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Human Metabolome Database Version 2.5

 

Showing metabocard for Alpha-Lactose (HMDB00186)

Legend: metabolite field enzyme field

Version 2.5
Creation Date 2005-11-16 15:48:42
Update Date 2009-05-05 20:57:45
Accession Number HMDB00186
Secondary Accession Numbers HMDB05761
Common Name Alpha-Lactose
Description alpha-Lactose is the major sugar present in milk and the main source of energy supplied to the newborn mammalian in its mother's milk. Lactose is also an important osmotic regulator of lactation. It is digested by the intestinal lactase (EC 3.2.1.108), an enzyme expressed in newborns. Its activity declines following weaning. As a result, adult mammals are normally lactose-intolerant and more than 75% of the human adult population suffers from lactase deficiency. Lactase deficiency is present in up to 80 percent of blacks and Latinos, and up to 100 percent of American Indians and Asians. Persons with lactose intolerance are unable to digest significant amounts of lactose. Common symptoms include abdominal pain and bloating, excessive flatus, and watery stool following the ingestion of foods containing lactose. A sizable number of adults believe they are lactose intolerant but do not actually have impaired lactose digestion, and some persons with lactase deficiency can tolerate moderate amounts of ingested lactose. A diagnosis of lactose intolerance can usually be made with a careful history supported by dietary manipulation. If necessary, diagnosis can be confirmed by using a breath hydrogen or lactose tolerance test. These mostly uncomfortable symptoms of lactose maldigestion are blamed for a variably dairy consumption. There is, however, emerging evidence that certain lactic acid-producing bacteria, which selectively consume prebiotics, may be beneficial against some lower intestinal diseases. Lactose maldigestion and lactose should perhaps be re-evaluated as a potential provider of such a prebiotic. Treatment consists primarily of avoiding lactose-containing foods. Lactase enzyme supplements may be helpful. The degree of lactose malabsorption varies greatly among patients with lactose intolerance, but most of them can ingest up to 350 mL of milk daily without symptoms. Lactose-intolerant patients must ensure adequate calcium intake. (PMID: 13130292, 12216958, 12197838, 12018807)
Synonyms
  1. (+)-lactose
  2. 1-beta-D-Galactopyranosyl-4-alpha-D-glucopyranose
  3. 4-O-Hexopyranosylhexose
  4. Aletobiose
  5. Anhydrous lactose
  6. Lactin
  7. Lactobiose
  8. Lactose
  9. Milk sugar
  10. Osmolactan
  11. Saccharum lactin
  12. 1-beta-delta-Galactopyranosyl-4-alpha-delta-glucopyranose
  13. a-Lactose
  14. Dilactose
  15. Fast-Flo Lactose
  16. Flowlac 100
  17. Galactinum
  18. Granulac 140M
  19. Lactin (carbohydrate)
  20. Lactohale 300
  21. Lactose Fast-flo
  22. Lactose anhydride
  23. Pharmatosa DCL 21
  24. Pharmatose 21
  25. Pharmatose 325M
  26. Pharmatose DCL 15
  27. Prismalac
  28. Respitose ML 003
  29. Respitose SV 003
  30. Sachelac
  31. Sorbalac 400
  32. Sorbolac 400
  33. Spherolac
  34. Super-Tab
  35. Tablettose
  36. Tablettose 70
  37. Tablettose 80
  38. Zeparox EP
  39. Glc-(4-1)Gal
  40. alpha-Lactose
Chemical IUPAC Name (2R,3S,4S,5R,6S)-2-(hydroxymethyl)-6-[(2R,3R,4S,5R,6S)-4,5,6-trihydroxy-2-(hydroxymethyl)oxan-3-yl]oxy-oxane-3,4,5-triol
Chemical Formula C12H22O11
Chemical Structure Structure
Chemical Taxonomy
Kingdom
  • Organic
Super Class
  • Carbohydrates and Carbohydrate conjugates
Class
  • Carbohydrates
Sub Class
  • Disaccharides
Family
  • Mammalian Metabolite
Species
  • hemiacetal
  • acetal
  • primary alcohol
  • secondary alcohol
  • 1,2-diol
  • heterocyclic compound
Biofunction
  • Component of Galactose metabolism
  • Component of Glycerolipid metabolism
  • Component of Glycosphingolipid metabolism
  • Component of Keratan sulfate biosynthesis
  • Component of N-Glycan biosynthesis
Application
Source
  • Endogenous
Average Molecular Weight 342.297
Monoisotopic Molecular Weight 342.116211
Isomeric SMILES OC[C@H]1O[C@@H](O[C@@H]2[C@@H](CO)O[C@H](O)[C@H](O)[C@H]2O)[C@H](O)[C@@H](O)[C@H]1O
Canonical SMILES OCC1OC(OC2C(CO)OC(O)C(O)C2O)C(O)C(O)C1O
KEGG Compound ID C00243 Link Image
BioCyc ID LACTOSE Link Image
BiGG ID 34366 Link Image
Wikipedia Link Lactose Link Image
NuGOwiki Link HMDB00186 Link Image
Metagene Link HMDB00186 Link Image
METLIN ID 267 Link Image
PubChem Compound 84571 Link Image
PubChem Substance 10220749 Link Image
ChEBI ID 36219 Link Image
CAS Registry Number 63-42-3
InChI Identifier InChI=1/C12H22O11/c13-1-3-5(15)6(16)9(19)12(22-3)23-10-4(2-14)21-11(20)8(18)7(10)17/h3-20H,1-2H2/t3-,4-,5+,6+,7-,8-,9-,10-,11+,12+/m1/s1
Synthesis Reference Ruffing, Anne; Mao, Zichao; Ruizhen Chen, Rachel. Metabolic engineering of Agrobacterium sp. for UDP-galactose regeneration and oligosaccharide synthesis. Metabolic Engineering (2006), 8(5), 465-473.
