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Human Metabolome Database Version 2.5

 

Showing metabocard for D-Maltose (HMDB00163)

Legend: metabolite field enzyme field

Version 2.5
Creation Date 2005-11-16 15:48:42
Update Date 2010-07-23 12:22:41
Accession Number HMDB00163
Secondary Accession Numbers Not Available
Common Name D-Maltose
Description Maltose, or malt sugar, is a primary disaccharide in the human diet formed from two units of glucose joined with an alpha (1->4) linkage. It is the second member of an important biochemical series of glucose chains. The addition of another glucose unit yields maltotriose, Further additions will produce dextrins, also called maltodextrins, and eventually starch. Maltose can be broken down into two glucose molecules by hydrolysis in living organisms. At the surface of the small intestine, the brush border enzymes maltase, breaks down maltose. (PMID: 14522745)
Synonyms
  1. alpha-Malt sugar
  2. alpha-D-glucopyranosyl-(1->4)-D-glucose
  3. alpha-D-glucopyranosyl-(1->4)-D-glucopyranose
  4. alpha-D-Glcp-(1->4)-D-Glcp
  5. Sunmalt S
  6. Sunmalt
  7. Martos-10
  8. Malzzucker
  9. Maltose solution
  10. Maltose HHH
  11. Maltose HH
  12. Maltose
  13. Maltos
  14. Maltodiose
  15. Maltobiose
  16. Malt sugar
  17. Madoros (TN)
  18. Madoros
  19. Finetose F
  20. Finetose
  21. D-Maltose
  22. D-(+)-maltose
  23. Cextromaltose
  24. Advantose 100
  25. 4-O-alpha-D-glucopyranosyl-D-glucose
  26. 4-O-alpha-D-glucopyranosyl-D-glucopyranose
  27. 4-O-a-D-Glucopyranosyl-D-glucose
  28. 4-(alpha-D-glucosido)-D-glucose
  29. 4-(alpha-D-glucopyranosido)-alpha-glucopyranose
  30. 1-alpha-D-Glucopyranosyl-4-alpha-D-glucopyranose
  31. alpha-delta-glucopyranosyl-(1->4)-delta-glucose
  32. alpha-delta-glucopyranosyl-(1->4)-delta-glucopyranose
  33. alpha-delta-Glcp-(1->4)-delta-Glcp
  34. delta-Maltose
  35. delta-(+)-maltose
  36. 4-O-alpha-delta-glucopyranosyl-delta-glucose
  37. 4-O-alpha-delta-glucopyranosyl-delta-glucopyranose
  38. 4-(alpha-delta-glucosido)-delta-glucose
  39. 4-(alpha-delta-glucopyranosido)-alpha-glucopyranose
  40. 1-alpha-delta-Glucopyranosyl-4-alpha-delta-glucopyranose
Chemical IUPAC Name (2R,3S,4S,5R,6R)-2-(hydroxymethyl)-6-[(2R,3S,4R,5R)-4,5,6-trihydroxy-2-(hydroxymethyl)oxan-3-yl]oxyoxane-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
—
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 C00208 Link Image
BioCyc ID MALTOSE Link Image
BiGG ID 34261 Link Image
Wikipedia Link Malt sugar Link Image
NuGOwiki Link HMDB00163 Link Image
Metagene Link HMDB00163 Link Image
METLIN ID 413 Link Image
PubChem Compound 439186 Link Image
PubChem Substance 24882612 Link Image
ChEBI ID 17306 Link Image
CAS Registry Number 69-79-4
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 Pedersen, Sven; Vang Hendriksen, Hanne. Method for production of maltose and/or enzymatically modified starch. PCT Int. Appl. (2001), 99 pp.
Melting Point (Experimental) 102-103 oC
Experimental Water Solubility 780.0 mg/mL [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 1A7L Link Image
Experimental PDB File Show
Experimental PDB Structure
Experimental 1H NMR Spectrum Download Spectrum
Download FID (Varian)
Show Experimental Conditions Link Image
Experimental 13C NMR Spectrum Download Spectrum
Download FID (Bruker)
Show Experimental Conditions Link Image
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
Show Experimental Conditions Link Image
Medium Energy
Download File
Show Experimental Conditions Link Image
High Energy
Download File
Show Experimental Conditions Link Image
Simplified TOCSY Spectrum Show Image
Show Peaklist
