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Human Metabolome Database Version 2.5

 

Showing metabocard for Melibiose (HMDB00048)

Legend: metabolite field enzyme field

Version 2.5
Creation Date 2005-11-16 15:48:42
Update Date 2009-05-05 20:57:39
Accession Number HMDB00048
Secondary Accession Numbers Not Available
Common Name Melibiose
Description Melibiose is disaccharide consisting of one galactose and one glucose moiety in an alpha (1-6) glycosidic linkage. This sugar is produced and metabolized only by enteric and lactic acid bacteria and other microbes. It is not an endogenous metabolite but may be obtained from the consumption of partially fermented molasses, brown sugar or honey. Antibodies to melibiose will appear in individuals affected by Chagas' disease (Trypanosoma cruzi infection). Melibiose is not metabolized by humans, but can be broken down by gut microflora, such as E. coli. In fact, E. coli is able to utilize melibiose as a sole source of carbon. Melibiose is first imported by the melibiose permease, MelB and then converted to β-D-glucose and β-D-galactose by the α-galactosidase encoded by melA. Because of its poor digestability Melibiose (along with rhamnose) can be used together for noninvasive intestinal mucosa barrier testing. This test can be used to assess malabsorption or impairment of intestinal permeability. Recent studies with dietary melibiose have shown that can strongly affected the Th cell responses to an ingested antigen. It has been suggested that melibiose could be used to enhance the induction of oral tolerance. (PMID 17986780)
Synonyms
  1. 6-(D-galactosido)-D-glucose
  2. 6-(a-D-galactosido)-D-glucose
  3. 6-O-Hexopyranosylhexose
  4. 6-O-a-D-galactopyranosyl-D-Glucose
  5. 6-O-alpha-D-galactopyranosyl-D-Glucose
  6. D-(+)-Melibiose
  7. D-Melibiose
  8. Melibiose
  9. Mellibiose
  10. alpha-D-Melibiose
  11. alpha-Melibiose
  12. 6-(D-galactosido)-delta-glucose
  13. 6-(a-delta-galactosido)-delta-glucose
  14. 6-O-alpha-delta-galactopyranosyl-delta-Glucose
  15. delta-(+)-Melibiose
  16. delta-Melibiose
  17. alpha-delta-Melibiose
Chemical IUPAC Name 2,3,4,5-tetrahydroxy-6-[3,4,5-trihydroxy-6-(hydroxymethyl)oxan-2-yl]oxy-hexanal
Chemical Formula C12H22O11
Chemical Structure Structure
Chemical Taxonomy
Kingdom
  • Organic
Super Class
  • Carbohydrates and Carbohydrate conjugates
Class
  • Carbohydrates
Sub Class
  • Disaccharides
Family
  • Microbial Metabolite
Species
  • hemiacetal
  • acetal
  • primary alcohol
  • secondary alcohol
  • 1,2-diol
  • heterocyclic compound
Biofunction
—
Application
—
Source
  • Exogenous
Average Molecular Weight 342.297
Monoisotopic Molecular Weight 342.116211
Isomeric SMILES OC[C@H]1O[C@H](OC[C@H]2OC(O)[C@H](O)[C@@H](O)[C@@H]2O)[C@H](O)[C@@H](O)[C@H]1O
Canonical SMILES OCC1OC(OCC2OC(O)C(O)C(O)C2O)C(O)C(O)C1O
KEGG Compound ID C05402 Link Image
BioCyc ID MELIBIOSE Link Image
BiGG ID Not Available
Wikipedia Link Not Available
NuGOwiki Link HMDB00048 Link Image
Metagene Link HMDB00048 Link Image
METLIN ID 3478 Link Image
PubChem Compound 440658 Link Image
PubChem Substance 7769 Link Image
ChEBI ID 28053 Link Image
CAS Registry Number 585-99-9
InChI Identifier InChI=1/C12H22O11/c13-1-3-5(14)8(17)10(19)12(23-3)21-2-4-6(15)7(16)9(18)11(20)22-4/h3-20H,1-2H2/t3-,4-,5+,6-,7+,8+,9-,10-,11u,12+/m1/s1
Synthesis Reference Pictet, Ame; Vogel, Hans. The synthesis of melibiose. Helvetica Chimica Acta (1927), 10 280.
Melting Point (Experimental) 84 oC
Experimental Water Solubility 1000.0 mg/mL [MERCK INDEX (1996)] Source: PhysProp
Predicted Water Solubility 511.0 mg/mL [Predicted by ALOGPS] Calculated using ALOGPS
Physiological Charge 0
State Solid
Experimental LogP/Hydrophobicity Not Available Source: PhysProp
Predicted LogP/Hydrophobicity -3.00 [Predicted by ALOGPS]; -4.1 [Predicted by PubChem via XLOGP]; -5.30 [MEYLAN,WM & HOWARD,PH (1995)] Calculated using ALOGPS
Material Safety Data Sheet (MSDS)
MOL File Show
SDF File Show
PDB File Show
2D Structure
3D Structure
Experimental PDB ID Not Available
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
Not Available
Predicted 13C NMR Spectrum Show Image
Not Available
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 Not Available
BMRB Spectrum Not Available
Cellular Location
  • Extracellular
  • Cytoplasm (Predicted from LogP)
Biofluid Location
  • Urine
Tissue Location
Tissue References
Spleen —
Tissues Containing Microbial Flora —
Concentrations (Normal)