Melting Point (Experimental) 201-202 oC
Experimental Water Solubility 195 mg/mL at 20 oC [YALKOWSKY,SH & DANNENFELSER,RM (1992)] Source: PhysProp
Predicted Water Solubility 586.0 mg/mL [Predicted by ALOGPS] Calculated using ALOGPS
Physiological Charge 0
State Solid
Experimental LogP/Hydrophobicity Not Available Source: PhysProp
Predicted LogP/Hydrophobicity -5.03 [MEYLAN,WM & HOWARD,PH (1995)]; -4.3 [Predicted by PubChem via XLOGP]; -3.01 [Predicted by ALOGPS] Calculated using ALOGPS
Material Safety Data Sheet (MSDS)
MOL File Show
SDF File Show
PDB File Show
2D Structure
3D Structure
Experimental PDB ID 1DLL Link Image
Experimental PDB File Show
Experimental PDB Structure
Experimental 1H NMR Spectrum Download Spectrum
Download FID (Varian)
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Experimental 13C NMR Spectrum Download Spectrum
Download FID (Bruker)
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Experimental 13C HSQC Spectrum Download Spectrum
Download FID (Bruker)
Show Experimental Conditions Link Image
Predicted 1H NMR Spectrum Show Image
Show Peaklist
Predicted 13C NMR Spectrum Show Image
Show Peaklist
Mass Spectrum
Low Energy
Download File
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Medium Energy
Download File
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High Energy
Download File
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Simplified TOCSY Spectrum Show Image
Show Peaklist
BMRB Spectrum Show Image
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Cellular Location
  • Cytoplasm
  • Extracellular
  • golgi apparatus
  • lysosome
Biofluid Location
  • Urine
Tissue Location
Tissue References
Bladder
Gut
Intestine
Muscle
Platelet
Skin
Spleen
Concentrations (Normal)
Biofluid Urine
Value 6.08 +/- 6.07 umol/mmol creatinine
Age Infant:0-1 yr old
Sex Both
Patient information Normal
Comments Not Available
References
  • Shoemaker JD, Elliott WH: Automated screening of urine samples for carbohydrates, organic and amino acids after treatment with urease. J Chromatogr. 1991 Jan 2;562(1-2):125-38. [PubMed Link Image]
Biofluid Urine
Value 30.0 (13.0-49.0) umol/mmol creatinine
Age Infant:0-1 yr old
Sex Both
Patient information Normal
Comments Not Available
References
  • Geigy Scientific Tables, 8th Rev edition, pp. 130. Edited by C. Lentner, West Cadwell, N.J.: Medical education Div., Ciba-Geigy Corp. Basel, Switzerland c1981-1992.
Biofluid Urine
Value 1.45 (0.63-3.45) umol/mmol creatinine
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Geigy Scientific Tables, 8th Rev edition, pp. 130. Edited by C. Lentner, West Cadwell, N.J.: Medical education Div., Ciba-Geigy Corp. Basel, Switzerland c1981-1992.