BMRB Spectrum Show Image
Show Peaklist
Cellular Location
  • Cytoplasm
  • Extracellular
  • lysosome
Biofluid Location
  • Blood
  • Urine
Tissue Location
Tissue References
Platelet —
Concentrations (Normal)
Biofluid Urine
Value 6.14 +/- 5.12 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]
Concentrations (Abnormal)
Biofluid Blood
Value 1169.0 +/- 526.0 uM
Age Adult:>18 yrs old
Sex Both
Condition Peritoneal dialysis
Comments Not Available
References
  • Garcia-Lopez E, Anderstam B, Heimburger O, Amici G, Werynski A, Lindholm B: Determination of high and low molecular weight molecules of icodextrin in plasma and dialysate, using gel filtration chromatography, in peritoneal dialysis patients. Perit Dial Int. 2005 Mar-Apr;25(2):181-91. [PubMed Link Image]
Associated Disorders
Condition References
Peritoneal dialysis
  • Garcia-Lopez E, Anderstam B, Heimburger O, Amici G, Werynski A, Lindholm B: Determination of high and low molecular weight molecules of icodextrin in plasma and dialysate, using gel filtration chromatography, in peritoneal dialysis patients. Perit Dial Int. 2005 Mar-Apr;25(2):181-91. [PubMed Link Image]
OMIM ID Not Available
Pathways
Name SMPDB Link KEGG Link
Starch and Sucrose Metabolism SMP00058 Link Image map00500 Link Image
General References
  1. Rubaltelli FF, Biadaioli R, Pecile P, Nicoletti P: Intestinal flora in breast- and bottle-fed infants. J Perinat Med. 1998;26(3):186-91. [PubMed Link Image]
  2. Andrews RK, Suzuki-Inoue K, Shen Y, Tulasne D, Watson SP, Berndt MC: Interaction of calmodulin with the cytoplasmic domain of platelet glycoprotein VI. Blood. 2002 Jun 1;99(11):4219-21. [PubMed Link Image]
  3. Hirooka EY, Muller EE, Freitas JC, Vicente E, Yoshimoto Y, Bergdoll MS: Enterotoxigenicity of Staphylococcus intermedius of canine origin. Int J Food Microbiol. 1988 Dec;7(3):185-91. [PubMed Link Image]
  4. Daly JJ, Sherman JK, Green L, Hostetler TL: Survival of Trichomonas vaginalis in human semen. Genitourin Med. 1989 Apr;65(2):106-8. [PubMed Link Image]
  5. Sherman JK, Hostetler TL, McHenry K, Daly JJ: Cryosurvival of Trichomonas vaginalis during cryopreservation of human semen. Cryobiology. 1991 Jun;28(3):246-50. [PubMed Link Image]
  6. van Leeuwen L: New saccharogenic determination of alpha-amylase in serum and urine. Clin Chem. 1979 Feb;25(2):215-7. [PubMed Link Image]
  7. Miller LJ, Malagelada JR, Taylor WF, Go VL: Intestinal control of human postprandial gastric function: the role of components of jejunoileal chyme in regulating gastric secretion and gastric emptying. Gastroenterology. 1981 Apr;80(4):763-9. [PubMed Link Image]
  8. Roy E, Stavropoulos E, Brennan J, Coade S, Grigorieva E, Walker B, Dagg B, Tascon RE, Lowrie DB, Colston MJ, Jolles S: Therapeutic efficacy of high-dose intravenous immunoglobulin in Mycobacterium tuberculosis infection in mice. Infect Immun. 2005 Sep;73(9):6101-9. [PubMed Link Image]
  9. Wyss C, Choi BK, Schupbach P, Guggenheim B, Gobel UB: Treponema maltophilum sp. nov., a small oral spirochete isolated from human periodontal lesions. Int J Syst Bacteriol. 1996 Jul;46(3):745-52. [PubMed Link Image]
  10. Morse DR, Schacterle GR, Furst L, Zaydenberg M, Pollack RL: Oral digestion of a complex-carbohydrate cereal: effects of stress and relaxation on physiological and salivary measures. Am J Clin Nutr. 1989 Jan;49(1):97-105. [PubMed Link Image]
  11. Yamamoto T, Kajiura S, Hirai Y, Watanabe T: Capnocytophaga haemolytica sp. nov. and Capnocytophaga granulosa sp. nov., from human dental plaque. Int J Syst Bacteriol. 1994 Apr;44(2):324-9. [PubMed Link Image]