Biofluid Urine
Value < 0.1 umol/mmol creatinine
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Barboza Junior MS, Silva TM, Guerrant RL, Lima AA: Measurement of intestinal permeability using mannitol and lactulose in children with diarrheal diseases. Braz J Med Biol Res. 1999 Dec;32(12):1499-504. [PubMed Link Image]
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
General References
  1. Almeida IC, Milani SR, Gorin PA, Travassos LR: Complement-mediated lysis of Trypanosoma cruzi trypomastigotes by human anti-alpha-galactosyl antibodies. J Immunol. 1991 Apr 1;146(7):2394-400. [PubMed Link Image]
  2. Sharma A, Ahmed H, Allen HJ: Isolation of a melibiose-binding protein from human spleen. Glycoconj J. 1995 Feb;12(1):17-21. [PubMed Link Image]
  3. Steuer MK, Steuer M, Bonkowsky V, Gabius HJ, Hofstadter F: Characterization of sugar receptor expression by neoglycoproteins in oral and oropharyngeal squamous cell carcinomas. Eur Arch Otorhinolaryngol. 1995;252(5):292-7. [PubMed Link Image]
  4. Vaughan HA, Loveland BE, Sandrin MS: Gal alpha(1,3)Gal is the major xenoepitope expressed on pig endothelial cells recognized by naturally occurring cytotoxic human antibodies. Transplantation. 1994 Oct 27;58(8):879-82. [PubMed Link Image]
  5. Barboza Junior MS, Silva TM, Guerrant RL, Lima AA: Measurement of intestinal permeability using mannitol and lactulose in children with diarrheal diseases. Braz J Med Biol Res. 1999 Dec;32(12):1499-504. [PubMed Link Image]
  6. Furukawa K, Ying R, Nakajima T, Matsuki T: Hemagglutinins in fungus extracts and their blood group specificity. Exp Clin Immunogenet. 1995;12(4):223-31. [PubMed Link Image]
  7. Gibbons RJ, Qureshi JV: Inhibition of adsorption of Streptococcus mutans strains to saliva-treated hydroxyapatite by galactose and certain amines. Infect Immun. 1979 Dec;26(3):1214-7. [PubMed Link Image]
  8. Nicolopoulou A, Zoumbou K, Papageorgacopoulou N, Papapetropoulou M: Metabolic and compositional changes in Escherichia coli cells starved in seawater. Microbiol Res. 1994 Nov;149(4):343-50. [PubMed Link Image]
  9. Wu AM, Song SC, Chen YY, Gilboa-Garber N: Defining the carbohydrate specificities of aplysia gonad lectin exhibiting a peculiar D-galacturonic acid affinity. J Biol Chem. 2000 May 12;275(19):14017-24. [PubMed Link Image]
  10. Rietra PJ, Van den Bergh FA, Tager JM: Properties of the residual alpha-galactosidase activity in the tissues of a Fabry hemizygote. Clin Chim Acta. 1975 Aug 4;62(3):401-13. [PubMed Link Image]
  11. Colby SM, Harrington DJ, Russell RR: Identification and genetic characterisation of melibiose-negative isolates of Streptococcus mutans. Caries Res. 1995;29(5):407-12. [PubMed Link Image]
Metabolic Enzymes
  1. Alpha-galactosidase A precursor
  2. Maltase-glucoamylase, intestinal [Includes: Maltase
  3. Neutral alpha-glucosidase C
  4. Uncharacterized protein GAA
  5. Alpha-galactosidase
  6. Melibiose carrier protein
Enzyme 1 [top]
Enzyme 1 ID 5997
Enzyme 1 Name Alpha-galactosidase A precursor
Enzyme 1 Synonyms
  1. Melibiase
  2. Alpha-D- galactoside galactohydrolase
  3. Alpha-D-galactosidase A
  4. Agalsidase alfa
Enzyme 1 Gene Name GLA
Enzyme 1 Protein Sequence >Alpha-galactosidase A precursor 
MQLRNPELHLGCALALRFLALVSWDIPGARALDNGLARTPTMGWLHWERFMCNLDCQEEP
DSCISEKLFMEMAELMVSEGWKDAGYEYLCIDDCWMAPQRDSEGRLQADPQRFPHGIRQL
ANYVHSKGLKLGIYADVGNKTCAGFPGSFGYYDIDAQTFADWGVDLLKFDGCYCDSLENL
ADGYKHMSLALNRTGRSIVYSCEWPLYMWPFQKPNYTEIRQYCNHWRNFADIDDSWKSIK
SILDWTSFNQERIVDVAGPGGWNDPDMLVIGNFGLSWNQQVTQMALWAIMAAPLFMSNDL
RHISPQAKALLQDKDVIAINQDPLGKQGYQLRQGDNFEVWERPLSGLAWAVAMINRQEIG
GPRSYTIAVASLGKGVACNPACFITQLLPVKRKLGFYEWTSRLRSHINPTGTVLLQLENT
MQMSLKDLL
Enzyme 1 Number of Residues 429
Enzyme 1 Molecular Weight 48767
Enzyme 1 Theoretical pI 5.27
Enzyme 1 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 1 General Function Not Available
Enzyme 1 Specific Function Hydrolysis of terminal, non-reducing alpha-D- galactose residues in alpha-D-galactosides, including galactose oligosaccharides, galactomannans and galactohydrolase
Enzyme 1 Pathways
Enzyme 1 Reactions
  • Hydrolysis of terminal, non-reducing alpha-D-galactose residues in alpha-D-galactosides, including galactose oligosaccharides, galactomannans and galactohydrolase
Enzyme 1 Pfam Domain Function
Enzyme 1 Signals
  • 1-31
Enzyme 1 Transmembrane Regions Not Available
Enzyme 1 Essentiality Not Available
Enzyme 1 GenBank ID Protein 757912 Link Image