Concentrations (Abnormal) Not Available
Associated Disorders Not Available
OMIM ID Not Available
Pathways
Name SMPDB Link KEGG Link
Galactose Metabolism SMP00043 Link Image map00052 Link Image
Lactose Degradation SMP00457 Link Image
Lactose Synthesis SMP00444 Link Image
General References
  1. Jung SK, Fujimoto D: A novel beta-galactoside-binding lectin in adult rat kidney. J Biochem (Tokyo). 1994 Sep;116(3):547-53. [PubMed Link Image]
  2. Oozeer R, Furet JP, Goupil-Feuillerat N, Anba J, Mengaud J, Corthier G: Differential activities of four Lactobacillus casei promoters during bacterial transit through the gastrointestinal tracts of human-microbiota-associated mice. Appl Environ Microbiol. 2005 Mar;71(3):1356-63. [PubMed Link Image]
  3. Dimopoulos MA, Anagnostopoulos A: Thalidomide in relapsed/refractory multiple myeloma: pivotal trials conducted outside the United States. Semin Hematol. 2003 Oct;40(4 Suppl 4):8-16. [PubMed Link Image]
  4. Muthusamy A, Erickson DR, Sheykhnazari M, Bhavanandan VP: Enhanced binding of modified pentosan polysulfate and heparin to bladder--a strategy for improved treatment of interstitial cystitis. Urology. 2006 Jan;67(1):209-13. [PubMed Link Image]
  5. Johnson JD, Simoons FJ, Hurwitz R, Grange A, Mitchell CH, Sinatra FR, Sunshine P, Robertson WV, Bennett PH, Kretchmer N: Lactose malabsorption among the Pima indians of Arizona. Gastroenterology. 1977 Dec;73(6):1299-304. [PubMed Link Image]
  6. Lustenberger RW: [A 23-year old patient with chronic diarrhea. Celiac disease and lactose intolerance] Schweiz Rundsch Med Prax. 2005 Feb 2;94(5):163-4. [PubMed Link Image]
  7. Sharma A, DiCioccio RA, Allen HJ: Identification and synthesis of a novel 15 kDa beta-galactoside-binding lectin in human leukocytes. Glycobiology. 1992 Aug;2(4):285-92. [PubMed Link Image]
  8. Rana SV, Bhasin DK, Vinayak VK: Lactose hydrogen breath test in Giardia lamblia-positive patients. Dig Dis Sci. 2005 Feb;50(2):259-61. [PubMed Link Image]
  9. Mitchell JD, Brand J, Halbisch J: Weight-gain inhibition by lactose in Australian Aboriginal children. A controlled trial of normal and lactose hydrolysed milk. Lancet. 1977 Mar 5;1(8010):500-2. [PubMed Link Image]
  10. Soupene E, van Heeswijk WC, Plumbridge J, Stewart V, Bertenthal D, Lee H, Prasad G, Paliy O, Charernnoppakul P, Kustu S: Physiological studies of Escherichia coli strain MG1655: growth defects and apparent cross-regulation of gene expression. J Bacteriol. 2003 Sep;185(18):5611-26. [PubMed Link Image]
  11. Yeoh E, Horowitz M, Russo A, Muecke T, Robb T, Chatterton B: The effects of abdominal irradiation for seminoma of the testis on gastrointestinal function. J Gastroenterol Hepatol. 1995 Mar-Apr;10(2):125-30. [PubMed Link Image]
  12. Bondesson E, Bengtsson T, Borgstrom L, Nilsson LE, Norrgren K, Olsson B, Svensson M, Wollmer P: Dose delivery late in the breath can increase dry powder aerosol penetration into the lungs. J Aerosol Med. 2005 Spring;18(1):23-33. [PubMed Link Image]
  13. Roberson CM: Lactose intolerance. Ala Nurse. 2004 Dec-2005 Feb;31(4):23-4; quiz 24. [PubMed Link Image]
  14. Kim KI, Lee WS, Benevenga NJ: Feeding diets containing high levels of milk products or cellulose decrease urease activity and ammonia production in rat intestine. J Nutr. 1998 Jul;128(7):1186-91. [PubMed Link Image]
  15. Gunther S, Patterson RE, Kristal AR, Stratton KL, White E: Demographic and health-related correlates of herbal and specialty supplement use. J Am Diet Assoc. 2004 Jan;104(1):27-34. [PubMed Link Image]
  16. Wikipedia Link Image
Metabolic Enzymes
  1. Lactase-phlorizin hydrolase precursor
  2. Alpha-lactalbumin precursor
  3. Beta-1,4-galactosyltransferase 1
  4. Beta-galactosidase precursor