  12. Zhu J, Marchant RE: Dendritic saccharide surfactant polymers as antifouling interface materials to reduce platelet adhesion. Biomacromolecules. 2006 Apr;7(4):1036-41. [PubMed Link Image]
  13. Lingstrom P, Birkhed D, Granfeldt Y, Bjorck I: pH measurements of human dental plaque after consumption of starchy foods using the microtouch and the sampling method. Caries Res. 1993;27(5):394-401. [PubMed Link Image]
  14. Leth-Larsen R, Holmskov U, Hojrup P: Structural characterization of human and bovine lung surfactant protein D. Biochem J. 1999 Nov 1;343 Pt 3:645-52. [PubMed Link Image]
  15. Janoshazi A, Solomon AK: Initial steps of alpha- and beta-D-glucose binding to intact red cell membrane. J Membr Biol. 1993 Mar;132(2):167-78. [PubMed Link Image]
  16. Tiwari F, Singh DK: Behavioural responses of the snail Lymnaea acuminata to carbohydrates in snail-attractant pellets. Naturwissenschaften. 2004 Aug;91(8):378-80. Epub 2004 Jun 2. [PubMed Link Image]
  17. Chiba S, Hiromi K, Minamiura N, Ohnishi M, Shimomura T, Suga K, Suganuma T, Tanaka A, Tomioka S, Yamamoto T: Quantitative study on anomeric forms of glucose produced by alpha-glucosidases. J Biochem (Tokyo). 1979 May;85(5):1135-41. [PubMed Link Image]
  18. McCue JP, Hein RH, Tenold R: Three generations of immunoglobulin G preparations for clinical use. Rev Infect Dis. 1986 Jul-Aug;8 Suppl 4:S374-81. [PubMed Link Image]
  19. Dorner KM: Quantitative determination of lactose, maltose, and sucrose in urine. Eur J Pediatr. 1977 Aug 23;126(1-2):45-52. [PubMed Link Image]
  20. Lu J, Willis AC, Reid KB: Purification, characterization and cDNA cloning of human lung surfactant protein D. Biochem J. 1992 Jun 15;284 ( Pt 3):795-802. [PubMed Link Image]
  21. Wikipedia Link Image
Metabolic Enzymes
  1. Glycogen debranching enzyme
  2. Salivary alpha-amylase precursor
  3. Maltase-glucoamylase, intestinal [Includes: Maltase
  4. Neutral alpha-glucosidase C
  5. Uncharacterized protein GAA
Enzyme 1 [top]
Enzyme 1 ID 5603
Enzyme 1 Name Glycogen debranching enzyme
Enzyme 1 Synonyms
  1. Glycogen debrancher[Includes: 4-alpha- glucanotransferase
  2. Oligo-1,4-1,4-glucantransferase
  3. Amylo-alpha-1,6-glucosidase
  4. Amylo-1,6-glucosidase
  5. Dextrin 6-alpha-D-glucosidase]
Enzyme 1 Gene Name AGL
Enzyme 1 Protein Sequence >Glycogen debranching enzyme 
MGHSKQIRILLLNEMEKLEKTLFRLEQGYELQFRLGPTLQGKAVTVYTNYPFPGETFNRE
KFRSLDWENPTEREDDSDKYCKLNLQQSGSFQYYFLQGNEKSGGGYIVVDPILRVGADNH
VLPLDCVTLQTFLAKCLGPFDEWESRLRVAKESGYNMIHFTPLQTLGLSRSCYSLANQLE
LNPDFSRPNRKYTWNDVGQLVEKLKKEWNVICITDVVYNHTAANSKWIQEHPECAYNLVN
SPHLKPAWVLDRALWRFSCDVAEGKYKEKGIPALIENDHHMNSIRKIIWEDIFPKLKLWE
FFQVDVNKAVEQFRRLLTQENRRVTKSDPNQHLTIIQDPEYRRFGCTVDMNIALTTFIPH
DKGPAAIEECCNWFHKRMEELNSEKHRLINYHQEQAVNCLLGNVFYERLAGHGPKLGPVT
RKHPLVTRYFTFPFEEIDFSMEESMIHLPNKACFLMAHNGWVMGDDPLRNFAEPGSEVYL
RRELICWGDSVKLRYGNKPEDCPYLWAHMKKYTEITATYFQGVRLDNCHSTPLHVAEYML
DAARNLQPNLYVVAELFTGSEDLDNVFVTRLGISSLIREAMSAYNSHEEGRLVYRYGGEP
VGSFVQPCLRPLMPAIAHALFMDITHDNECPIVHRSAYDALPSTTIVSMACCASGSTRGY
DELVPHQISVVSEERFYTKWNPEALPSNTGEVNFQSGIIAARCAISKLHQELGAKGFIQV
YVDQVDEDIVAVTRHSPSIHQSVVAVSRTAFRNPKTSFYSKEVPQMCIPGKIEEVVLEAR
TIERNTKPYRKDENSINGTPDITVEIREHIQLNESKIVKQAGVATKGPNEYIQEIEFENL
SPGSVIIFRVSLDPHAQVAVGILRNHLTQFSPHFKSGSLAVDNADPILKIPFASLASRLT
LAELNQILYRCESEEKEDGGGCYDIPNWSALKYAGLQGLMSVLAEIRPKNDLGHPFCNNL
RSGDWMIDYVSNRLISRSGTIAEVGKWLQAMFFYLKQIPRYLIPCYFDAILIGAYTTLLD
TAWKQMSSFVQNGSTFVKHLSLGSVQLCGVGKFPSLPILSPALMDVPYRLNEITKEKEQC
CVSLAAGLPHFSSGIFRCWGRDTFIALRGILLITGRYVEARNIILAFAGTLRHGLIPNLL
GEGIYARYNCRDAVWWWLQCIQDYCKMVPNGLDILKCPVSRMYPTDDSAPLPAGTLDQPL
FEVIQEAMQKHMQGIQFRERNAGPQIDRNMKDEGFNITAGVDEETGFVYGGNRFNCGTWM
DKMGESDRARNRGIPATPRDGSAVEIVGLSKSAVRWLLELSKKNIFPYHEVTVKRHGKAI