Enzyme 1 UniProtKB/Swiss-Prot ID P06280 Link Image
Enzyme 1 UniProtKB/Swiss-Prot Entry Name AGAL_HUMAN Link Image
Enzyme 1 PDB ID 1R47 Link Image
Enzyme 1 PDB File Show
Enzyme 1 3D Structure
Enzyme 1 Cellular Location Not Available
Enzyme 1 Gene Sequence >1290 bp 
ATGCAGCTGAGGAACCCAGAACTACATCTGGGCTGCGCGCTTGCGCTTCGCTTCCTGGCC
CTCGTTTCCTGGGACATCCCTGGGGCTAGAGCACTGGACAATGGATTGGCAAGGACGCCT
ACCATGGGCTGGCTGCACTGGGAGCGCTTCATGTGCAACCTTGACTGCCAGGAAGAGCCA
GATTCCTGCATCAGTGAGAAGCTCTTCATGGAGATGGCAGAGCTCATGGTCTCAGAAGGC
TGGAAGGATGCAGGTTATGAGTACCTCTGCATTGATGACTGTTGGATGGCTCCCCAAAGA
GATTCAGAAGGCAGACTTCAGGCAGACCCTCAGCGCTTTCCTCATGGGATTCGCCAGCTA
GCTAATTATGTTCACAGCAAAGGACTGAAGCTAGGGATTTATGCAGATGTTGGAAATAAA
ACCTGCGCAGGCTTCCCTGGGAGTTTTGGATACTACGACATTGATGCCCAGACCTTTGCT
GACTGGGGAGTAGATCTGCTAAAATTTGATGGTTGTTACTGTGACAGTTTGGAAAATTTG
GCAGATGGTTATAAGCACATGTCCTTGGCCCTGAATAGGACTGGCAGAAGCATTGTGTAC
TCCTGTGAGTGGCCTCTTTATATGTGGCCCTTTCAAAAGCCCAATTATACAGAAATCCGA
CAGTACTGCAATCACTGGCGAAATTTTGCTGACATTGATGATTCCTGGAAAAGTATAAAG
AGTATCTTGGACTGGACATCTTTTAACCAGGAGAGAATTGTTGATGTTGCTGGACCAGGG
GGTTGGAATGACCCAGATATGTTAGTGATTGGCAACTTTGGCCTCAGCTGGAATCAGCAA
GTAACTCAGATGGCCCTCTGGGCTATCATGGCTGCTCCTTTATTCATGTCTAATGACCTC
CGACACATCAGCCCTCAAGCCAAAGCTCTCCTTCAGGATAAGGACGTAATTGCCATCAAT
CAGGACCCCTTGGGCAAGCAAGGGTACCAGCTTAGACAGGGAGACAACTTTGAAGTGTGG
GAACGACCTCTCTCAGGCTTAGCCTGGGCTGTAGCTATGATAAACCGGCAGGAGATTGGT
GGACCTCGCTCTTATACCATCGCAGTTGCTTCCCTGGGTAAAGGAGTGGCCTGTAATCCT
GCCTGCTTCATCACACAGCTCCTCCCTGTGAAAAGGAAGCTAGGGTTCTATGAATGGACT
TCAAGGTTAAGAAGTCACATAAATCCCACAGGCACTGTTTTGCTTCAGCTAGAAAATACA
ATGCAGATGTCATTAAAAGACTTACTTTAA
Enzyme 1 GenBank Gene ID X05790 Link Image
Enzyme 1 GeneCard ID GLA Link Image
Enzyme 1 GenAtlas ID GLA Link Image
Enzyme 1 HGNC ID HGNC:4296 Link Image
Enzyme 1 Chromosome Location X
Enzyme 1 Locus Xq22
Enzyme 1 SNPs SNPJam Report Link Image
Enzyme 1 General References
  1. Tsuji S, Martin BM, Kaslow DC, Migeon BR, Choudary PV, Stubbleflied BK, Mayor JA, Murray GJ, Barranger JA, Ginns EI: Signal sequence and DNA-mediated expression of human lysosomal alpha-galactosidase A. Eur J Biochem. 1987 Jun 1;165(2):275-80. [PubMed Link Image]
  2. Kornreich R, Desnick RJ, Bishop DF: Nucleotide sequence of the human alpha-galactosidase A gene. Nucleic Acids Res. 1989 Apr 25;17(8):3301-2. [PubMed Link Image]
  3. Oeltjen JC, Liu X, Lu J, Allen RC, Muzny D, Belmont JW, Gibbs RA: Sixty-nine kilobases of contiguous human genomic sequence containing the alpha-galactosidase A and Bruton's tyrosine kinase loci. Mamm Genome. 1995 May;6(5):334-8. [PubMed Link Image]
  4. Bishop DF, Calhoun DH, Bernstein HS, Hantzopoulos P, Quinn M, Desnick RJ: Human alpha-galactosidase A: nucleotide sequence of a cDNA clone encoding the mature enzyme. Proc Natl Acad Sci U S A. 1986 Jul;83(13):4859-63. [PubMed Link Image]
  5. Quinn M, Hantzopoulos P, Fidanza V, Calhoun DH: A genomic clone containing the promoter for the gene encoding the human lysosomal enzyme, alpha-galactosidase A. Gene. 1987;58(2-3):177-88. [PubMed Link Image]
  6. Bishop DF, Kornreich R, Desnick RJ: Structural organization of the human alpha-galactosidase A gene: further evidence for the absence of a 3' untranslated region. Proc Natl Acad Sci U S A. 1988 Jun;85(11):3903-7. [PubMed Link Image]
  7. Novo FJ, Kruszewski A, MacDermot KD, Goldspink G, Gorecki DC: Editing of human alpha-galactosidase RNA resulting in a pyrimidine to purine conversion. Nucleic Acids Res. 1995 Jul 25;23(14):2636-40. [PubMed Link Image]
  8. Eng CM, Desnick RJ: Molecular basis of Fabry disease: mutations and polymorphisms in the human alpha-galactosidase A gene. Hum Mutat. 1994;3(2):103-11. [PubMed Link Image]
  9. Koide T, Ishiura M, Iwai K, Inoue M, Kaneda Y, Okada Y, Uchida T: A case of Fabry's disease in a patient with no alpha-galactosidase A activity caused by a single amino acid substitution of Pro-40 by Ser. FEBS Lett. 1990 Jan 1;259(2):353-6. [PubMed Link Image]
  10. von Scheidt W, Eng CM, Fitzmaurice TF, Erdmann E, Hubner G, Olsen EG, Christomanou H, Kandolf R, Bishop DF, Desnick RJ: An atypical variant of Fabry's disease with manifestations confined to the myocardium. N Engl J Med. 1991 Feb 7;324(6):395-9. [PubMed Link Image]
  11. Sakuraba H, Oshima A, Fukuhara Y, Shimmoto M, Nagao Y, Bishop DF, Desnick RJ, Suzuki Y: Identification of point mutations in the alpha-galactosidase A gene in classical and atypical hemizygotes with Fabry disease. Am J Hum Genet. 1990 Nov;47(5):784-9. [PubMed Link Image]