  5. cDNA, FLJ93218, Homo sapiens UDP-Gal:betaGlcNAc beta 1,4- galactosyltransferase,polypeptide 1 (B4GALT1), mRNA (UDP-Gal:betaGlcNAc beta 1,4-galactosyltransferase, polypeptide 1, isoform CRA_a)
  6. cDNA FLJ38554 fis, clone HCHON2002496, highly similar to Beta-1,4-galactosyltransferase 2 (EC 2.4.1.-)
Enzyme 1 [top]
Enzyme 1 ID 5601
Enzyme 1 Name Lactase-phlorizin hydrolase precursor
Enzyme 1 Synonyms
  1. Lactase-glycosylceramidase[Includes: Lactase
Enzyme 1 Gene Name LCT
Enzyme 1 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 1 Number of Residues 1927
Enzyme 1 Molecular Weight 218604
Enzyme 1 Theoretical pI 6.30
Enzyme 1 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 1 General Function Carbohydrate transport and metabolism
Enzyme 1 Specific Function LPH splits lactose in the small intestine
Enzyme 1 Pathways
Enzyme 1 Reactions
  • lactose + H2O = D-galactose + D-glucose
Enzyme 1 Pfam Domain Function
Enzyme 1 Signals
  • 1-19
Enzyme 1 Transmembrane Regions
  • 1883-1901
Enzyme 1 Essentiality Not Available
Enzyme 1 GenBank ID Protein 34400 Link Image
Enzyme 1 UniProtKB/Swiss-Prot ID P09848 Link Image
Enzyme 1 UniProtKB/Swiss-Prot Entry Name LPH_HUMAN Link Image
Enzyme 1 PDB ID Not Available
Enzyme 1 Cellular Location Not Available
Enzyme 1 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 1 GenBank Gene ID X07994 Link Image
Enzyme 1 GeneCard ID LCT Link Image
Enzyme 1 GenAtlas ID LCT Link Image
Enzyme 1 HGNC ID HGNC:6530 Link Image
Enzyme 1 Chromosome Location Not Available
Enzyme 1 Locus Not Available
Enzyme 1 SNPs SNPJam Report Link Image
Enzyme 1 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 1 Metabolite References Not Available
Enzyme 2 [top]
Enzyme 2 ID 5608
Enzyme 2 Name Alpha-lactalbumin precursor
Enzyme 2 Synonyms
  1. Lactose synthase B protein
  2. Lysozyme- like protein 7
Enzyme 2 Gene Name LALBA
Enzyme 2 Protein Sequence >Alpha-lactalbumin precursor
MRFFVPLFLVGILFPAILAKQFTKCELSQLLKDIDGYGGIALPELICTMFHTSGYDTQAI
VENNESTEYGLFQISNKLWCKSSQVPQSRNICDISCDKFLDDDITDDIMCAKKILDIKGI
DYWLAHKALCTEKLEQWLCEKL
Enzyme 2 Number of Residues 142
Enzyme 2 Molecular Weight 16225
Enzyme 2 Theoretical pI 4.60
Enzyme 2 GO Classification
Function
  • UDP-galactosyltransferase activity
  • UDP-glycosyltransferase activity
  • binding
  • calcium ion binding
  • catalytic activity
  • cation binding
  • ion binding
  • lactose synthase activity
  • transferase activity
  • transferase activity, transferring glycosyl groups
Process
  • carbohydrate metabolism
  • cellular carbohydrate metabolism
  • disaccharide metabolism
  • lactose biosynthesis
  • lactose metabolism
  • macromolecule metabolism
  • metabolism
  • physiological process
Component
  • extracellular region
Enzyme 2 General Function Not Available
Enzyme 2 Specific Function Regulatory subunit of lactose synthase, changes the substrate specificity of galactosyltransferase in the mammary gland making glucose a good acceptor substrate for this enzyme. This enables LS to synthesize lactose, the major carbohydrate component of milk. In other tissues, galactosyltransferase transfers galactose onto the N-acetylglucosamine of the oligosaccharide chains in glycoproteins
Enzyme 2 Pathways Not Available
Enzyme 2 Reactions Not Available
Enzyme 2 Pfam Domain Function
Enzyme 2 Signals
  • 1-19
Enzyme 2 Transmembrane Regions Not Available
Enzyme 2 Essentiality Not Available
Enzyme 2 GenBank ID Protein 307104 Link Image
Enzyme 2 UniProtKB/Swiss-Prot ID P00709 Link Image
Enzyme 2 UniProtKB/Swiss-Prot Entry Name LALBA_HUMAN Link Image
Enzyme 2 PDB ID 1HML Link Image
Enzyme 2 PDB File Show
Enzyme 2 3D Structure
Enzyme 2 Cellular Location Not Available
Enzyme 2 Gene Sequence >429 bp