KVSYDEWNRKIQDNFEKLFHVSEDPSDLNEKHPNLVHKRGIYKDSYGASSPWCDYQLRPN
FTIAMVVAPELFTTEKAWKALEIAEKKLLGPLGMKTLDPDDMVYCGIYDNALDNDNYNLA
KGFNYHQGPEWLWPIGYFLRAKLYFSRLMGPETTAKTIVLVKNVLSRHYVHLERSPWKGL
PELTNENAQYCPFSCETQAWSIATILETLYDL
Enzyme 1 Number of Residues 1532
Enzyme 1 Molecular Weight 174766
Enzyme 1 Theoretical pI 6.74
Enzyme 1 GO Classification
Function
  • 4-alpha-glucanotransferase activity
  • amylo-alpha-1,6-glucosidase activity
  • catalytic activity
  • glycogen debranching enzyme activity
Process
  • carbohydrate metabolism
  • cellular polysaccharide metabolism
  • glucan metabolism
  • glycogen biosynthesis
  • glycogen metabolism
  • macromolecule metabolism
  • metabolism
  • physiological process
  • polysaccharide metabolism
Component
—
Enzyme 1 General Function Carbohydrate transport and metabolism
Enzyme 1 Specific Function Multifunctional enzyme acting as 1,4-alpha-D-glucan:1,4- alpha-D-glucan 4-alpha-D-glycosyltransferase and amylo-1,6- glucosidase in glycogen degradation
Enzyme 1 Pathways
Enzyme 1 Reactions
  • Hydrolysis of (1->6)-alpha-D-glucosidic branch linkages in glycogen phosphorylase limit dextrin
Enzyme 1 Pfam Domain Function
Enzyme 1 Signals
  • None
Enzyme 1 Transmembrane Regions
  • None
Enzyme 1 Essentiality Not Available
Enzyme 1 GenBank ID Protein 187577 Link Image
Enzyme 1 UniProtKB/Swiss-Prot ID P35573 Link Image
Enzyme 1 UniProtKB/Swiss-Prot Entry Name GDE_HUMAN Link Image
Enzyme 1 PDB ID Not Available
Enzyme 1 Cellular Location Not Available
Enzyme 1 Gene Sequence >4548 bp 
ATGAGTTTATTAACATGTGCTTTTTATTTAGGGTATGAGCTACAGTTCCGATTAGGCCCA
ACTTTACAGGGAAAAGCAGTTACCGTGTATACAAATTACCCATTTCCTGGAGAAACATTT
AATAGAGAAAAATTCCGTTCTCTGGATTGGGAAAATCCAACAGAAAGAGAAGATGATTCT
GATAAATACTGTAAACTTAATCTGCAACAATCTGGTTCATTTCAGTATTATTTCCTTCAA
GGAAATGAGAAAAGTGGTGGAGGTTACATAGTTGTGGACCCCATTTTACGTGTTGGTGCT
GATAATCATGTGCTACCCTTGGACTGTGTTACTCTTCAGACATTTTTAGCTAAGTGTTTG
GGACCTTTTGATGAATGGGAAAGCAGACTTAGGGTTGCAAAAGAATCAGGCTACAACATG
ATTCATTTTACCCCATTGCAGACTCTTGGACTATCTAGGTCATGCTACTCCCTTGCCAAT
CAGTTAGAATTAAATCCTGACTTTTCAAGACCTAATAGAAAGTATACCTGGAATGATGTT
GGACAGCTAGTGGAAAAATTAAAAAAGGAATGGAATGTTATTTGTATTACTGATGTTGTC
TACAATCATACTGCTGCTAATAGTAAATGGATCCAGGAACATCCAGAATGTGCCTATAAT
CTTGTGAATTCTCCACACTTAAAACCTGCCTGGGTCTTAGACAGAGCACTTTGGCGTTTC
TCCTGTGATGTTGCAGAAGGGAAATACAAAGAAAAGGGAATACCTGCTTTGATTGAAAAT
GATCACCATATGAATTCCATCCGAAAAATAATTTGGGAGGATATTTTTCCAAAGCTTAAA
CTCTGGGAATTTTTCCAAGTAGATGTCAACAAAGCGGTTGAGCAATTTAGAAGACTTCTT
ACACAAGAAAATAGGCGAGTAACCAAGTCTGATCCAAACCAACACCTTACGATTATTCAA
GATCCTGAATACAGACGGTTTGGCTGTACTGTAGATATGAACATTGCACTAACGACTTTC
ATACCACATGACAAGGGGCCAGCAGCAATTGAAGAATGCTGTAATTGGTTTCATAAAAGA
ATGGAGGAATTAAATTCAGAGAAGCATCGACTCATTAACTATCATCAGGAACAGGCAGTT
AATTGCCTTTTGGGAAATGTGTTTTATGAACGACTGGCTGGCCATGGTCCAAAACTAGGA
CCTGTCACTAGAAAGCATCCTTTAGTTACCAGGTATTTTACTTTCCCATTTGAAGAGATA
GACTTCTCCATGGAAGAATCTATGATTCATCTGCCAAATAAAGCTTGTTTTCTGATGGCA
CACAATGGATGGGTAATGGGAGATGATCCTCTTCGAAACTTTGCTGAACCGGGTTCAGAA
GTTTACCTAAGGAGAGAACTTATTTGCTGGGGAGACAGTGTTAAATTACGCTATGGGAAT
AAACCAGAGGACTGTCCTTATCTCTGGGCACACATGAAAAAATACACTGAAATAACTGCA
ACTTATTTCCAGGGAGTACGTCTTGATAACTGCCACTCAACACCTCTTCACGTAGCTGAG
TACATGTTGGATGCTGCTAGGAATTTGCAACCCAATTTATATGTAGTAGCTGAACTGTTC
ACAGGAAGTGAAGATCTGGACAATGTCTTTGTTACTAGACTGGGCATTAGTTCCTTAATA
AGAGAGGCAATGAGTGCATATAATAGTCATGAAGAGGGCAGATTAGTTTACCGATATGGA
GGAGAACCTGTTGGATCCTTTGTTCAGCCCTGTTTGAGGCCTTTAATGCCAGCTATTGCA
CATGCCCTGTTTATGGATATTACGCATGATAATGAGTGTCCTATTGTGCATAGATCAGCG
TATGATGCTCTTCCAAGTACTACAATTGTTTCTATGGCATGTTGTGCTAGTGGAAGTACA
AGAGGCTATGATGAATTAGTGCCTCATCAGATTTCAGTGGTTTCTGAAGAACGGTTTTAC
ACTAAGTGGAATCCTGAAGCATTGCCTTCAAACACAGGTGAAGTTAATTTCCAAAGCGGC
ATTATTGCAGCCAGGTGTGCTATCAGTAAACTTCATCAGGAGCTTGGAGCCAAGGGTTTT