  12. Bernstein HS, Bishop DF, Astrin KH, Kornreich R, Eng CM, Sakuraba H, Desnick RJ: Fabry disease: six gene rearrangements and an exonic point mutation in the alpha-galactosidase gene. J Clin Invest. 1989 Apr;83(4):1390-9. [PubMed Link Image]
  13. Ishii S, Sakuraba H, Suzuki Y: Point mutations in the upstream region of the alpha-galactosidase A gene exon 6 in an atypical variant of Fabry disease. Hum Genet. 1992 Apr;89(1):29-32. [PubMed Link Image]
  14. Eng CM, Resnick-Silverman LA, Niehaus DJ, Astrin KH, Desnick RJ: Nature and frequency of mutations in the alpha-galactosidase A gene that cause Fabry disease. Am J Hum Genet. 1993 Dec;53(6):1186-97. [PubMed Link Image]
  15. Davies JP, Winchester BG, Malcolm S: Mutation analysis in patients with the typical form of Anderson-Fabry disease. Hum Mol Genet. 1993 Jul;2(7):1051-3. [PubMed Link Image]
  16. Davies J, Christomanou H, Winchester B, Malcolm S: Detection of 8 new mutations in the alpha-galactosidase A gene in Fabry disease. Hum Mol Genet. 1994 Apr;3(4):667-9. [PubMed Link Image]
  17. Eng CM, Niehaus DJ, Enriquez AL, Burgert TS, Ludman MD, Desnick RJ: Fabry disease: twenty-three mutations including sense and antisense CpG alterations and identification of a deletional hot-spot in the alpha-galactosidase A gene. Hum Mol Genet. 1994 Oct;3(10):1795-9. [PubMed Link Image]
  18. Okumiya T, Ishii S, Takenaka T, Kase R, Kamei S, Sakuraba H, Suzuki Y: Galactose stabilizes various missense mutants of alpha-galactosidase in Fabry disease. Biochem Biophys Res Commun. 1995 Sep 25;214(3):1219-24. [PubMed Link Image]
  19. Okumiya T, Ishii S, Kase R, Kamei S, Sakuraba H, Suzuki Y: Alpha-galactosidase gene mutations in Fabry disease: heterogeneous expressions of mutant enzyme proteins. Hum Genet. 1995 May;95(5):557-61. [PubMed Link Image]
  20. Madsen KM, Hasholt L, Sorensen SA, Fermer ML, Dahl N: Two novel mutations (L32P) and (G85N) among five different missense mutations in six Danish families with Fabry's disease. Hum Mutat. 1995;5(3):277-8. [PubMed Link Image]
  21. Nakao S, Takenaka T, Maeda M, Kodama C, Tanaka A, Tahara M, Yoshida A, Kuriyama M, Hayashibe H, Sakuraba H, et al.: An atypical variant of Fabry's disease in men with left ventricular hypertrophy. N Engl J Med. 1995 Aug 3;333(5):288-93. [PubMed Link Image]
  22. Davies JP, Eng CM, Hill JA, Malcolm S, MacDermot K, Winchester B, Desnick RJ: Fabry disease: fourteen alpha-galactosidase A mutations in unrelated families from the United Kingdom and other European countries. Eur J Hum Genet. 1996;4(4):219-24. [PubMed Link Image]
  23. Cariolou MA, Christodoulides M, Manoli P, Kokkofitou A, Tsambaos D: Novel trinucleotide deletion in Fabry's disease. Hum Genet. 1996 Apr;97(4):468-70. [PubMed Link Image]
  24. Germain D, Biasotto M, Tosi M, Meo T, Kahn A, Poenaru L: Fluorescence-assisted mismatch analysis (FAMA) for exhaustive screening of the alpha-galactosidase A gene and detection of carriers in Fabry disease. Hum Genet. 1996 Dec;98(6):719-26. [PubMed Link Image]
  25. Blanch LC, Meaney C, Morris CP: A sensitive mutation screening strategy for Fabry disease: detection of nine mutations in the alpha-galactosidase A gene. Hum Mutat. 1996;8(1):38-43. [PubMed Link Image]
  26. Redonnet-Vernhet I, Ploos van Amstel JK, Jansen RP, Wevers RA, Salvayre R, Levade T: Uneven X inactivation in a female monozygotic twin pair with Fabry disease and discordant expression of a novel mutation in the alpha-galactosidase A gene. J Med Genet. 1996 Aug;33(8):682-8. [PubMed Link Image]
  27. Takata T, Okumiya T, Hayashibe H, Shimmoto M, Kase R, Itoh K, Utsumi K, Kamei S, Sakuraba H: Screening and detection of gene mutations in Japanese patients with Fabry disease by non-radioactive single-stranded conformation polymorphism analysis. Brain Dev. 1997 Mar;19(2):111-6. [PubMed Link Image]
  28. Eng CM, Ashley GA, Burgert TS, Enriquez AL, D'Souza M, Desnick RJ: Fabry disease: thirty-five mutations in the alpha-galactosidase A gene in patients with classic and variant phenotypes. Mol Med. 1997 Mar;3(3):174-82. [PubMed Link Image]
  29. Miyazaki T, Kajita M, Ohmori S, Mizutani N, Niwa T, Murata Y, Seo H: A novel mutation (E358K) in the alpha-galactosidase A gene detected in a Japanese family with Fabry disease. Hum Mutat. 1998;Suppl 1:S139-40. [PubMed Link Image]
  30. Okumiya T, Kawamura O, Itoh K, Kase R, Ishii S, Kamei S, Sakuraba H: Novel missense mutation (M72V) of alpha-galactosidase gene and its expression product in an atypical Fabry hemizygote. Hum Mutat. 1998;Suppl 1:S213-6. [PubMed Link Image]