ATGAGGTTCTTTGTCCCTCTGTTCCTGGTGGGCATCCTGTTCCCTGCCATCCTGGCCAAG
CAATTCACAAAATGTGAGCTGTCCCAGCTGCTGAAAGACATAGATGGTTATGGAGGCATC
GCTTTGCCTGAATTGATCTGTACCATGTTTCACACCAGTGGTTATGACACACAAGCCATA
GTTGAAAACAATGAAAGCACGGAATATGGACTCTTCCAGATCAGTAATAAGCTTTGGTGC
AAGAGCAGCCAGGTCCCTCAGTCAAGGAACATCTGTGACATCTCCTGTGACAAGTTCCTG
GATGATGACATTACTGATGACATAATGTGTGCCAAGAAGATCCTGGATATTAAAGGAATT
GACTACTGGTTGGCCCATAAAGCCCTCTGCACTGAGAAGCTGGAACAGTGGCTTTGTGAG
AAGTTGTGA
Enzyme 2 GenBank Gene ID J00270 Link Image
Enzyme 2 GeneCard ID LALBA Link Image
Enzyme 2 GenAtlas ID LALBA Link Image
Enzyme 2 HGNC ID HGNC:6480 Link Image
Enzyme 2 Chromosome Location 12
Enzyme 2 Locus 12q13
Enzyme 2 SNPs SNPJam Report Link Image
Enzyme 2 General References
  1. Hall L, Craig RK, Edbrooke MR, Campbell PN: Comparison of the nucleotide sequence of cloned human and guinea-pig pre-alpha-lactalbumin cDNA with that of chick pre-lysozyme cDNA suggests evolution from a common ancestral gene. Nucleic Acids Res. 1982 Jun 11;10(11):3503-15. [PubMed Link Image]
  2. Hall L, Emery DC, Davies MS, Parker D, Craig RK: Organization and sequence of the human alpha-lactalbumin gene. Biochem J. 1987 Mar 15;242(3):735-42. [PubMed Link Image]
  3. Findlay JB, Brew K: The complete amino-acid sequence of human -lactalbumin. Eur J Biochem. 1972 May;27(1):65-86. [PubMed Link Image]
  4. Acharya KR, Ren JS, Stuart DI, Phillips DC, Fenna RE: Crystal structure of human alpha-lactalbumin at 1.7 A resolution. J Mol Biol. 1991 Sep 20;221(2):571-81. [PubMed Link Image]
  5. Ren J, Stuart DI, Acharya KR: Alpha-lactalbumin possesses a distinct zinc binding site. J Biol Chem. 1993 Sep 15;268(26):19292-8. [PubMed Link Image]
  6. Chandra N, Brew K, Acharya KR: Structural evidence for the presence of a secondary calcium binding site in human alpha-lactalbumin. Biochemistry. 1998 Apr 7;37(14):4767-72. [PubMed Link Image]
  7. Harata K, Abe Y, Muraki M: Crystallographic evaluation of internal motion of human alpha-lactalbumin refined by full-matrix least-squares method. J Mol Biol. 1999 Mar 26;287(2):347-58. [PubMed Link Image]
Enzyme 2 Metabolite References Not Available
Enzyme 3 [top]
Enzyme 3 ID 5614
Enzyme 3 Name Beta-1,4-galactosyltransferase 1
Enzyme 3 Synonyms
  1. Beta-1,4-GalTase 1
  2. Beta4Gal-T1
  3. b4Gal-T1
  4. UDP-galactose:beta-N-acetylglucosamine beta- 1,4-galactosyltransferase 1
  5. UDP-Gal:beta-GlcNAc beta-1,4- galactosyltransferase 1[Includes: Lactose synthase A protein
  6. Nal synthetase
  7. Beta-N-acetylglucosaminylglycopeptide beta-1,4- galactosyltransferase
Enzyme 3 Gene Name B4GALT1
Enzyme 3 Protein Sequence >Beta-1,4-galactosyltransferase 1
MRLREPLLSGSAAMPGASLQRACRLLVAVCALHLGVTLVYYLAGRDLSRLPQLVGVSTPL
QGGSNSAAAIGQSSGELRTGGARPPPPLGASSQPRPGGDSSPVVDSGPGPASNLTSVPVP
HTTALSLPACPEESPLLVGPMLIEFNMPVDLELVAKQNPNVKMGGRYAPRDCVSPHKVAI
IIPFRNRQEHLKYWLYYLHPVLQRQQLDYGIYVINQAGDTIFNRAKLLNVGFQEALKDYD
YTCFVFSDVDLIPMNDHNAYRCFSQPRHISVAMDKFGFSLPYVQYFGGVSALSKQQFLTI
NGFPNNYWGWGGEDDDIFNRLVFRGMSISRPNAVVGRCRMIRHSRDKKNEPNPQRFDRIA
HTKETMLSDGLNSLTYQVLDVQRYPLYTQITVDIGTPS
Enzyme 3 Number of Residues 398
Enzyme 3 Molecular Weight 43921
Enzyme 3 Theoretical pI 8.77
Enzyme 3 GO Classification
Function
  • catalytic activity
  • transferase activity
  • transferase activity, transferring glycosyl groups
Process
  • carbohydrate metabolism
  • macromolecule metabolism
  • metabolism
  • physiological process
Component
Enzyme 3 General Function Not Available
Enzyme 3 Specific Function The cell surface form functions as a recognition molecule during a variety of cell to cell and cell to matrix interactions, as those occurring during development and egg fertilization, by binding to specific oligosaccharide ligands on opposing cells or in the extracellular matrix
