSYHVEGNLVNTNAGFTARLKNLPSSPVFGSNVDNVLLTAEYQTS
NRFHFKLTDQTNNRFEVPHEHVQSFSGNAAASLTYQVEISRQPFSIKVTRRSNNRVLFDS
SIGPLLFADQFLQLSTRLPSTNVYGLGEHVHQQYRHDMNWKTWPIFNRDTTPNGNGTNLY
GAQTFFLCLEDASGLSFGVFLMNSNAMEVVLQPAPAITYRTIGGILDFYVFLGNTPEQVV
QEYLELIGRPALPSYWALGFHLSRYEYGTLDNMREVVERNRAAQLPYDVQHADIDYMDER
RDFTYDSVDFKGFPEFVNELHNNGQKLVIIVDPAISNNSSSSKPYGPYDRGSDMKIWVNS
SDGVTPLIGEVWPGQTVFPDYTNPNCAVWWTKEFELFHNQVEFDGIWIDMNEVSNFVDGS
VSGCSTNNLNNPPFTPRILDGYLFCKTLCMDAVQHWGKQYDIHNLYGYSMAVATAEAAKT
VFPNKRSFILTRSTFAGSGKFAAHWLGDNTATWDDLRWSIPGVLEFNLFGIPMVGPDICG
FALDTPEELCRRWMQLGAFYPFSRNHNGQGYKDQDPASFGADSLLLNSSRHYLNIRYTLL
PYLYTLFFRAHSRGDTVARPLLHEFYEDNSTWDVHQQFLWGPGLLITPVLDEGAEKVMAY
VPDAVWYDYETGSQVRWRKQKVEMELPGDKIGLHLRGGYIFPTQQPNTTTLASRKNPLGL
IIALDENKEAKGELFWDDGETKDTVANKVYLLCEFSVTQNRLEVNISQSTYKDPNNLAFN
EIKILGTEEPSNVTVKHNGVPSQTSPTVTYDSNLKVAIITDIDLLLGEAYTVEWSIKIRD
EEKIDCYPDENGASAENCTARGCIWEASNSSGVPFCYFVNDLYSVSDVQYNSHGATADIS
LKSSVYANAFPSTPVNPLRLDVTYHKNEMLQFKIYDPNKNRYEVPVPLNIPSMPSSTPEG
QLYDVLIKKNPFGIEIRRKSTGTIIWDSQLLGFTFSDMFIRISTRLPSKYLYGFGETEHR
SYRRDLEWHTWGMFSRDQPPGYKKNSYGVHPYYMGLEEDGSAHGVLLLNSNAMDVTFQPL
PALTYRTTGGVLDFYVFLGPTPELVTQQYTELIGRPVMVPYWSLGFQLCRYGYQNDSEIA
SLYDEMVAAQIPYDVQYSDIDYMERQLDFTLSPKFAGFPALINRMKADGMRVILILDPAI
SGNETQPYPAFTRGVEDDVFIKYPNDGDIVWGKVWPDFPDVVVNGSLDWDSQVELYRAYV
AFPDFFRNSTAKWWKREIEELYNNPQNPERSLKFDGMWIDMNEPSSFVNGAVSPGCRDAS
LNHPPYMPHLESRDRGLSSKTLCMESQQILPDGSLVQHYNVHNLYGWSQTRPTYEAVQEV
TGQRGVVITRSTFPSSGRWAGHWLGDNTAAWDQLKKSIIGMMEFSLFGISYTGADICGFF
QDAEYEMCVRWMQLGAFYPFSRNHNTIGTRRQDPVSWDVAFVNISRTVLQTRYTLLPYLY
TLMHKAHTEGVTVVRPLLHEFVSDQVTWDIDSQFLLGPAFLVSPVLERNARNVTAYFPRA
RWYDYYTGVDINARGEWKTLPAPLDHINLHVRGGYILPWQEPALNTHLSRQKFMGFKIAL
DDEGTAGGWLFWDDGQSIDTYGKGLYYLASFSASQNTMQSHIIFNNYITGTNPLKLGYIE
IWGVGSVPVTSVSISVSGMVITPSFNNDPTTQVLSIDVTDRNISLHNFTSLTWISTL
Enzyme 11 Number of Residues 1857
Enzyme 11 Molecular Weight 209855
Enzyme 11 Theoretical pI 5.14
Enzyme 11 GO Classification
Function
  • catalytic activity
  • hydrolase activity
  • hydrolase activity, acting on glycosyl bonds
  • hydrolase activity, hydrolyzing O-glycosyl compounds
Process
  • carbohydrate metabolism
  • macromolecule metabolism
  • metabolism
  • physiological process
Component
—
Enzyme 11 General Function Carbohydrate transport and metabolism
Enzyme 11 Specific Function May serve as an alternate pathway for starch digestion when luminal alpha-amylase activity is reduced because of immaturity or malnutrition. May play a unique role in the digestion of malted dietary oligosaccharides used in food manufacturing
Enzyme 11 Pathways
Enzyme 11 Reactions