  31. Guffon N, Froissart R, Chevalier-Porst F, Maire I: Mutation analysis in 11 French patients with Fabry disease. Hum Mutat. 1998;Suppl 1:S288-90. [PubMed Link Image]
  32. Germain DP, Poenaru L: Fabry disease: identification of novel alpha-galactosidase A mutations and molecular carrier detection by use of fluorescent chemical cleavage of mismatches. Biochem Biophys Res Commun. 1999 Apr 21;257(3):708-13. [PubMed Link Image]
  33. Beyer EM, Karpova EA, Udalova OV, Ploos van Amstel JK, van Diggelen OP, Tsvetkova IV: The multiple cases of Fabry disease in a Russian family caused by an E341K amino acid substitution in the alpha-galactosidase A. Clin Chim Acta. 1999 Feb;280(1-2):81-9. [PubMed Link Image]
  34. Topaloglu AK, Ashley GA, Tong B, Shabbeer J, Astrin KH, Eng CM, Desnick RJ: Twenty novel mutations in the alpha-galactosidase A gene causing Fabry disease. Mol Med. 1999 Dec;5(12):806-11. [PubMed Link Image]
  35. Lee JK, Kim GH, Kim JS, Kim KK, Lee MC, Yoo HW: Identification of four novel mutations in five unrelated Korean families with Fabry disease. Clin Genet. 2000 Sep;58(3):228-33. [PubMed Link Image]
  36. Ashton-Prolla P, Tong B, Shabbeer J, Astrin KH, Eng CM, Desnick RJ: Fabry disease: twenty-two novel mutations in the alpha-galactosidase A gene and genotype/phenotype correlations in severely and mildly affected hemizygotes and heterozygotes. J Investig Med. 2000 Jul;48(4):227-35. [PubMed Link Image]
  37. Germain DP, Salard D, Fellmann F, Azibi K, Caillaud C, Bernard MC, Poenaru L: Identification of a novel de novo mutation (G373D) in the alpha-galactosidase A gene (GLA) in a patient affected with Fabry disease. Hum Mutat. 2001 Apr;17(4):353. [PubMed Link Image]
  38. Blaydon D, Hill J, Winchester B: Fabry disease: 20 novel GLA mutations in 35 families. Hum Mutat. 2001 Nov;18(5):459. [PubMed Link Image]
Enzyme 1 Metabolite References Not Available
Enzyme 2 [top]
Enzyme 2 ID 8603
Enzyme 2 Name Maltase-glucoamylase, intestinal [Includes: Maltase
Enzyme 2 Synonyms
  1. Alpha-glucosidase
  2. Glucoamylase
  3. Glucan 1,4-alpha- glucosidase]
Enzyme 2 Gene Name MGAM
Enzyme 2 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 2 Number of Residues 1857
Enzyme 2 Molecular Weight 209855
Enzyme 2 Theoretical pI 5.14
Enzyme 2 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 2 General Function Carbohydrate transport and metabolism
Enzyme 2 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 2 Pathways
Enzyme 2 Reactions
  • Hydrolysis of terminal, non-reducing 1,4-linked alpha-D-glucose residues with release of alpha-D-glucose
Enzyme 2 Pfam Domain Function
Enzyme 2 Signals
  • 1-35
Enzyme 2 Transmembrane Regions
  • 14-34
Enzyme 2 Essentiality Not Available
Enzyme 2 GenBank ID Protein 17648144 Link Image
Enzyme 2 UniProtKB/Swiss-Prot ID O43451 Link Image
Enzyme 2 UniProtKB/Swiss-Prot Entry Name MGA_HUMAN Link Image
Enzyme 2 PDB ID Not Available
Enzyme 2 Cellular Location Not Available
Enzyme 2 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 2 GenBank Gene ID AF016833 Link Image
Enzyme 2 GeneCard ID MGAM Link Image
Enzyme 2 GenAtlas ID MGAM Link Image
Enzyme 2 HGNC ID HGNC:7043 Link Image
Enzyme 2 Chromosome Location 7
Enzyme 2 Locus 7q34
Enzyme 2 SNPs SNPJam Report Link Image
Enzyme 2 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 2 Metabolite References Not Available
Enzyme 3 [top]
Enzyme 3 ID 11581
Enzyme 3 Name Neutral alpha-glucosidase C
Enzyme 3 Synonyms Not Available
Enzyme 3 Gene Name GANC
Enzyme 3 Protein Sequence >Neutral alpha-glucosidase C 
MEAAVKEEISVEDEAVDKNIFRDCNKIAFYRRQKQWLSKKSTYRALLDSVTTDEDSTRFQ
IINEASKVPLLAEIYGIEGNIFRLKINEETPLKPRFEVPDVLTSKPSTVRLISCSGDTGS
LILADGKGDLKCHITANPFKVDLVSEEEVVISINSLGQLYFEHLQILHKQRAAKENEEET
SVDTSQENQEDLGLWEEKFGKFVDIKANGPSSIGLDFSLHGFEHLYGIPQHAESHQLKNT
GDGDAYRLYNLDVYGYQIYDKMGIYGSVPYLLAHKLGRTIGIFWLNASETLVEINTEPAV
EYTLTQMGPVAAKQKVRSRTHVHWMSESGIIDVFLLTGPTPSDVFKQYSHLTGTQAMPPL
FSLGYHQCRWNYEDEQDVKAVDAGFDEHDIPYDAMWLDIEHTEGKRYFTWDKNRFPNPKR
MQELLRSKKRKLVVISDPHIKIDPDYSVYVKAKDQGFFVKNQEGEDFEGVCWPGLSSYLD
FTNPKVREWYSSLFAFPVYQGSTDILFLWNDMNEPSVFRGPEQTMQKNAIHHGNWEHREL
HNIYGFYHQMATAEGLIKRSKGKERPFVLTRSFFAGSQKYGAVWTGDNTAEWSNLKISIP
MLLTLSITGISFCGADIGGFIGNPETELLVRWYQAGAYQPFFRGHATMNTKRREPWLFGE
EHTRLIREAIRERYGLLPYWYSLFYHAHVASQPVMRPLWVEFPDELKTFDMEDEYMLGSA
LLVHPVTEPKATTVDVFLPGSNEVWYDYKTFAHWEGGCTVKIPVALDTIPVFQRGGSVIP