ATTCAGGTGTATGTGGATCAAGTTGATGAAGACATAGTGGCAGTAACAAGACACTCACCT
AGCATCCATCAGTCTGTTGTGGCTGTATCTAGAACTGCTTTCAGGAATCCCAAGACTTCA
TTTTACAGCAAGGAAGTGCCTCAAATGTGCATCCCTGGCAAAATTGAAGAAGTAGTTCTT
GAAGCTAGAACTATTGAGAGAAACACGAAACCTTATAGGAAGGATGAGAATTCAATCAAT
GGAACACCAGATATCACAGTAGAAATTAGAGAACATATTCAGCTTAATGAAAGTAAAATT
GTTAAACAAGCTGGAGTTGCCACAAAAGGGCCCAATGAATATATTCAAGAAATAGAATTT
GAAAACTTGTCTCCAGGAAGTGTTATTATATTCAGAGTTAGTCTTGATCCACATGCACAA
GTCGCTGTTGGAATTCTTCGAAATCATCTGACACAATTCAGTCCTCACTTTAAATCTGGC
AGCCTAGCTGTTGACAATGCAGATCCTATATTAAAAATTCCTTTTGCTTCTCTTGCCTCC
AGATTAACTTTGGCTGAGCTAAATCAGATCCTTTACCGATGTGAATCAGAAGAAAAGGAA
GATGGTGGAGGGTGCTATGACATACCAAACTGGTCAGCCCTTAAATATGCAGGTCTTCAA
GGTTTAATGTCTGTATTGGCAGAAATAAGACCAAAGAATGACTTGGGGCATCCTTTTTGT
AATAATTTGAGATCTGGAGATTGGATGATTGACTATGTCAGTAACCGGCTTATTTCACGA
TCAGGAACTATTGCTGAAGTTGGTAAATGGTTGCAGGCTATGTTCTTCTACCTGAAGCAG
ATCCCACGTTACCTTATCCCATGTTACTTTGATGCTATATTAATTGGTGCATATACCACT
CTTCTGGATACAGCATGGAAGCAGATGTCAAGCTTTGTTCAGAATGGTTCAACCTTTGTG
AAACACCTTTCATTGGGTTCAGTTCAACTGTGTGGAGTAGGAAAATTCCCTTCCCTGCCA
ATTCTTTCACCTGCCCTAATGGATGTACCTTATAGGTTAAATGAGATCACAAAAGAAAAG
GAGCAATGTTGTGTTTCTCTAGCTGCAGGCTTACCTCATTTTTCTTCTGGTATTTTCCGC
TGCTGGGGAAGGGATACTTTTATTGCACTTAGAGGTATACTGCTGATTACTGGACGCTAT
GTAGAAGCCAGGAATATTATTTTAGCATTTGCGGGTACCCTGAGGCATGGTCTCATTCCT
AATCTACTGGGTGAAGGGATTTATGCCAGATACAATTGTCGGGATGCTGTGTGGTGGTGG
CTGCAGTGTATCCAGGATTACTGTAAAATGGTTCCAAATGGTCTAGACATTCTCAAGTGC
CCAGTTTCCAGAATGTATCCTACAGATGATTCTGCTCCTTTGCCTGCTGGCACACTGGAT
CAGCCATTGTTTGAAGTCATACAGGAAGCAATGCAAAAACACATGCAGGGCATACAGTTC
CGAGAAAGGAATGCTGGTCCCCAGATAGATCGAAACATGAAGGACGAAGGTTTTAATATA
ACTGCAGGAGTTGATGAAGAAACAGGATTTGTTTATGGAGGAAATCGTTTCAATTGTGGC
ACATGGATGGATAAAATGGGAGAAAGTGACAGAGCTAGAAACAGAGGAATCCCAGCCACA
CCAAGAGATGGGTCTGCTGTGGAAATTGTGGGCCTGAGTAAATCTGCTGTTCGCTGGTTG
CTGGAATTATCCAAAAAAAATATTTTCCCTTATCATGAAGTCACAGTAAAAAGACATGGA
AAGGCTATAAAGGTCTCATATGATGAGTGGAACAGAAAAATACAAGACAACTTTGAAAAG
CTATTTCATGTTTCCGAAGACCCTTCAGATTTAAATGAAAAGCATCCAAATCTGGTTCAC
AAACGTGGCATATACAAAGATAGTTATGGAGCTTCAAGTCCTTGGTGTGACTATCAGCTC
AGGCCTAATTTTACCATAGCAATGGTTGTGGCCCCTGAGCTCTTTACTACAGAAAAAGCA
GGGAAAGCTTTGGAGATTGCAGAAAAAAAATTGCTTGGTCCCCTTGGCATGAAAACTTTA
GATCCAGATGATATGGTTTACTGTGGAATTTATGACAATGCATTAGACAATGACAACTAC
AATCTTGCTAAAGGTTTCAATTATCACCAAGGACCTGAGTGGCTGTGGCCTATTGGGTAT
TTTCTTCGTGCAAAATTATATTTTTCCAGATTGATGGGCCCGGAGACTACTGCAAAGACT
ATAGTTTTGGTTAAAAATGTTCTTTCCCGACATTATGTTCATCTTGAGAGATCCCCTTGG
AAAGGACTTCCAGAACTGACCAATGAGAATGCCCAGTACTGTCCTTTCAGCTGTGAAACA
CAAGCCTGGTCAATTGCTACTATTCTTGAGACACTTTATGATTTATAG
Enzyme 1 GenBank Gene ID M85168 Link Image
Enzyme 1 GeneCard ID AGL Link Image
Enzyme 1 GenAtlas ID AGL Link Image
Enzyme 1 HGNC ID HGNC:321 Link Image
Enzyme 1 Chromosome Location 1
Enzyme 1 Locus 1p21
Enzyme 1 SNPs SNPJam Report Link Image
Enzyme 1 General References
  1. Yang BZ, Ding JH, Enghild JJ, Bao Y, Chen YT: Molecular cloning and nucleotide sequence of cDNA encoding human muscle glycogen debranching enzyme. J Biol Chem. 1992 May 5;267(13):9294-9. [PubMed Link Image]
  2. Bao Y, Dawson TL Jr, Chen YT: Human glycogen debranching enzyme gene (AGL): complete structural organization and characterization of the 5' flanking region. Genomics. 1996 Dec 1;38(2):155-65. [PubMed Link Image]
  3. Bao Y, Yang BZ, Dawson TL Jr, Chen YT: Isolation and nucleotide sequence of human liver glycogen debranching enzyme mRNA: identification of multiple tissue-specific isoforms. Gene. 1997 Sep 15;197(1-2):389-98. [PubMed Link Image]
  4. Okubo M, Horinishi A, Takeuchi M, Suzuki Y, Sakura N, Hasegawa Y, Igarashi T, Goto K, Tahara H, Uchimoto S, Omichi K, Kanno H, Hayasaka K, Murase T: Heterogeneous mutations in the glycogen-debranching enzyme gene are responsible for glycogen storage disease type IIIa in Japan. Hum Genet. 2000 Jan;106(1):108-15. [PubMed Link Image]