  • Hydrolysis of terminal, non-reducing 1,4-linked alpha-D-glucose residues with release of alpha-D-glucose
Enzyme 11 Pfam Domain Function
Enzyme 11 Signals
  • 1-35
Enzyme 11 Transmembrane Regions
  • 14-34
Enzyme 11 Essentiality Not Available
Enzyme 11 GenBank ID Protein 17648144 Link Image
Enzyme 11 UniProtKB/Swiss-Prot ID O43451 Link Image
Enzyme 11 UniProtKB/Swiss-Prot Entry Name MGA_HUMAN Link Image
Enzyme 11 PDB ID Not Available
Enzyme 11 Cellular Location Not Available
Enzyme 11 Gene Sequence >5574 bp 
ATGGCAAGAAAGAAGCTGAAAAAATTTACTACTTTGGAGATTGTGCTCAGTGTTCTTCTG
CTTGTGTTGTTTATCATCAGTATTGTTCTAATTGTGCTTTTAGCCAAAGAGTCACTGAAA
TCAACAGCCCCAGATCCTGGGACAACTGGTACCCCAGATCCTGGGACAACTGGTACCCCA
GATCCTGGAACAACTGGTACCACACATGCTAGGACAACGGGTCCCCCAGATCCTGGAACA
ACTGGTACCACTCCTGTTTCTGCTGAATGTCCAGTGGTAAATGAATTGGAACGAATTAAT
TGCATCCCTGACCAGCCGCCAACAAAGGCCACATGTGACCAACGTGGCTGTTGCTGGAAT
CCCCAGGGAGCTGTAAGTGTTCCCTGGTGCTACTATTCCAAGAATCATAGCTACCATGTA
GAGGGCAACCTTGTCAACACAAATGCAGGATTCACAGCCCGGTTGAAAAATCTGCCTTCT
TCACCAGTGTTTGGAAGCAATGTTGACAATGTTCTTCTCACAGCAGAATATCAGACATCT
AATCGTTTCCACTTTAAGTTGACTGACCAAACCAATAACAGGTTTGAAGTGCCCCACGAA
CACGTGCAGTCCTTCAGTGGAAATGCTGCTGCTTCTTTGACCTACCAAGTTGAAATCTCC
AGACAGCCATTTAGCATCAAAGTGACCAGAAGAAGCAACAATCGTGTTTTGTTTGACTCG
AGCATTGGGCCCCTACTGTTTGCTGACCAGTTCTTGCAGCTCTCCACTCGACTGCCTAGC
ACTAACGTGTATGGCCTGGGAGAGCATGTGCACCAGCAGTATCGGCATGATATGAATTGG
AAGACCTGGCCCATATTTAACAGAGACACAACTCCCAATGGAAACGGAACTAATTTGTAT
GGTGCGCAGACATTCTTCTTGTGCCTTGAAGATGCTAGTGGATTGTCCTTTGGGGTGTTT
CTGATGAACAGCAATGCCATGGAGGTTGTCCTTCAGCCTGCGCCAGCCATCACTTACCGC
ACCATTGGGGGCATTCTCGACTTCTATGTGTTCTTGGGAAACACTCCAGAGCAAGTTGTT
CAAGAATATCTAGAGCTCATTGGGCGGCCAGCCCTTCCCTCCTACTGGGCGCTTGGATTT
CACCTCAGTCGTTACGAATATGGAACCTTAGACAACATGAGGGAAGTCGTGGAGAGAAAT
CGCGCAGCACAGCTCCCTTATGATGTTCAGCATGCTGATATTGATTATATGGATGAGAGA
AGGGACTTCACTTATGATTCAGTGGATTTTAAAGGCTTCCCTGAATTTGTCAACGAGTTA
CACAATAATGGACAGAAGCTTGTCATCATTGTGGATCCAGCCATCTCCAACAACTCTTCC
TCAAGTAAACCCTATGGCCCATATGACAGGGGTTCAGATATGAAGATATGGGTGAATAGT
TCAGATGGAGTGACTCCACTCATTGGGGAGGTCTGGCCTGGACAAACTGTGTTTCCTGAT
TATACCAATCCCAACTGTGCTGTTTGGTGGACAAAGGAATTTGAGCTTTTTCACAATCAA
GTAGAGTTTGATGGAATCTGGATTGATATGAATGAAGTCTCCAACTTTGTTGATGGTTCG
GTCTCAGGATGTTCCACAAACAACCTAAATAATCCCCCATTCACTCCCAGAATCCTGGAT
GGGTACCTGTTCTGCAAGACTCTCTGTATGGATGCAGTGCAGCACTGGGGCAAGCAGTAT
GACATTCACAATCTGTATGGCTACTCCATGGCGGTCGCCACAGCAGAAGCTGCCAAGACT
GTGTTCCCTAATAAGAGAAGCTTCATTCTGACCCGTTCTACCTTTGCGGGCTCTGGCAAG
TTTGCAGCACATTGGTTAGGAGACAACACTGCCACCTGGGATGACCTGAGATGGTCCATC
CCTGGCGTGCTTGAGTTCAACCTTTTTGGCATCCCAATGGTGGGTCCTGACATATGTGGC
TTTGCTTTGGACACCCCTGAGGAGCTCTGTAGGCGGTGGATGCAGTTGGGTGCATTTTAT