IKTTVGKSTGWMTESSYGLRVALSTKGSSVGELYLDDGHSFQYLHQKQFLHRKFSFCSSV
LINSFADQRGHYPSKCVVEKILVLGFRKEPSSVTTHSSDGKDQPVAFTYCAKTSILSLEK
LSLNIATDWEVRII
Enzyme 3 Number of Residues 914
Enzyme 3 Molecular Weight 104349
Enzyme 3 Theoretical pI Not Available
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 Has alpha-glucosidase activity
Enzyme 3 Pathways
Enzyme 3 Reactions
  • H2O + Maltotriose --> D-Glucose + Maltose
Enzyme 3 Pfam Domain Function
Enzyme 3 Signals
  • None
Enzyme 3 Transmembrane Regions
  • None
Enzyme 3 Essentiality Not Available
Enzyme 3 GenBank ID Protein 25272046 Link Image
Enzyme 3 UniProtKB/Swiss-Prot ID Q8TET4 Link Image
Enzyme 3 UniProtKB/Swiss-Prot Entry Name GANC_HUMAN Link Image
Enzyme 3 PDB ID Not Available
Enzyme 3 Cellular Location Not Available
Enzyme 3 Gene Sequence Not Available
Enzyme 3 GenBank Gene ID AF545044 Link Image
Enzyme 3 GeneCard ID Not Available
Enzyme 3 GenAtlas ID GANC Link Image
Enzyme 3 HGNC ID HGNC:4139 Link Image
Enzyme 3 Chromosome Location Not Available
Enzyme 3 Locus Not Available
Enzyme 3 SNPs SNPJam Report Link Image
Enzyme 3 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 3 Metabolite References Not Available
Enzyme 4 [top]
Enzyme 4 ID 13037
Enzyme 4 Name Uncharacterized protein GAA
Enzyme 4 Synonyms Not Available
Enzyme 4 Gene Name GAA
Enzyme 4 Protein Sequence >Uncharacterized protein GAA 
MGVRHPPCSHRLLAVCALVSLATAALLGHILLHDFLLVPRELSGSSPVLEETHPAHQQGA
SRPGPRDAQAHPGRPRAVPTQCDVPPNSRFDCAPDKAITQEQCEARGCCYIPAKQGLQGA
QMGQPWCFFPPSYPSYKLENLSSSEMGYTATLTRTTPTFFPKDILTLRLDVMMETENRLH
FTIKDPANRRYEVPLETPHVHSRAPSPLYSVEFSEEPFGVIVRRQLDGRVLLNTTVAPLF
FADQFLQLSTSLPSQYITGLAEHLSPLMLSTSWTRITLWNRDLAPTPGANLYGSHPFYLA
LEDGGSAHGVFLLNSNAMDVVLQPSPALSWRSTGGILDVYIFLGPEPKSVVQQYLDVVGY
PFMPPYWGLGFHLCRWGYSSTAITRQVVENMTRAHFPLDVQWNDLDYMDSRRDFTFNKDG
FRDFPAMVQELHQGGRRYMMIVDPAISSSGPAGSYRPYDEGLRRGVFITNETGQPLIGKV
WPGSTAFPDFTNPTALAWWEDMVAEFHDQVPFDGMWIDMNEPSNFIRGSEDGCPNNELEN
PPYVPGVVGGTLQAATICASSHQFLSTHYNLHNLYGLTEAIASHRALVKARGTRPFVISR
STFAGHGRYAGHWTGDVWSSWEQLASSVPEILQFNLLGVPLVGADVCGFLGNTSEELCVR
WTQLGAFYPFMRNHNSLLSLPQEPYSFSEPAQQAMRKALTLRYALLPHLYTLFHQAHVAG
ETVARPLFLEFPKDSSTWTVDHQLLWGEALLITPVLQAGKAEVTGYFPLGTWYDLQTVPV
EALGSLPPPPAAPREPAIHSEGQWVTLPAPLDTINVHLRAGYIIPLQGPGLTTTESRQQP
MALAVALTKGGEARGELFWDDGESLEVLERGAYTQVIFLARNNTIVNELVRVTSEGAGLQ
LQKVTVLGVATAPQQVLSNGVPVSNFTYSPDTKARGPRVLDICVSLLMGEQFLVSWC
Enzyme 4 Number of Residues 957
Enzyme 4 Molecular Weight 105862
Enzyme 4 Theoretical pI 6.04
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 Not Available
Enzyme 4 Pathways Not Available
Enzyme 4 Reactions Not Available
Enzyme 4 Pfam Domain Function
Enzyme 4 Signals
  • None
Enzyme 4 Transmembrane Regions
  • None
Enzyme 4 Essentiality Not Available
Enzyme 4 GenBank ID Protein Not Available
Enzyme 4 UniProtKB/Swiss-Prot ID A6NFM4 Link Image
Enzyme 4 UniProtKB/Swiss-Prot Entry Name A6NFM4_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 AC087741 Link Image
Enzyme 4 GeneCard ID A6NFM4 Link Image
Enzyme 4 GenAtlas ID GAA Link Image
Enzyme 4 HGNC ID HGNC:4065 Link Image
Enzyme 4 Chromosome Location Not Available
Enzyme 4 Locus Not Available
Enzyme 4 SNPs SNPJam Report Link Image
Enzyme 4 General References Not Available
Enzyme 4 Metabolite References Not Available
Enzyme 5 [top]
Enzyme 5 ID 14856
Enzyme 5 Name Alpha-galactosidase
Enzyme 5 Synonyms
  1. Melibiase
Enzyme 5 Gene Name melA
Enzyme 5 Protein Sequence >Alpha-galactosidase 
MMSAPKITFIGAGSTIFVKNILGDVFHREALKTAHIALMDIDPTRLEESHIVVRKLMDSA
GASGKITCHTQQKEALEDADFVVVAFQIGGYEPCTVTDFEVCKRHGLEQTIADTLGPGGI
MRALRTIPHLWQICEDMTEVCPDATMLNYVNPMAMNTWAMYARYPHIKQVGLCHSVQGTA
EELARDLNIDPATLRYRCAGINHMAFYLELERKTADGSYVNLYPELLAAYEAGQAPKPNI
HGNTRCQNIVRYEMFKKLGYFVTESSEHFAEYTPWFIKPGREDLIERYKVPLDEYPKRCV
EQLANWHKELEEYKKASRIDIKPSREYASTIMNAIWTGEPSVIYGNVRNDGLIDNLPQGC
CVEVACLVDANGIQPTKVGTLPSHLAALMQTNINVQTLLTEAILTENRDRVYHAAMMDPH
TAAVLGIDEIYALVDDLIAAHGDWLPGWLHR
Enzyme 5 Number of Residues 451
Enzyme 5 Molecular Weight 50658
Enzyme 5 Theoretical pI 5.68
Enzyme 5 GO Classification
Function
  • catalytic activity
  • hydrolase activity
  • hydrolase activity, acting on glycosyl bonds
  • hydrolase activity, hydrolyzing O-glycosyl compounds
  • oxidoreductase activity
Process
  • carbohydrate metabolism
  • cellular metabolism
  • energy derivation by oxidation of organic compounds
  • generation of precursor metabolites and energy
  • macromolecule metabolism
  • main pathways of carbohydrate metabolism
  • metabolism
  • physiological process