  5. Okubo M, Kanda F, Horinishi A, Takahashi K, Okuda S, Chihara K, Murase T: Glycogen storage disease type IIIa: first report of a causative missense mutation (G1448R) of the glycogen debranching enzyme gene found in a homozygous patient. Hum Mutat. 1999 Dec;14(6):542-3. [PubMed Link Image]
Enzyme 1 Metabolite References Not Available
Enzyme 2 [top]
Enzyme 2 ID 7564
Enzyme 2 Name Salivary alpha-amylase precursor
Enzyme 2 Synonyms
  1. 1,4-alpha-D-glucan glucanohydrolase
Enzyme 2 Gene Name AMY1A
Enzyme 2 Protein Sequence >Salivary alpha-amylase precursor 
MKLFWLLFTIGFCWAQYSSNTQQGRTSIVHLFEWRWVDIALECERYLAPKGFGGVQVSPP
NENVAIHNPFRPWWERYQPVSYKLCTRSGNEDEFRNMVTRCNNVGVRIYVDAVINHMCGN
AVSAGTSSTCGSYFNPGSRDFPAVPYSGWDFNDGKCKTGSGDIENYNDATQVRDCRLSGL
LDLALGKDYVRSKIAEYMNHLIDIGVAGFRIDASKHMWPGDIKAILDKLHNLNSNWFPEG
SKPFIYQEVIDLGGEPIKSSDYFGNGRVTEFKYGAKLGTVIRKWNGEKMSYLKNWGEGWG
FMPSDRALVFVDNHDNQRGHGAGGASILTFWDARLYKMAVGFMLAHPYGFTRVMSSYRWP
RYFENGKDVNDWVGPPNDNGVTKEVTINPDTTCGNDWVCEHRWRQIRNMVNFRNVVDGQP
FTNWYDNGSNQVAFGRGNRGFIVFNNDDWTFSLTLQTGLPAGTYCDVISGDKINGNCTGI
KIYVSDDGKAHFSISNSAEDPFIAIHAESKL
Enzyme 2 Number of Residues 511
Enzyme 2 Molecular Weight 57768
Enzyme 2 Theoretical pI 6.92
Enzyme 2 GO Classification
Function
  • alpha-amylase activity
  • amylase activity
  • 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 2 General Function Carbohydrate transport and metabolism
Enzyme 2 Specific Function Endohydrolysis of 1,4-alpha-D-glucosidic linkages in oligosaccharides and polysaccharides
Enzyme 2 Pathways
Enzyme 2 Reactions
  • Endohydrolysis of 1,4-alpha-D-glucosidic linkages in polysaccharides containing three or more 1,4-alpha-linked D-glucose units
Enzyme 2 Pfam Domain Function
Enzyme 2 Signals
  • 1-15
Enzyme 2 Transmembrane Regions Not Available
Enzyme 2 Essentiality Not Available
Enzyme 2 GenBank ID Protein 178585 Link Image
Enzyme 2 UniProtKB/Swiss-Prot ID P04745 Link Image
Enzyme 2 UniProtKB/Swiss-Prot Entry Name AMYS_HUMAN Link Image
Enzyme 2 PDB ID 1MFV Link Image
Enzyme 2 PDB File Show
Enzyme 2 3D Structure
Enzyme 2 Cellular Location Not Available
Enzyme 2 Gene Sequence >1536 bp 
ATGAAGCTCTTTTGGTTGCTTTTCACCATTGGGTTCTGCTGGGCTCAGTATTCCTCAAAT
ACACAACAAGGACGAACATCTATTGTTCATCTGTTTGAATGGCGATGGGTTGATATTGCT
CTTGAATGTGAGCGATATTTAGCTCCCAAGGGATTTGGAGGGGTTCAGGTCTCTCCACCA
AATGAAAATGTTGCCATTCACAACCCTTTCAGACCTTGGTGGGAAAGATACCAACCAGTT
AGCTATAAATTATGCACAAGATCTGGAAATGAAGATGAATTTAGAAACATGGTGACTAGA
TGCAACAATGTTGGGGTTCGTATTTATGTGGATGCTGTAATTAATCATATGTGTGGTAAT
GCTGTGAGTGCAGGAACAAGCAGTACCTGTGGAAGTTACTTCAACCCTGGAAGTAGGGAC
TTTCCAGCAGTCCCATATTCTGGATGGGATTTTAATGATGGTAAATGTAAAACTGGAAGT
GGAGATATCGAGAACTATAATGATGCTACTCAGGTCAGAGATTGTCGTCTGTCTGGTCTT
CTCGATCTTGCACTGGGGAAGGATTATGTGCGTTCTAAGATTGCCGAATATATGAACCAT
CTCATTGACATTGGTGTTGCAGGGTTCAGAATTGATGCTTCCAAGCACATGTGGCCTGGA
GACATAAAGGCAATTTTGGACAAACTGCATAATCTAAACAGTAACTGGTTCCCGGAAGGT
AGTAAACCTTTCATTTACCAGGAGGTAATTGATCTGGGTGGTGAGCCAATTAAAAGCAGT
GACTACTTTGGTAATGGCCGGGTGACAGAATTCAAGTATGGTGCAAAACTCGGCACAGTT
ATTCGCAAGTGGAATGGAGAGAAGATGTCTTACTTAAAGAACTGGGGAGAAGGTTGGGGT
TTCATGCCTTCTGACAGAGCGCTTGTCTTTGTGGATAACCATGACAATCAACGAGGACAT
GGCGCTGGAGGAGCCTCTATACTTACCTTCTGGGATGCTAGGCTGTACAAAATGGCAGTT
GGATTTATGCTTGCTCATCCTTATGGATTTACACGAGTAATGTCAAGCTACCGTTGGCCA
AGATATTTTGAAAATGGAAANGATGTTAATGATTGGGTTGGGCCACCAAATGATAATGGA
GTAACTAAAGAAGTTACTATTAATCCAGACACTACTTGTGGCAATGACTGGGTCTGTGAA
CATCGATGGCGCCAAATAAGGAACATGGTTAATTTCCGCAATGTAGTGGATGGCCAGCCT
TTTACAAACTGGTATGATAATGGGAGCAACCAAGTGGCTTTTGGGAGAGGAAACAGAGGA
TTCATTGTTTTCAACAATGATGACTGGACATTTTCTTTAACTTTGCAAACTGGTCTTCCT