CCGTTTTCTAGAAATCACAATGGCCAAGGCTACAAGGACCAGGATCCTGCCTCCTTTGGA
GCTGACTCCCTGCTGTTGAATTCCTCCAGGCACTACCTTAACATCCGCTATACTCTATTG
CCCTACCTATACACCCTTTTCTTCCGTGCTCACAGCCGAGGGGACACGGTGGCCAGGCCC
CTTTTGCATGAGTTCTACGAGGACAACAGCACTTGGGATGTGCACCAACAGTTCTTATGG
GGGCCCGGCCTCCTCATCACTCCAGTTCTGGATGAAGGTGCAGAGAAAGTGATGGCATAT
GTGCCTGATGCTGTCTGGTATGACTACGAGACTGGGAGCCAAGTGAGATGGAGGAAGCAA
AAAGTCGAGATGGAACTTCCTGGAGACAAAATTGGACTTCACCTTCGAGGAGGCTACATC
TTCCCCACACAGCAGCCAAATACAACCACTCTGGCCAGTCGAAAGAACCCTCTTGGTCTT
ATCATTGCCCTAGATGAGAACAAAGAAGCAAAAGGAGAACTTTTCTGGGATGATGGGGAA
ACGAAGGATACTGTGGCCAATAAAGTGTATCTTTTATGTGAGTTTTCTGTCACTCAAAAC
CGCTTGGAGGTGAATATTTCACAATCAACCTACAAGGACCCCAATAATTTAGCATTTAAT
GAGATTAAAATTCTTGGGACGGAGGAACCTAGCAATGTTACAGTGAAACACAATGGTGTC
CCAAGTCAGACTTCTCCTACAGTCACTTATGATTCTAACCTGAAGGTTGCCATTATCACA
GATATTGATCTTCTCCTGGGAGAAGCATACACAGTGGAATGGAGCATAAAGATAAGGGAT
GAAGAAAAAATAGACTGTTACCCTGATGAGAATGGTGCTTCTGCCGAAAACTGCACTGCC
CGTGGCTGTATCTGGGAGGCATCCAATTCTTCTGGAGTCCCTTTTTGCTATTTTGTCAAC
GACCTATACTCTGTCAGTGATGTTCAGTATAATTCCCATGGGGCCACAGCTGACATCTCC
TTAAAGTCTTCCGTTTATGCCAATGCCTTCCCCTCCACACCCGTGAACCCCCTTCGCCTG
GATGTCACTTACCATAAGAATGAAATGCTGCAGTTCAAGATTTATGATCCCAACAAGAAT
CGGTATGAAGTTCCAGTCCCTCTGAACATACCCAGCATGCCATCCAGCACCCCTGAGGGT
CAACTCTATGATGTGCTCATTAAGAAGAATCCATTTGGGATTGAAATTCGCCGGAAGAGT
ACAGGCACTATAATTTGGGACTCTCAGCTCCTTGGCTTTACCTTCAGTGACATGTTTATC
CGCATCTCCACCCGCCTTCCCTCCAAGTACCTCTATGGCTTTGGGGAAACTGAGCACAGG
TCCTATAGGAGAGACTTGGAGTGGCACACTTGGGGGATGTTCTCCCGAGACCAGCCCCCA
GGGTACAAGAAGAATTCCTATGGTGTCCACCCCTACTACATGGGGCTGGAGGAGGACGGC
AGTGCCCATGGAGTGCTCCTGCTGAACAGCAATGCCATGGATGTGACGTTCCAGCCCCTG
CCTGCCTTGACATACCGCACCACAGGGGGAGTTCTGGACTTTTATGTGTTCTTGGGGCCG
ACTCCAGAGCTTGTCACCCAGCAGTACACTGAGTTGATTGGCCGGCCTGTGATGGTACCT
TACTGGTCTTTGGGGTTCCAGCTGTGTCGCTATGGCTACCAGAATGACTCTGAGATCGCC
AGCTTGTATGATGAGATGGTGGCTGCCCAGATCCCTTATGATGTGCAGTACTCAGACATC
GACTACATGGAGCGGCAGCTGGACTTCACCCTCAGCCCCAAGTTTGCTGGGTTTCCAGCT
CTGATCAATCGCATGAAGGCTGATGGGATGCGGGTCATCCTCATTCTGGATCCAGCCATT
TCTGGCAATGAGACACAGCCTTATCCTGCCTTCACTCGGGGCGTGGAGGATGACGTCTTC
ATCAAATACCCAAATGATGGAGACATTGTCTGGGGAAAGGTCTGGCCTGATTTTCCTGAT
GTTGTTGTGAATGGGTCTCTAGACTGGGACAGCCAAGTGGAGCTATATCGAGCTTATGTG
GCCTTCCCAGACTTTTTCCGTAATTCAACTGCCAAGTGGTGGAAGAGGGAAATAGAAGAA
CTATACAACAATCCACAGAATCCAGAGAGGAGCTTGAAGTTTGATGGCATGTGGATTGAT
ATGAATGAACCATCAAGCTTCGTGAATGGGGCAGTTTCTCCAGGCTGCAGGGACGCCTCT
CTGAACCACCCTCCCTACATGCCACATTTGGAGTCCAGGGACAGGGGCCTGAGCAGCAAG
ACCCTTTGTATGGAGAGTCAGCAGATCCTCCCAGACGGCTCCCTGGTGCAGCACTACAAC
GTGCACAACCTGTATGGGTGGTCCCAGACCAGACCCACATACGAAGCCGTGCAGGAGGTG