Enzyme 3 Pathways
Enzyme 3 Reactions
  • UDP-galactose + N-acetyl-D-glucosamine = UDP + N-acetyllactosamine
Enzyme 3 Pfam Domain Function
Enzyme 3 Signals
  • 1-37
Enzyme 3 Transmembrane Regions Not Available
Enzyme 3 Essentiality Not Available
Enzyme 3 GenBank ID Protein 29424 Link Image
Enzyme 3 UniProtKB/Swiss-Prot ID P15291 Link Image
Enzyme 3 UniProtKB/Swiss-Prot Entry Name B4GT1_HUMAN Link Image
Enzyme 3 PDB ID Not Available
Enzyme 3 Cellular Location Not Available
Enzyme 3 Gene Sequence >1203 bp
ATGAGGCTTCGGGAGCCGCTCCTGAGCGGCGCCGCGATGCCAGGCGCGTCCCTACAGCGG
GCCTGCCGCCTGCTCGTGGCCGTCTGCGCTCTGCACCTTGGCGTCACCCTCGTTTACTAC
CTGGCTGGCCGCGACCTGAGCCGCCTGCCCCAACTGGTCGGAGTCTCCACACCGCTGCAG
GGCGGCTCGAACAGTGCCGCCGCCATCGGGCAGTCCTCCGGGGAGCTCCGGACCGGAGGG
GCCCGGCCGCCGCCTCCTCTAGGCGCCTCCTCCCAGCCGCGCCCGGGTGGCGACTCCAGC
CCAGTCGTGGATTCTGGCCCTGGCCCCGCTAGCAACTTGACCTCGGTCCCAGTGCCCCAC
ACCACCGCACTGTCGCTGCCCGCCTGCCCTGAGGAGTCCCCGCTGCTTGTGGGCCCCATG
CTGATTGAGTTTAACATGCCTGTGGACCTGGAGCTCGTGGCAAAGCAGAACCCAAATGTG
AAGATGGGCGGCCGCTATGCCCCCAGGGACTGCGTCTCTCCTCACAAAGTGGCCATCATC
ATTCCATTCCGCAACCGGCAGGAGCACCTCAAGTACTGGCTATATTATTTGCACCCAGTC
CTGCAGCGCCAGCAGCTGGACTATGGCATCTATGGCATCTATGTTATCAACCAGGCGGGA
GACACTATATTCAATCGTGCTAAGCTCCTCAATGTTGGCTTTCAAGAAGCCTTGAAGGAC
TATGACTACACCTGCTTTGTGTTTAGTGACGTGGACCTCATCCCAATGAATGACCATAAT
GCGTACAGGTGTTTTTCACAGCCACGGCACATTTCCGTTGCAATGGATAAGTTTGGATTC
AGCCTACCTTATGTTCAGTATTTTGGAGGTGTCTCTGCTCTAAGTAAACAACAGTTTCTA
ACCATCAATGGATTTCCTAATAATTATTGGGGCTGGGGAGGAGAAGATGATGACATTTTT
AACAGATTAGTTTTTAGAGGCATGTCTATATCTCGCCCAAATGCTGTGGTCGGGAGGTGT
CGCATGATCCGCCACTCAAGAGACAAAAAAAATGAACCCAATCCTCAGAGGTTTGACCGA
ATTGCACACACAAAGGAGACAATGCTCTCTGATGGTTTGAACTCACTCACCTACCAGGTG
CTGGATGTACAGAGATACCCATTGTATACCCAAATCACAGTGGACATCGGGACACCGAGC
TAG
Enzyme 3 GenBank Gene ID X14085 Link Image
Enzyme 3 GeneCard ID B4GALT1 Link Image
Enzyme 3 GenAtlas ID B4GALT1 Link Image
Enzyme 3 HGNC ID HGNC:924 Link Image
Enzyme 3 Chromosome Location 9
Enzyme 3 Locus 9p13
Enzyme 3 SNPs SNPJam Report Link Image
Enzyme 3 General References
  1. Masri KA, Appert HE, Fukuda MN: Identification of the full-length coding sequence for human galactosyltransferase (beta-N-acetylglucosaminide: beta 1,4-galactosyltransferase). Biochem Biophys Res Commun. 1988 Dec 15;157(2):657-63. [PubMed Link Image]
  2. Watzele G, Berger EG: Near identity of HeLa cell galactosyltransferase with the human placental enzyme. Nucleic Acids Res. 1990 Dec 11;18(23):7174. [PubMed Link Image]
  3. Mengle-Gaw L, McCoy-Haman MF, Tiemeier DC: Genomic structure and expression of human beta-1,4-galactosyltransferase. Biochem Biophys Res Commun. 1991 May 15;176(3):1269-76. [PubMed Link Image]
  4. Uejima T, Uemura M, Nozawa S, Narimatsu H: Complementary DNA cloning for galactosyltransferase associated with tumor and determination of antigenic epitopes recognized by specific monoclonal antibodies. Cancer Res. 1992 Nov 15;52(22):6158-63. [PubMed Link Image]
  5. Kudo T, Narimatsu H: The beta 1,4-galactosyltransferase gene is post-transcriptionally regulated during differentiation of mouse F9 teratocarcinoma cells. Glycobiology. 1995 Jun;5(4):397-403. [PubMed Link Image]
  6. Chatterjee SK, Mukerjee S, Tripathi PK: Analysis of the sequences of human beta-1,4-galactosyltransferase cDNA clones. Int J Biochem Cell Biol. 1995 Mar;27(3):329-36. [PubMed Link Image]
  7. Appert HE, Rutherford TJ, Tarr GE, Wiest JS, Thomford NR, McCorquodale DJ: Isolation of a cDNA coding for human galactosyltransferase. Biochem Biophys Res Commun. 1986 Aug 29;139(1):163-8. [PubMed Link Image]
  8. Appert HE, Rutherford TJ, Tarr GE, Thomford NR, McCorquodale DJ: Isolation of galactosyltransferase from human milk and the determination of its N-terminal amino acid sequence. Biochem Biophys Res Commun. 1986 Jul 16;138(1):224-9. [PubMed Link Image]