  • tricarboxylic acid cycle intermediate metabolism
Component
—
Enzyme 5 General Function Carbohydrate transport and metabolism
Enzyme 5 Specific Function Hydrolysis of terminal, non-reducing alpha-D- galactose residues in alpha-D-galactosides, including galactose oligosaccharides, galactomannans and galactohydrolase
Enzyme 5 Pathways
Enzyme 5 Reactions
  • Hydrolysis of terminal, non-reducing alpha-D-galactose residues in alpha-D-galactosides, including galactose oligosaccharides, galactomannans and galactohydrolase ALL_REAC (other) R01101 R01103 R01104 R01194 R01329 R02926 R03618 R03634 R04019 R04470 R05549 R05961(G) R06002(G) R06070(G) R06091(G) R06093(G) R06094(G) R06096(G) R06142(G) R06152(G)
Enzyme 5 Pfam Domain Function
Enzyme 5 Signals
  • None
Enzyme 5 Transmembrane Regions
  • None
Enzyme 5 Essentiality Not Available
Enzyme 5 GenBank ID Protein 41991 Link Image
Enzyme 5 UniProtKB/Swiss-Prot ID P06720 Link Image
Enzyme 5 UniProtKB/Swiss-Prot Entry Name AGAL_ECOLI Link Image
Enzyme 5 PDB ID Not Available
Enzyme 5 Cellular Location Not Available
Enzyme 5 Gene Sequence >1356 bp 
ATGATGTCTGCACCCAAAATTACATTTATCGGCGCTGGTTCGACGATTTTCGTTAAAAAT
ATTCTTGGTGATGTGTTCCATCGCGAGGCGCTGAAAACGGCGCATATTGCCCTGATGGAC
ATTGACCCCACCCGCCTGGAAGAGTCGCATATTGTGGTGCGTAAGCTGATGGATTCAGCA
GGGGCCAGCGGCAAAATCACCTGCCACACCCAACAGAAAGAAGCCTTAGAGGATGCCGAT
TTTGTCGTGGTGGCATTTCAGATTGGCGGTTATGAACCTTGCACGGTGACTGATTTCGAG
GTCTGTAAGCGGCATGGTCTGGAACAAACCATTGCCGATACGTTGGGGCCGGGCGGTATT
ATGCGCGCGCTACGTACCATTCCGCATCTGTGGCAAATTTGCGAGGACATGACGGAAGTC
TGCCCCGATGCCACCATGCTCAACTATGTTAACCCAATGGCGATGAATACCTGGGCGATG
TATGCCCGCTATCCGCATATCAAACAGGTCGGGCTGTGCCATTCGGTGCAGGGAACGGCG
GAAGAGTTGGCGCGTGACCTCAATATCGACCCAGCTACGCTGCGTTACCGTTGCGCAGGT
ATCAACCATATGGCGTTTTACCTGGAGCTGGAGCGCAAAACCGCCGACGGCAGTTATGTG
AATCTCTACCCGGAACTGCTGGCGGCTTATGAAGCAGGGCAGGCACCGAAGCCGAATATT
CATGGCAATACTCGCTGCCAGAATATTGTGCGCTACGAAATGTTCAAAAAGCTGGGCTAT
TTCGTCACGGAATCGTCAGAACATTTTGCTGAGTACACACCGTGGTTTATTAAGCCAGGT
CGTGAGGATTTGATTGAGCGTTATAAAGTACCGCTGGATGAGTACCCGAAACGCTGCGTC
GAGCAGCTGGCGAACTGGCATAAAGAGCTGGAGGAGTATAAAAAAGCCTCCCGGATTGAT
ATTAAACCGTCACGGGAATATGCCAGCACAATCATGAACGCTATCTGGACTGGCGAGCCG
AGTGTGATTTACGGCAACGTCCGTAACGATGGTTTGATTGATAACCTGCCACAAGGATGT
TGCGTGGAAGTAGCCTGTCTGGTTGATGCTAATGGCATTCAGCCGACCAAAGTCGGTACG
CTACCTTCGCATCTGGCCGCCCTGATGCAAACCAACATCAACGTACAGACGCTGCTGACC
GAAGCTATTCTTACGGAAAATCGCGACCGTGTTTACCACGCCGCGATGATGGACCCGCAT
ACTGCCGCCGTGCTGGGCATTGACGAAATATATGCTCTTGTTGACGACCTGATTGCCGCC
CACGGCGACTGGCTGCCAGGCTGGTTGCACCGTTAA
Enzyme 5 GenBank Gene ID X04894 Link Image
Enzyme 5 GeneCard ID Not Available
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
  1. Liljestrom PL, Liljestrom P: Nucleotide sequence of the melA gene, coding for alpha-galactosidase in Escherichia coli K-12. Nucleic Acids Res. 1987 Mar 11;15(5):2213-20. [PubMed Link Image]
  2. Burland V, Plunkett G 3rd, Sofia HJ, Daniels DL, Blattner FR: Analysis of the Escherichia coli genome VI: DNA sequence of the region from 92.8 through 100 minutes. Nucleic Acids Res. 1995 Jun 25;23(12):2105-19. [PubMed Link Image]
  3. Blattner FR, Plunkett G 3rd, Bloch CA, Perna NT, Burland V, Riley M, Collado-Vides J, Glasner JD, Rode CK, Mayhew GF, Gregor J, Davis NW, Kirkpatrick HA, Goeden MA, Rose DJ, Mau B, Shao Y: The complete genome sequence of Escherichia coli K-12. Science. 1997 Sep 5;277(5331):1453-74. [PubMed Link Image]
  4. Shimamoto T, Yazyu H, Futai M, Tsuchiya T: Nucleotide sequence of the promoter region of the melibiose operon of Escherichia coli. Biochem Biophys Res Commun. 1984 May 31;121(1):41-6. [PubMed Link Image]
  5. Nagao Y, Nakada T, Imoto M, Shimamoto T, Sakai S, Tsuda M, Tsuchiya T: Purification and analysis of the structure of alpha-galactosidase from Escherichia coli. Biochem Biophys Res Commun. 1988 Feb 29;151(1):236-41. [PubMed Link Image]
Enzyme 5 Metabolite References Not Available
Enzyme 6 [top]
Enzyme 6 ID 14857
Enzyme 6 Name Melibiose carrier protein
Enzyme 6 Synonyms
  1. Thiomethylgalactoside permease II
  2. Melibiose permease
  3. Na+
  4. Li+/melibiose symporter
  5. Melibiose transporter
Enzyme 6 Gene Name melB
Enzyme 6 Protein Sequence >Melibiose carrier protein 
MTTKLSYGFGAFGKDFAIGIVYMYLMYYYTDVVGLSVGLVGTLFLVARIWDAINDPIMGW
IVNATRSRWGKFKPWILIGTLANSVILFLLFSAHLFEGTTQIVFVCVTYILWGMTYTIMD
IPFWSLVPTITLDKREREQLVPYPRFFASLAGFVTAGVTLPFVNYVGGGDRGFGFQMFTL
VLIAFFIVSTIITLRNVHEVFSSDNQPSAEGSHLTLKAIVALIYKNDQLSCLLGMALAYN
VASNIITGFAIYYFSYVIGDADLFPYYLSYAGAANLVTLVFFPRLVKSLSRRILWAGASI