ACGGGACAGCGAGGGGTCGTCATCACCCGCTCCACATTTCCCTCTTCTGGCCGCTGGGCA
GGACATTGGCTGGGAGACAACACGGCCGCATGGGATCAGCTGAAGAAGTCTATCATTGGC
ATGATGGAGTTCAGCCTCTTCGGCATATCCTATACGGGAGCAGATATCTGTGGGTTCTTT
CAAGATGCTGAATATGAGATGTGTGTTCGCTGGATGCAGCTGGGGGCCTTTTACCCCTTC
TCAAGAAACCACAACACCATTGGGACCAGGAGACAAGACCCTGTGTCCTGGGATGTTGCT
TTTGTGAATATTTCCAGAACTGTCCTGCAGACCAGATACACCCTGTTGCCATATCTGTAT
ACCTTGATGCATAAGGCCCACACGGAGGGCGTCACTGTTGTGCGGCCTCTGCTCCATGAA
TTTGTGTCAGACCAGGTGACATGGGACATAGACAGTCAGTTCCTGCTGGGCCCAGCCTTC
CTGGTCAGCCCTGTCCTGGAGCGTAATGCCAGAAATGTCACTGCATATTTCCCTAGAGCC
CGCTGGTATGATTACTACACGGGTGTGGATATTAATGCAAGAGGAGAGTGGAAGACCTTG
CCAGCCCCTCTTGACCACATTAATCTTCATGTCCGTGGGGGCTACATCCTGCCCTGGCAA
GAGCCTGCACTGAACACCCACTTAAGCCGCCAGAAATTCATGGGCTTCAAAATTGCCTTG
GATGATGAAGGAACTGCTGGGGGCTGGCTCTTCTGGGATGATGGGCAAAGCATTGATACC
TATGGGAAAGGACTCTATTACTTGGCCAGCTTTTCTGCCAGCCAGAATACGATGCAAAGC
CATATAATTTTCAACAATTACATCACTGGTACAAATCCTTTGAAACTGGGCTACATTGAA
ATCTGGGGAGTGGGCAGTGTCCCCGTTACCAGTGTCAGCATCTCTGTGAGTGGCATGGTC
ATAACACCCTCCTTCAACAATGACCCCACGACACAGGTATTAAGCATCGATGTGACTGAC
AGAAACATCAGCCTACATAATTTTACTTCATTGACGTGGATAAGCACTCTGTGA
Enzyme 11 GenBank Gene ID AF016833 Link Image
Enzyme 11 GeneCard ID MGAM Link Image
Enzyme 11 GenAtlas ID MGAM Link Image
Enzyme 11 HGNC ID HGNC:7043 Link Image
Enzyme 11 Chromosome Location 7
Enzyme 11 Locus 7q34
Enzyme 11 SNPs SNPJam Report Link Image
Enzyme 11 General References
  1. Nichols BL, Eldering J, Avery S, Hahn D, Quaroni A, Sterchi E: Human small intestinal maltase-glucoamylase cDNA cloning. Homology to sucrase-isomaltase. J Biol Chem. 1998 Jan 30;273(5):3076-81. [PubMed Link Image]
  2. Naim HY, Sterchi EE, Lentze MJ: Structure, biosynthesis, and glycosylation of human small intestinal maltase-glucoamylase. J Biol Chem. 1988 Dec 25;263(36):19709-17. [PubMed Link Image]
  3. Danielsen EM: Tyrosine sulfation, a post-translational modification of microvillar enzymes in the small intestinal enterocyte. EMBO J. 1987 Oct;6(10):2891-6. [PubMed Link Image]
Enzyme 11 Metabolite References Not Available
Enzyme 12 [top]
Enzyme 12 ID 12896
Enzyme 12 Name Aldose 1-epimerase
Enzyme 12 Synonyms
  1. Galactose mutarotase
Enzyme 12 Gene Name GALM
Enzyme 12 Protein Sequence >Aldose 1-epimerase 
MASVTRAVFGELPSGGGTVEKFQLQSDLLRVDIISWGCTITALEVKDRQGRASDVVLGFA
ELEGYLQKQPYFGAVIGRVANRIAKGTFKVDGKEYHLAINKEPNSLHGGVRGFDKVLWTP
RVLSNGVQFSRISPDGEEGYPGELKVWVTYTLDGGELIVNYRAQASQATPVNLTNHSYFN
LAGQASPNINDHEVTIEADTYLPVDETLIPTGEVAPVQGTAFDLRKPVELGKHLQDFHLN
GFDHNFCLKGSKEKHFCARVHHAASGRVLEVYTTQPGVQFYTGNFLDGTLKGKNGAVYPK
HSGFCLETQNWPDAVNQPRFPPVLLRPGEEYDHTTWFKFSVA
Enzyme 12 Number of Residues 342