GCTGGCACATACTGTGATGTCATTTCTGGAGATAAAATTAATGGCAACTGCACAGGCATT
AAAATCTACGTTTCTGATGATGGCAAAGCTCATTTTTCTATTAGTAACTCTGCTGAAGAT
CCATTTATTGCAATTCATGCTGAATCTAAATTGTAA
Enzyme 2 GenBank Gene ID M18786 Link Image
Enzyme 2 GeneCard ID AMY1A Link Image
Enzyme 2 GenAtlas ID AMY1A Link Image
Enzyme 2 HGNC ID HGNC:474 Link Image
Enzyme 2 Chromosome Location 1
Enzyme 2 Locus 1p21
Enzyme 2 SNPs SNPJam Report Link Image
Enzyme 2 General References
  1. Nishide T, Nakamura Y, Emi M, Yamamoto T, Ogawa M, Mori T, Matsubara K: Primary structure of human salivary alpha-amylase gene. Gene. 1986;41(2-3):299-304. [PubMed Link Image]
  2. Nishide T, Emi M, Nakamura Y, Matsubara K: Corrected sequences of cDNAs for human salivary and pancreatic alpha-amylases [corrected] Gene. 1984 May;28(2):263-70. [PubMed Link Image]
  3. Gumucio DL, Wiebauer K, Caldwell RM, Samuelson LC, Meisler MH: Concerted evolution of human amylase genes. Mol Cell Biol. 1988 Mar;8(3):1197-205. [PubMed Link Image]
  4. Bank RA, Hettema EH, Arwert F, Amerongen AV, Pronk JC: Electrophoretic characterization of posttranslational modifications of human parotid salivary alpha-amylase. Electrophoresis. 1991 Jan;12(1):74-9. [PubMed Link Image]
  5. Ramasubbu N, Ragunath C, Mishra PJ: Probing the role of a mobile loop in substrate binding and enzyme activity of human salivary amylase. J Mol Biol. 2003 Jan 31;325(5):1061-76. [PubMed Link Image]
Enzyme 2 Metabolite References Not Available
Enzyme 3 [top]
Enzyme 3 ID 8603
Enzyme 3 Name Maltase-glucoamylase, intestinal [Includes: Maltase
Enzyme 3 Synonyms
  1. Alpha-glucosidase
  2. Glucoamylase
  3. Glucan 1,4-alpha- glucosidase]
Enzyme 3 Gene Name MGAM
Enzyme 3 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 3 Number of Residues 1857
Enzyme 3 Molecular Weight 209855
Enzyme 3 Theoretical pI 5.14
Enzyme 3 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 3 General Function Carbohydrate transport and metabolism
Enzyme 3 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 3 Pathways
Enzyme 3 Reactions
  • Hydrolysis of terminal, non-reducing 1,4-linked alpha-D-glucose residues with release of alpha-D-glucose
Enzyme 3 Pfam Domain Function
Enzyme 3 Signals
  • 1-35
Enzyme 3 Transmembrane Regions
  • 14-34
Enzyme 3 Essentiality Not Available
Enzyme 3 GenBank ID Protein 17648144 Link Image
Enzyme 3 UniProtKB/Swiss-Prot ID O43451 Link Image
Enzyme 3 UniProtKB/Swiss-Prot Entry Name MGA_HUMAN Link Image
Enzyme 3 PDB ID Not Available
Enzyme 3 Cellular Location Not Available
Enzyme 3 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 3 GenBank Gene ID AF016833 Link Image
Enzyme 3 GeneCard ID MGAM Link Image
Enzyme 3 GenAtlas ID MGAM Link Image
Enzyme 3 HGNC ID HGNC:7043 Link Image
Enzyme 3 Chromosome Location 7
Enzyme 3 Locus 7q34
Enzyme 3 SNPs SNPJam Report Link Image
Enzyme 3 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 3 Metabolite References Not Available
Enzyme 4 [top]
Enzyme 4 ID 11581
Enzyme 4 Name Neutral alpha-glucosidase C
Enzyme 4 Synonyms Not Available
Enzyme 4 Gene Name GANC
Enzyme 4 Protein Sequence >Neutral alpha-glucosidase C 
MEAAVKEEISVEDEAVDKNIFRDCNKIAFYRRQKQWLSKKSTYRALLDSVTTDEDSTRFQ
IINEASKVPLLAEIYGIEGNIFRLKINEETPLKPRFEVPDVLTSKPSTVRLISCSGDTGS
LILADGKGDLKCHITANPFKVDLVSEEEVVISINSLGQLYFEHLQILHKQRAAKENEEET
SVDTSQENQEDLGLWEEKFGKFVDIKANGPSSIGLDFSLHGFEHLYGIPQHAESHQLKNT
GDGDAYRLYNLDVYGYQIYDKMGIYGSVPYLLAHKLGRTIGIFWLNASETLVEINTEPAV
EYTLTQMGPVAAKQKVRSRTHVHWMSESGIIDVFLLTGPTPSDVFKQYSHLTGTQAMPPL
FSLGYHQCRWNYEDEQDVKAVDAGFDEHDIPYDAMWLDIEHTEGKRYFTWDKNRFPNPKR
MQELLRSKKRKLVVISDPHIKIDPDYSVYVKAKDQGFFVKNQEGEDFEGVCWPGLSSYLD
FTNPKVREWYSSLFAFPVYQGSTDILFLWNDMNEPSVFRGPEQTMQKNAIHHGNWEHREL