LPVLSCGVLLLMALMSYHNVVLIVIAGILLNVGTALFWVLQVIMVADIVDYGEYKLHVRC
ESIAYSVQTMVVKGGSAFAAFFIAVVLGMIGYVPNVEQSTQALLGMQFIMIALPTLFFMV
TLILYFRFYRLNGDTLRRIQIHLLDKYRKVPPEPVHADIPVGAVSDVKA
Enzyme 6 Number of Residues 469
Enzyme 6 Molecular Weight 52219
Enzyme 6 Theoretical pI 8.69
Enzyme 6 GO Classification
Function
  • transporter activity
Process
  • cation transport
  • cellular physiological process
  • ion transport
  • monovalent inorganic cation transport
  • physiological process
  • sodium ion transport
  • transport
Component
  • cell
  • membrane
Enzyme 6 General Function Carbohydrate transport and metabolism
Enzyme 6 Specific Function Responsible for melibiose transport. It is capable of using hydrogen, sodium, and lithium cations as coupling cations for cotransport, depending on the particular sugar transported (symport system)
Enzyme 6 Pathways Not Available
Enzyme 6 Reactions Not Available
Enzyme 6 Pfam Domain Function Not Available
Enzyme 6 Signals
  • None
Enzyme 6 Transmembrane Regions
  • 16-36 39-59 77-97 105-125 150-170 183-203 232-252 266-286 296-316 325-345 378-398 407-427
Enzyme 6 Essentiality Not Available
Enzyme 6 GenBank ID Protein 26986738 Link Image
Enzyme 6 UniProtKB/Swiss-Prot ID P02921 Link Image
Enzyme 6 UniProtKB/Swiss-Prot Entry Name MELB_ECOLI Link Image
Enzyme 6 PDB ID Not Available
Enzyme 6 Cellular Location Not Available
Enzyme 6 Gene Sequence >1410 bp 
ATGACTACAAAACTCAGTTATGGATTTGGAGCGTTCGGGAAGGATTTTGCGATCGGCATT
GTGTATATGTACCTCATGTATTACTACACCGATGTCGTCGGGCTGTCTGTGGGTTTGGTC
GGTACTTTGTTTCTGGTGGCGAGGATCTGGGATGCTATTAACGATCCGATTATGGGATGG
ATTGTAAATGCTACGCGATCGCGATGGGGTAAGTTCAAACCCTGGATCCTGATCGGTACG
TTGGCAAACTCTGTAATCTTATTTCTCCTCTTTAGTGCGCATCTGTTTGAAGGTACTACT
CAGATTGTCTTTGTTTGCGTGACCTACATCCTCTGGGGCATGACTTACACCATTATGGAT
ATTCCCTTCTGGTCGCTGGTTCCAACCATCACGCTCGATAAACGTGAGCGCGAACAACTG
GTTCCTTATCCGCGTTTTTTTGCCAGTCTGGCAGGCTTTGTTACGGCAGGTGTGACGCTA
CCATTTGTTAATTATGTCGGCGGTGGCGATCGGGGATTTGGCTTTCAGATGTTCACTCTG
GTACTGATCGCCTTTTTTATTGTTTCAACCATCATCACTCTGCGCAATGTGCATGAAGTC
TTTTCGTCAGACAATCAACCGTCTGCTGAAGGAAGCCATCTGACACTTAAAGCCATCGTT
GCGCTAATTTATAAAAACGATCAGCTTTCATGCCTCTTGGGTATGGCTCTTGCTTATAAT
GTAGCCAGCAACATTATTACCGGCTTTGCTATCTATTATTTCTCATATGTTATCGGTGAT
GCGGATTTGTTCCCCTATTATCTGTCGTATGCGGGAGCTGCTAACCTGGTGACGTTAGTA
TTCTTCCCACGCTTAGTTAAATCATTATCCCGACGCATTTTATGGGCCGGAGCATCTATT
CTTCCGGTGTTAAGCTGTGGTGTTCTCCTGTTAATGGCATTAATGAGCTATCACAACGTC
GTCCTCATTGTGATTGCGGGTATTTTGCTGAATGTGGGAACGGCGCTTTTCTGGGTATTA
CAGGTCATCATGGTGGCAGATATCGTTGATTACGGTGAATATAAACTGCACGTACGCTGT
GAAAGTATCGCTTACTCCGTGCAGACTATGGTGGTGAAGGGCGGTTCAGCCTTTGCGGCT
TTTTTCATTGCGGTTGTGTTAGGGATGATTGGCTATGTACCGAATGTTGAACAGTCTACG
CAAGCCCTATTAGGTATGCAGTTTATTATGATTGCTCTACCAACTCTGTTTTTCATGGTA
ACGCTGATTCTCTACTTCCGTTTCTATCGCCTCAATGGTGACACGCTGCGCAGGATCCAG
ATCCATCTGCTGGATAAATATCGCAAAGTACCGCCCGAGCCTGTTCATGCTGATATTCCG
GTCGGTGCAGTGAGTGATGTGAAAGCCTGA
Enzyme 6 GenBank Gene ID K01991 Link Image
Enzyme 6 GeneCard ID Not Available
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
  1. Yazyu H, Shiota-Niiya S, Shimamoto T, Kanazawa H, Futai M, Tsuchiya T: Nucleotide sequence of the melB gene and characteristics of deduced amino acid sequence of the melibiose carrier in Escherichia coli. J Biol Chem. 1984 Apr 10;259(7):4320-6. [PubMed Link Image]
  2. Burland V, Plunkett G 3rd, Sofia HJ, Daniels DL, Blattner FR: Analysis of the Escherichia coli genome VI: DNA sequence of the region from 92.8 through 100 minutes. Nucleic Acids Res. 1995 Jun 25;23(12):2105-19. [PubMed Link Image]
  3. Blattner FR, Plunkett G 3rd, Bloch CA, Perna NT, Burland V, Riley M, Collado-Vides J, Glasner JD, Rode CK, Mayhew GF, Gregor J, Davis NW, Kirkpatrick HA, Goeden MA, Rose DJ, Mau B, Shao Y: The complete genome sequence of Escherichia coli K-12. Science. 1997 Sep 5;277(5331):1453-74. [PubMed Link Image]
  4. Botfield MC, Naguchi K, Tsuchiya T, Wilson TH: Membrane topology of the melibiose carrier of Escherichia coli. J Biol Chem. 1992 Jan 25;267(3):1818-22. [PubMed Link Image]
  5. Pourcher T, Bibi E, Kaback HR, Leblanc G: Membrane topology of the melibiose permease of Escherichia coli studied by melB-phoA fusion analysis. Biochemistry. 1996 Apr 2;35(13):4161-8. [PubMed Link Image]
  6. Pourcher T, Deckert M, Bassilana M, Leblanc G: Melibiose permease of Escherichia coli: mutation of aspartic acid 55 in putative helix II abolishes activation of sugar binding by Na+ ions. Biochem Biophys Res Commun. 1991 Aug 15;178(3):1176-81. [PubMed Link Image]
Enzyme 6 Metabolite References Not Available