Enzyme 12 Molecular Weight 37766
Enzyme 12 Theoretical pI Not Available
Enzyme 12 GO Classification
Function
  • aldose 1-epimerase activity
  • catalytic activity
  • isomerase activity
  • racemase and epimerase activity
  • racemase and epimerase activity, acting on carbohydrates and derivatives
Process
  • alcohol metabolism
  • cellular metabolism
  • galactose metabolism
  • hexose metabolism
  • metabolism
  • monosaccharide metabolism
  • physiological process
Component
—
Enzyme 12 General Function Carbohydrate transport and metabolism
Enzyme 12 Specific Function Mutarotase converts alpha-aldose to the beta-anomer. It is active on D-glucose, L-arabinose, D-xylose, D-galactose, maltose and lactose
Enzyme 12 Pathways
Enzyme 12 Reactions
  • alpha-D-glucose = beta-D-glucose [RN:R01602] ALL_REAC R01602
Enzyme 12 Pfam Domain Function
Enzyme 12 Signals
  • None
Enzyme 12 Transmembrane Regions
  • None
Enzyme 12 Essentiality Not Available
Enzyme 12 GenBank ID Protein Not Available
Enzyme 12 UniProtKB/Swiss-Prot ID Q96C23 Link Image
Enzyme 12 UniProtKB/Swiss-Prot Entry Name GALM_HUMAN Link Image
Enzyme 12 PDB ID 1SO0 Link Image
Enzyme 12 PDB File Show
Enzyme 12 3D Structure
Enzyme 12 Cellular Location Not Available
Enzyme 12 Gene Sequence Not Available
Enzyme 12 GenBank Gene ID AY064382 Link Image
Enzyme 12 GeneCard ID Not Available
Enzyme 12 GenAtlas ID GALM Link Image
Enzyme 12 HGNC ID HGNC:24063 Link Image
Enzyme 12 Chromosome Location Not Available
Enzyme 12 Locus Not Available
Enzyme 12 SNPs SNPJam Report Link Image
Enzyme 12 General References Not Available
Enzyme 12 Metabolite References Not Available
Enzyme 13 [top]
Enzyme 13 ID 15209
Enzyme 13 Name cDNA FLJ78173, highly similar to Homo sapiens hexokinase 1 (HK1) mRNA
Enzyme 13 Synonyms Not Available
Enzyme 13 Gene Name Not Available
Enzyme 13 Protein Sequence >cDNA FLJ78173, highly similar to Homo sapiens hexokinase 1 (HK1) mRNA 
MIAAQLLAYYFTELKDDQVKKIDKYLYAMRLSDETLIDIMTRFRKEMKNGLSRDFNPTAT
VKMLPTFVRSIPDGSEKGDFIALDLGGSSFRILRVQVNHEKNQNVHMESEVYDTPENIVH
GSGSQLFDHVAECLGDFMEKRKIKDKKLPVGFTFSFPCQQSKIDEAILITWTKRFKASGV
EGADVVKLLNKAIKKRGDYDANIVAVVNDTVGTMMTCGYDDQHCEVGLIIGTGTNACYME
ELRHIDLVEGDEGRMCINTEWGAFGDDGSLEDIRTEFDREIDRGSLNPGKQLFEKMVSGM
YLGELVRLILVKMAKEGLLFEGRITPELLTRGKFNTSDVSAIEKNKEGLHNAKEILTRLG
VEPSDDDCVSVQHVCTIVSFRSANLVAATLGAILNRLRDNKGTPRLRTTVGVDGSLYKTH
PQYSRRFHKTLRRLVPDSDVRFLLSESGSGKGAAMVTAVAYRLAEQHRQIEETLAHFHLT
KDMLLEVKKRMRAEMELGLRKQTHNNAVVKMLPSFVRRTPDGTENGDFLALDLGGTNFRV
LLVKIRSGKKRTVEMHNKIYAIPIEIMQGTGEELFDHIVSCISDFLDYMGIKGPRMPLGF