  9. Aoki D, Appert HE, Johnson D, Wong SS, Fukuda MN: Analysis of the substrate binding sites of human galactosyltransferase by protein engineering. EMBO J. 1990 Oct;9(10):3171-8. [PubMed Link Image]
  10. Lopez LC, Youakim A, Evans SC, Shur BD: Evidence for a molecular distinction between Golgi and cell surface forms of beta 1,4-galactosyltransferase. J Biol Chem. 1991 Aug 25;266(24):15984-91. [PubMed Link Image]
  11. Yamaguchi N, Fukuda MN: Golgi retention mechanism of beta-1,4-galactosyltransferase. Membrane-spanning domain-dependent homodimerization and association with alpha- and beta-tubulins. J Biol Chem. 1995 May 19;270(20):12170-6. [PubMed Link Image]
  12. Amado M, Almeida R, Schwientek T, Clausen H: Identification and characterization of large galactosyltransferase gene families: galactosyltransferases for all functions. Biochim Biophys Acta. 1999 Dec 6;1473(1):35-53. [PubMed Link Image]
Enzyme 3 Metabolite References Not Available
Enzyme 4 [top]
Enzyme 4 ID 6124
Enzyme 4 Name Beta-galactosidase precursor
Enzyme 4 Synonyms
  1. Lactase
  2. Acid beta- galactosidase
Enzyme 4 Gene Name GLB1
Enzyme 4 Protein Sequence >Beta-galactosidase precursor
MPGFLVRILLLLLVLLLLGPTRGLRNATQRMFEIDYSRDSFLKDGQPFRYISGSIHYSRV
PRFYWKDRLLKMKMAGLNAIQTYVPWNFHEPWPGQYQFSEDHDVEYFLRLAHELGLLVIL
RPGPYICAEWEMGGLPAWLLEKESILLRSSDPDYLAAVDKWLGVLLPKMKPLLYQNGGPV
ITVQVENEYGSYFACDFDYLRFLQKRFRHHLGDDVVLFTTDGAHKTFLKCGALQGLYTTV
DFGTGSNITDAFLSQRKCEPKGPLINSEFYTGWLDHWGQPHSTIKTEAVASSLYDILARG
ASVNLYMFIGGTNFAYWNGANSPYAAQPTSYDYDAPLSEAGDLTEKYFALRNIIQKFEKV
PEGPIPPSTPKFAYGKVTLEKLKTVGAALDILCPSGPIKSLYPLTFIQVKQHYGFVLYRT
TLPQDCSNPAPLSSPLNGVHDRAYVAVDGIPQGVLERNNVITLNITGKAGATLDLLVENM
GRVNYGAYINDFKGLVSNLTLSSNILTDWTIFPLDTEDAVRSHLGGWGHRDSGHHDEAWA
HNSSNYTLPAFYMGNFSIPSGIPDLPQDTFIQFPGWTKGQVWINGFNLGRYWPARGPQLT
LFVPQHILMTSAPNTITVLELEWAPCSSDDPELCAVTFVDRPVIGSSVTYDHPSKPVEKR
LMPPPPQKNKDSWLDHV
Enzyme 4 Number of Residues 677
Enzyme 4 Molecular Weight 76092
Enzyme 4 Theoretical pI 6.55
Enzyme 4 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 4 General Function Carbohydrate transport and metabolism
Enzyme 4 Specific Function Cleaves beta-linked terminal galactosyl residues from gangliosides, glycoproteins, and glycosaminoglycans
Enzyme 4 Pathways
Enzyme 4 Reactions
  • Hydrolysis of terminal non-reducing beta-D-galactose residues in beta-D-galactosides
Enzyme 4 Pfam Domain Function
Enzyme 4 Signals
  • 1-23
Enzyme 4 Transmembrane Regions Not Available
Enzyme 4 Essentiality Not Available
Enzyme 4 GenBank ID Protein 179401 Link Image
Enzyme 4 UniProtKB/Swiss-Prot ID P16278 Link Image
Enzyme 4 UniProtKB/Swiss-Prot Entry Name BGAL_HUMAN Link Image
Enzyme 4 PDB ID Not Available
Enzyme 4 Cellular Location Not Available
Enzyme 4 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 4 GenBank Gene ID M27507 Link Image
Enzyme 4 GeneCard ID GLB1 Link Image
Enzyme 4 GenAtlas ID GLB1 Link Image
Enzyme 4 HGNC ID HGNC:4298 Link Image
Enzyme 4 Chromosome Location 3
Enzyme 4 Locus 3p21.33
Enzyme 4 SNPs SNPJam Report Link Image
Enzyme 4 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 4 Metabolite References Not Available
Enzyme 5 [top]
Enzyme 5 ID 16488
Enzyme 5 Name cDNA, FLJ93218, Homo sapiens UDP-Gal:betaGlcNAc beta 1,4- galactosyltransferase,polypeptide 1 (B4GALT1), mRNA (UDP-Gal:betaGlcNAc beta 1,4-galactosyltransferase, polypeptide 1, isoform CRA_a)
Enzyme 5 Synonyms Not Available
Enzyme 5 Gene Name B4GALT1
Enzyme 5 Protein Sequence >cDNA, FLJ93218, Homo sapiens UDP-Gal:betaGlcNAc beta 1,4- galactosyltransferase,polypeptide 1 (B4GALT1), mRNA (UDP-Gal:betaGlcNAc beta 1,4-galactosyltransferase, polypeptide 1, isoform CRA_a)