HNIYGFYHQMATAEGLIKRSKGKERPFVLTRSFFAGSQKYGAVWTGDNTAEWSNLKISIP
MLLTLSITGISFCGADIGGFIGNPETELLVRWYQAGAYQPFFRGHATMNTKRREPWLFGE
EHTRLIREAIRERYGLLPYWYSLFYHAHVASQPVMRPLWVEFPDELKTFDMEDEYMLGSA
LLVHPVTEPKATTVDVFLPGSNEVWYDYKTFAHWEGGCTVKIPVALDTIPVFQRGGSVIP
IKTTVGKSTGWMTESSYGLRVALSTKGSSVGELYLDDGHSFQYLHQKQFLHRKFSFCSSV
LINSFADQRGHYPSKCVVEKILVLGFRKEPSSVTTHSSDGKDQPVAFTYCAKTSILSLEK
LSLNIATDWEVRII
Enzyme 4 Number of Residues 914
Enzyme 4 Molecular Weight 104349
Enzyme 4 Theoretical pI Not Available
Enzyme 4 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 4 General Function Carbohydrate transport and metabolism
Enzyme 4 Specific Function Has alpha-glucosidase activity
Enzyme 4 Pathways
Enzyme 4 Reactions
  • H2O + Maltotriose --> D-Glucose + Maltose
Enzyme 4 Pfam Domain Function
Enzyme 4 Signals
  • None
Enzyme 4 Transmembrane Regions
  • None
Enzyme 4 Essentiality Not Available
Enzyme 4 GenBank ID Protein 25272046 Link Image
Enzyme 4 UniProtKB/Swiss-Prot ID Q8TET4 Link Image
Enzyme 4 UniProtKB/Swiss-Prot Entry Name GANC_HUMAN Link Image
Enzyme 4 PDB ID Not Available
Enzyme 4 Cellular Location Not Available
Enzyme 4 Gene Sequence Not Available
Enzyme 4 GenBank Gene ID AF545044 Link Image
Enzyme 4 GeneCard ID Not Available
Enzyme 4 GenAtlas ID GANC Link Image
Enzyme 4 HGNC ID HGNC:4139 Link Image
Enzyme 4 Chromosome Location Not Available
Enzyme 4 Locus Not Available
Enzyme 4 SNPs SNPJam Report Link Image
Enzyme 4 General References
  1. Hirschhorn R, Huie ML, Kasper JS: Computer assisted cloning of human neutral alpha-glucosidase C (GANC): a new paralog in the glycosyl hydrolase gene family 31. Proc Natl Acad Sci U S A. 2002 Oct 15;99(21):13642-6. Epub 2002 Oct 7. [PubMed Link Image]
Enzyme 4 Metabolite References Not Available
Enzyme 5 [top]
Enzyme 5 ID 13037
Enzyme 5 Name Uncharacterized protein GAA
Enzyme 5 Synonyms Not Available
Enzyme 5 Gene Name GAA
Enzyme 5 Protein Sequence >Uncharacterized protein GAA 
MGVRHPPCSHRLLAVCALVSLATAALLGHILLHDFLLVPRELSGSSPVLEETHPAHQQGA
SRPGPRDAQAHPGRPRAVPTQCDVPPNSRFDCAPDKAITQEQCEARGCCYIPAKQGLQGA
QMGQPWCFFPPSYPSYKLENLSSSEMGYTATLTRTTPTFFPKDILTLRLDVMMETENRLH
FTIKDPANRRYEVPLETPHVHSRAPSPLYSVEFSEEPFGVIVRRQLDGRVLLNTTVAPLF
FADQFLQLSTSLPSQYITGLAEHLSPLMLSTSWTRITLWNRDLAPTPGANLYGSHPFYLA
LEDGGSAHGVFLLNSNAMDVVLQPSPALSWRSTGGILDVYIFLGPEPKSVVQQYLDVVGY
PFMPPYWGLGFHLCRWGYSSTAITRQVVENMTRAHFPLDVQWNDLDYMDSRRDFTFNKDG
FRDFPAMVQELHQGGRRYMMIVDPAISSSGPAGSYRPYDEGLRRGVFITNETGQPLIGKV
WPGSTAFPDFTNPTALAWWEDMVAEFHDQVPFDGMWIDMNEPSNFIRGSEDGCPNNELEN
PPYVPGVVGGTLQAATICASSHQFLSTHYNLHNLYGLTEAIASHRALVKARGTRPFVISR
STFAGHGRYAGHWTGDVWSSWEQLASSVPEILQFNLLGVPLVGADVCGFLGNTSEELCVR
WTQLGAFYPFMRNHNSLLSLPQEPYSFSEPAQQAMRKALTLRYALLPHLYTLFHQAHVAG
ETVARPLFLEFPKDSSTWTVDHQLLWGEALLITPVLQAGKAEVTGYFPLGTWYDLQTVPV
EALGSLPPPPAAPREPAIHSEGQWVTLPAPLDTINVHLRAGYIIPLQGPGLTTTESRQQP
MALAVALTKGGEARGELFWDDGESLEVLERGAYTQVIFLARNNTIVNELVRVTSEGAGLQ
LQKVTVLGVATAPQQVLSNGVPVSNFTYSPDTKARGPRVLDICVSLLMGEQFLVSWC
Enzyme 5 Number of Residues 957
Enzyme 5 Molecular Weight 105862
Enzyme 5 Theoretical pI 6.04
Enzyme 5 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
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Enzyme 5 General Function Carbohydrate transport and metabolism
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 A6NFM4 Link Image
Enzyme 5 UniProtKB/Swiss-Prot Entry Name A6NFM4_HUMAN Link Image
Enzyme 5 PDB ID Not Available
Enzyme 5 Cellular Location Not Available
Enzyme 5 Gene Sequence Not Available
Enzyme 5 GenBank Gene ID AC087741 Link Image
Enzyme 5 GeneCard ID A6NFM4 Link Image
Enzyme 5 GenAtlas ID GAA Link Image
Enzyme 5 HGNC ID HGNC:4065 Link Image
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