TFSFPCQQTSLDAGILITWTKGFKATDCVGHDVVTLLRDAIKRREEFDLDVVAVVNDTVG
TMMTCAYEEPTCEVGLIVGTGSNACYMEEMKNVEMVEGDQGQMCINMEWGAFGDNGCLDD
IRTHYDRLVDEYSLNAGKQGYEKMISGMYLGEIVRNILIDFTKKGFLFRGQISETLKTRG
IFETKFLSQIESDRLALLQVRAILQQLGLNSTCDDSILVKTVCGVVSRRAAQLCGAGMAA
VVDKIRENRGLDRLNVTVGVDGTLYKLHPHFSRIMHQTVKELSPKCNVSFLLSEDGSGKG
AALITAVGVRLRTEASS
Enzyme 13 Number of Residues 917
Enzyme 13 Molecular Weight 102388
Enzyme 13 Theoretical pI 6.70
Enzyme 13 GO Classification Not Available
Enzyme 13 General Function Not Available
Enzyme 13 Specific Function Not Available
Enzyme 13 Pathways Not Available
Enzyme 13 Reactions Not Available
Enzyme 13 Pfam Domain Function Not Available
Enzyme 13 Signals
  • None
Enzyme 13 Transmembrane Regions
  • None
Enzyme 13 Essentiality Not Available
Enzyme 13 GenBank ID Protein 158257456 Link Image
Enzyme 13 UniProtKB/Swiss-Prot ID A8K7J7 Link Image
Enzyme 13 UniProtKB/Swiss-Prot Entry Name A8K7J7_HUMAN Link Image
Enzyme 13 PDB ID 1HKB Link Image
Enzyme 13 PDB File Show
Enzyme 13 3D Structure
Enzyme 13 Cellular Location Not Available
Enzyme 13 Gene Sequence >2754 bp 
ATGATCGCCGCGCAGCTCCTGGCCTATTACTTCACGGAGCTGAAGGATGACCAGGTCAAA
AAGATTGACAAGTATCTGTATGCCATGCGGCTCTCCGATGAAACTCTCATAGATATCATG
ACTCGCTTCAGGAAGGAGATGAAGAATGGCCTCTCCCGGGATTTTAATCCAACAGCCACA
GTCAAGATGTTGCCAACATTCGTAAGGTCCATTCCTGATGGCTCTGAAAAGGGAGATTTC
ATTGCCCTGGATCTTGGTGGGTCTTCCTTTCGAATTCTGCGGGTGCAAGTGAATCATGAG
AAAAACCAGAATGTTCACATGGAGTCCGAGGTTTATGACACCCCAGAGAACATCGTGCAC
GGCAGTGGAAGCCAGCTTTTTGATCATGTTGCTGAGTGCCTGGGAGATTTCATGGAGAAA
AGGAAGATCAAGGACAAGAAGTTACCTGTGGGATTCACGTTTTCTTTTCCTTGCCAACAA
TCCAAAATAGATGAGGCCATCCTGATCACCTGGACAAAGCGATTTAAAGCGAGCGGAGTG
GAAGGAGCAGATGTGGTCAAACTGCTTAACAAAGCCATCAAAAAGCGAGGGGACTATGAT
GCCAACATCGTAGCTGTGGTGAATGACACAGTGGGCACCATGATGACCTGTGGCTATGAC
GACCAGCACTGTGAAGTCGGCCTGATCATCGGCACTGGCACCAATGCTTGCTACATGGAG
GAACTGAGGCACATTGATCTGGTGGAAGGAGACGAGGGGAGGATGTGTATCAATACAGAA
TGGGGAGCCTTTGGAGACGATGGATCATTAGAAGACATCCGGACAGAGTTTGACAGGGAG
ATAGACCGGGGATCCCTCAACCCTGGAAAACAGCTGTTTGAGAAGATGGTCAGTGGCATG
TACTTGGGAGAGCTGGTTCGACTGATCCTAGTCAAGATGGCCAAGGAGGGCCTCTTATTT
GAAGGGCGGATCACCCCGGAGCTGCTCACCCGAGGGAAGTTTAACACCAGTGATGTGTCA
GCCATCGAAAAGAATAAGGAAGGCCTCCACAATGCCAAAGAAATCCTGACCCGCCTGGGA
GTGGAGCCGTCCGATGATGACTGTGTCTCAGTCCAGCACGTTTGCACCATTGTCTCATTT
CGCTCAGCCAACTTGGTGGCTGCCACACTGGGCGCCATCTTGAACCGCCTGCGTGATAAC
AAGGGCACACCCAGGCTGCGGACCACGGTTGGTGTCGACGGATCTCTTTACAAGACGCAC
CCACAGTATTCCCGGCGTTTCCACAAGACTCTAAGGCGCTTGGTGCCAGACTCCGATGTG
CGCTTCCTCCTCTCGGAGAGTGGCAGCGGCAAGGGGGCTGCCATGGTGACGGCGGTGGCC
TACCGCTTGGCCGAGCAGCACCGGCAGATAGAGGAGACCCTGGCTCATTTCCACCTCACC