MRLREPLLSGSAAMPGASLQRACRLLVAVCALHLGVTLVYYLAGRDLSRLPQLVGVSTPL
QGGSNSAAAIGQSSGELRTGGARPPPPLGASSQPRPGGDSSPVVDSGPGPASNLTSVPVP
HTTALSLPACPEESPLLVGPMLIEFNMPVDLELVAKQNPNVKMGGRYAPRDCVSPHKVAI
IIPFRNRQEHLKYWLYYLHPVLQRQQLDYGIYVINQAGDTIFNRAKLLNVGFQEALKDYD
YTCFVFSDVDLIPMNDHNAYRCFSQPRHISVAMDKFGFSLPYVQYFGGVSALSKQQFLTI
NGFPNNYWGWGGEDDDIFNRLVFRGMSISRPNAVVGRCRMIRHSRDKKNEPNPQRFDRIA
HTKETMLSDGLNSLTYQVLDVQRYPLYTQITVDIGTPS
Enzyme 5 Number of Residues 398
Enzyme 5 Molecular Weight 43921
Enzyme 5 Theoretical pI 8.77
Enzyme 5 GO Classification
Function
  • catalytic activity
  • transferase activity
  • transferase activity, transferring glycosyl groups
Process
  • carbohydrate metabolism
  • macromolecule metabolism
  • metabolism
  • physiological process
Component
Enzyme 5 General Function Not Available
Enzyme 5 Specific Function Not Available
Enzyme 5 Pathways Not Available
Enzyme 5 Reactions Not Available
Enzyme 5 Pfam Domain Function
Enzyme 5 Signals
  • None
Enzyme 5 Transmembrane Regions
  • None
Enzyme 5 Essentiality Not Available
Enzyme 5 GenBank ID Protein Not Available
Enzyme 5 UniProtKB/Swiss-Prot ID B2R710 Link Image
Enzyme 5 UniProtKB/Swiss-Prot Entry Name B2R710_HUMAN Link Image
Enzyme 5 PDB ID 1FR8 Link Image
Enzyme 5 PDB File Show
Enzyme 5 3D Structure
Enzyme 5 Cellular Location Not Available
Enzyme 5 Gene Sequence Not Available
Enzyme 5 GenBank Gene ID AK312797 Link Image
Enzyme 5 GeneCard ID B2R710 Link Image
Enzyme 5 GenAtlas ID Not Available
Enzyme 5 HGNC ID Not Available
Enzyme 5 Chromosome Location Not Available
Enzyme 5 Locus Not Available
Enzyme 5 SNPs SNPJam Report Link Image
Enzyme 5 General References Not Available
Enzyme 5 Metabolite References Not Available
Enzyme 6 [top]
Enzyme 6 ID 16489
Enzyme 6 Name cDNA FLJ38554 fis, clone HCHON2002496, highly similar to Beta-1,4-galactosyltransferase 2 (EC 2.4.1.-)
Enzyme 6 Synonyms
  1. SubName: UDP-Gal:betaGlcNAc beta 1,4-galactosyltransferase, polypeptide 2, isoform CRA_a
Enzyme 6 Gene Name B4GALT2
Enzyme 6 Protein Sequence >cDNA FLJ38554 fis, clone HCHON2002496, highly similar to Beta-1,4-galactosyltransferase 2 (EC 2.4.1.-)
MSRLLGGTLERVCKAVLLLCLLHFLVAVILYFDVYAQHLAFFSRFSARGPAHALHPAASS
SSSSSNCSRPNATASSSGLPEVPSALPGPTAPTLPPCPDSPPGLVGRLLIEFTSPMPLER
VQRENPGVLMGGRYTPPDCTPAQTVAVIIPFRHREHHLRYWLHYLHPILRRQRLRYGVYV
INQHGEDTFNRAKLLNVGFLEALKEDAAYDCFIFSDVDLVPMDDRNLYRCGDQPRHFAIA
MDKFGFRLPYAGYFGGVSGLSKAQFLRINGFPNEYWGWGGEDDDIFNRISLTGMKISRPD
IRIGRYRMIKHDRDKHNEPNPQRFTKIQNTKLTMKRDGIGSVRYQVLEVSRQPLFTNITV
DIGRPPSWPPRG
Enzyme 6 Number of Residues 372
Enzyme 6 Molecular Weight 41973
Enzyme 6 Theoretical pI 9.66
Enzyme 6 GO Classification
Function
  • catalytic activity
  • transferase activity
  • transferase activity, transferring glycosyl groups
Process
  • carbohydrate metabolism
  • macromolecule metabolism
  • metabolism
  • physiological process
Component
Enzyme 6 General Function Not Available
Enzyme 6 Specific Function Not Available
Enzyme 6 Pathways Not Available
Enzyme 6 Reactions Not Available
Enzyme 6 Pfam Domain Function
Enzyme 6 Signals
  • None
Enzyme 6 Transmembrane Regions
  • None
Enzyme 6 Essentiality Not Available
Enzyme 6 GenBank ID Protein Not Available
Enzyme 6 UniProtKB/Swiss-Prot ID B3KTP0 Link Image
Enzyme 6 UniProtKB/Swiss-Prot Entry Name B3KTP0_HUMAN Link Image
Enzyme 6 PDB ID Not Available
Enzyme 6 Cellular Location Not Available
Enzyme 6 Gene Sequence Not Available
Enzyme 6 GenBank Gene ID AK095873 Link Image
Enzyme 6 GeneCard ID B3KTP0 Link Image
Enzyme 6 GenAtlas ID Not Available
Enzyme 6 HGNC ID Not Available
Enzyme 6 Chromosome Location Not Available
Enzyme 6 Locus Not Available
Enzyme 6 SNPs SNPJam Report Link Image
Enzyme 6 General References Not Available
Enzyme 6 Metabolite References Not Available