AAAGACATGCTGCTGGAGGTGAAGAAGAGGATGCGGGCCGAGATGGAGCTGGGGCTGAGG
AAGCAGACGCACAACAATGCCGTGGTTAAGATGCTGCCCTCCTTCGTCCGGAGAACTCCC
GACGGGACCGAGAATGGTGACTTCTTGGCCCTGGATCTTGGAGGAACCAATTTCCGTGTG
CTGCTGGTGAAAATCCGTAGTGGGAAAAAGAGAACGGTGGAAATGCACAACAAGATCTAC
GCCATTCCTATTGAAATCATGCAGGGCACTGGGGAAGAGCTGTTTGATCACATTGTCTCC
TGCATCTCTGACTTCTTGGACTACATGGGGATCAAAGGCCCCAGGATGCCTCTGGGCTTC
ACGTTCTCATTTCCCTGCCAGCAGACGAGTCTGGACGCGGGAATCTTGATCACGTGGACA
AAGGGTTTTAAGGCAACAGACTGCGTGGGCCACGATGTAGTCACCTTACTAAGGGATGCG
ATAAAAAGGAGAGAGGAATTTGACCTGGACGTGGTGGCTGTGGTCAACGACACAGTGGGC
ACCATGATGACCTGTGCTTATGAGGAGCCCACCTGTGAGGTTGGACTCATTGTTGGGACC
GGCAGCAATGCCTGCTACATGGAGGAGATGAAGAACGTGGAGATGGTGGAGGGGGACCAG
GGGCAGATGTGCATCAACATGGAGTGGGGGGCCTTTGGGGACAACGGGTGTCTGGATGAT
ATCAGGACACACTACGACAGACTGGTGGACGAATATTCCCTAAATGCTGGGAAACAAGGG
TATGAGAAGATGATCAGTGGTATGTACCTGGGTGAAATCGTCCGCAACATCTTAATCGAC
TTCACCAAGAAGGGATTCCTCTTCCGAGGGCAGATCTCTGAGACGCTGAAGACCCGGGGC
ATCTTTGAGACCAAGTTTCTCTCTCAGATCGAGAGTGACCGATTAGCACTGCTCCAGGTC
CGGGCTATCCTCCAGCAGCTAGGTCTGAATAGCACCTGCGATGACAGTATCCTCGTCAAG
ACAGTGTGCGGGGTGGTGTCCAGGAGGGCCGCACAGCTGTGTGGCGCAGGCATGGCTGCG
GTTGTGGATAAGATCCGCGAGAACAGAGGACTGGACCGTCTGAATGTGACTGTGGGAGTG
GACGGGACACTCTACAAGCTTCATCCACACTTCTCCAGAATCATGCACCAGACGGTGAAG
GAACTGTCACCAAAATGTAACGTGTCCTTCCTCCTGTCTGAGGATGGCAGCGGCAAGGGG
GCCGCCCTCATCACGGCCGTGGGCGTGCGGTTACGCACAGAGGCAAGCAGCTAA
Enzyme 13 GenBank Gene ID AK292012 Link Image
Enzyme 13 GeneCard ID A8K7J7 Link Image
Enzyme 13 GenAtlas ID Not Available
Enzyme 13 HGNC ID Not Available
Enzyme 13 Chromosome Location Not Available
Enzyme 13 Locus Not Available
Enzyme 13 SNPs Not Available
Enzyme 13 General References Not Available
Enzyme 13 Metabolite References Not Available
Enzyme 14 [top]
Enzyme 14 ID 15316
Enzyme 14 Name Putative uncharacterized protein LOC130589 (Galactose mutarotase) (Aldose 1-epimerase) (cDNA FLJ75695, highly similar to Homo sapiens galactose mutarotase (aldose 1-epimerase) (GALM), mRNA)
Enzyme 14 Synonyms Not Available
Enzyme 14 Gene Name LOC130589
Enzyme 14 Protein Sequence >Putative uncharacterized protein LOC130589 (Galactose mutarotase) (Aldose 1-epimerase) (cDNA FLJ75695, highly similar to Homo sapiens galactose mutarotase (aldose 1-epimerase) (GALM), mRNA) 
MASVTRAVFGELPSGGGTVEKFQLQSDLLRVDIISWGCTITALEVKDRQGRASDVVLGFA
ELEGYLQKQPYFGAVIGRVANRIAKGTFKVDGKEYHLAINKEPNSLHGGVRGFDKVLWTP
RVLSNGVQFSRISPDGEEGYPGELKVWVTYTLDGGELIVNYRAQASQATPVNLTNHSYFN
LAGQASPNINDHEVTIEADTYLPVDETLIPTGEVAPVQGTAFDLRKPVELGKHLQDFHLN
GFDHNFCLKGSKEKHFCARVHHAASGRVLEVYTTQPGVQFYTGNFLDGTLKGKNGAVYPK
HSGFCLETQNWPDAVNQPRFPPVLLRPGEEYDHTTWFKFSVA
Enzyme 14 Number of Residues 342
Enzyme 14 Molecular Weight 37766
Enzyme 14 Theoretical pI 6.65
Enzyme 14 GO Classification
Function
  • aldose 1-epimerase activity
  • catalytic activity
  • isomerase activity
  • racemase and epimerase activity
  • racemase and epimerase activity, acting on carbohydrates and derivatives
Process
  • alcohol metabolism
  • cellular metabolism
  • galactose metabolism
  • hexose metabolism
  • metabolism
  • monosaccharide metabolism
  • physiological process
Component
—
Enzyme 14 General Function Carbohydrate transport and metabolism
Enzyme 14 Specific Function Not Available
Enzyme 14 Pathways Not Available
Enzyme 14 Reactions Not Available
Enzyme 14 Pfam Domain Function
Enzyme 14 Signals
  • None
Enzyme 14 Transmembrane Regions
  • None
Enzyme 14 Essentiality Not Available
Enzyme 14 GenBank ID Protein 62702175 Link Image
Enzyme 14 UniProtKB/Swiss-Prot ID Q53RY1 Link Image
Enzyme 14 UniProtKB/Swiss-Prot Entry Name Q53RY1_HUMAN Link Image
Enzyme 14 PDB ID 1SO0 Link Image
Enzyme 14 PDB File Show
Enzyme 14 3D Structure
Enzyme 14 Cellular Location Not Available
Enzyme 14 Gene Sequence >1029 bp 
ATGGCTTCGGTGACCAGGGCCGTGTTTGGAGAGCTGCCCTCGGGAGGAGGGACAGTGGAG
AAGTTCCAGCTGCAGTCAGACCTCTTGAGAGTGGACATCATCTCCTGGGGCTGCACGATC
ACAGCCCTAGAGGTCAAAGACAGGCAGGGGAGAGCCTCGGACGTGGTGCTTGGCTTCGCC
GAGTTGGAAGGATACCTCCAAAAGCAGCCATACTTTGGAGCAGTTATTGGGAGGGTGGCC
AACCGAATCGCCAAAGGAACCTTCAAGGTGGATGGGAAGGAGTATCACCTGGCCATTAAC
AAGGAACCCAACAGTCTGCATGGAGGAGTCAGAGGGTTTGATAAAGTGCTCTGGACCCCT
CGGGTGCTGTCAAATGGCGTCCAGTTCTCGCGCATCAGTCCAGATGGTGAAGAAGGCTAC
CCCGGAGAGTTAAAAGTCTGGGTGACATACACCCTGGATGGCGGAGAGCTCATAGTCAAC
TACAGAGCACAAGCCAGTCAGGCCACACCAGTCAACCTGACCAACCATTCTTACTTCAAC
CTGGCAGGCCAGGCTTCCCCAAATATAAATGACCATGAAGTCACCATAGAAGCGGATACT
TATTTGCCTGTGGATGAAACCCTGATTCCTACAGGAGAAGTTGCCCCAGTGCAAGGCACT
GCATTCGACCTGAGAAAGCCAGTGGAGCTTGGAAAACACCTGCAGGACTTCCATCTCAAT
GGTTTTGACCACAATTTCTGTCTGAAGGGATCTAAAGAAAAGCATTTTTGTGCAAGGGTG
CATCATGCTGCAAGCGGGCGGGTACTAGAAGTATACACCACCCAGCCCGGGGTCCAGTTT
TACACGGGCAACTTCCTGGATGGCACATTAAAGGGCAAGAATGGAGCTGTCTATCCCAAG
CACTCCGGTTTCTGCCTGGAGACTCAGAACTGGCCTGATGCAGTCAATCAGCCCCGCTTC
CCTCCTGTGCTGCTGAGGCCTGGTGAGGAGTATGACCACACCACCTGGTTCAAGTTTTCT
GTGGCTTAA
Enzyme 14 GenBank Gene ID AC074366 Link Image
Enzyme 14 GeneCard ID Q53RY1 Link Image
Enzyme 14 GenAtlas ID LOC130589 Link Image
Enzyme 14 HGNC ID HGNC:24063 Link Image
Enzyme 14 Chromosome Location Not Available
Enzyme 14 Locus Not Available
Enzyme 14 SNPs SNPJam Report Link Image
Enzyme 14 General References Not Available
Enzyme 14 Metabolite References Not Available