Glycoside hydrolasesEC 3.2.1. are a widespread group of enzymes that hydrolyse the glycosidic bond between two or more carbohydrates, or between a carbohydrate and a non-carbohydrate moiety. A classification system for glycoside hydrolases, based on sequence similarity, has led to the definition of >100 different families.[1][2][3] This classification is available on the CAZy web site,[4][5] and also discussed at CAZypedia, an online encyclopedia of carbohydrate active enzymes.[6][7]
Alpha-galactosidase (EC 3.2.1.22) (melibiase)[8] catalyzes the hydrolysis of melibiose into galactose and glucose. In man, the deficiency of this enzyme is the cause of Fabry's disease (X-linked sphingolipidosis). Alpha-galactosidase is present in a variety of organisms. There is a considerable degree of similarity in the sequence of alpha-galactosidase from various eukaryotic species. Escherichia coli alpha-galactosidase (gene melA), which requires NAD and magnesium as cofactors, is not structurally related to the eukaryotic enzymes; by contrast, an Escherichia coliplasmid encoded alpha-galactosidase (gene rafA P16551)[9] contains a region of about 50 amino acids which is similar to a domain of the eukaryotic alpha-galactosidases. Alpha-N-acetylgalactosaminidase (EC 3.2.1.49)[10] catalyzes the hydrolysis of terminal non-reducing N-acetyl-D-galactosamine residues in N-acetyl-alpha-D- galactosaminides. In man, the deficiency of this enzyme is the cause of Schindler and Kanzaki diseases. The sequence of this enzyme is highly related to that of the eukaryotic alpha-galactosidases.
External linksedit
GH27 in CAZypedia
Referencesedit
^Henrissat B, Callebaut I, Mornon JP, Fabrega S, Lehn P, Davies G (1995). "Conserved catalytic machinery and the prediction of a common fold for several families of glycosyl hydrolases". Proc. Natl. Acad. Sci. U.S.A. 92 (15): 7090–7094. Bibcode:1995PNAS...92.7090H. doi:10.1073/pnas.92.15.7090. PMC41477. PMID 7624375.
^Henrissat B, Davies G (1995). "Structures and mechanisms of glycosyl hydrolases". Structure. 3 (9): 853–859. doi:10.1016/S0969-2126(01)00220-9. PMID 8535779.
^. Archived from the original on 2011-05-25. Retrieved 2011-10-04.
^Lombard, Vincent; Golaconda Ramulu, Hemalatha; Drula, Elodie; Coutinho, Pedro M.; Henrissat, Bernard (2014-01-01). "The carbohydrate-active enzymes database (CAZy) in 2013". Nucleic Acids Research. 42 (D1): D490–D495. doi:10.1093/nar/gkt1178. ISSN 0305-1048. PMC3965031. PMID 24270786.
^"Glycoside Hydrolase Family 27". CAZypedia.org. Retrieved 2018-03-06.
^CAZypedia Consortium (2018-12-01). "Ten years of CAZypedia: a living encyclopedia of carbohydrate-active enzymes" (PDF). Glycobiology. 28 (1): 3–8. doi:10.1093/glycob/cwx089. ISSN 1460-2423. PMID 29040563.
^Dey PM, Pridham JB (1972). "Biochemistry of α‐Galactosidases". Advances in Enzymology and Related Areas of Molecular Biology. pp. 91–120. doi:10.1002/9780470122815.ch3. ISBN9780470122815. PMID 4561015. {{cite book}}: |journal= ignored (help)
^Aslanidis C, Schmid K, Schmitt R (1989). "Nucleotide sequences and operon structure of plasmid-borne genes mediating uptake and utilization of raffinose in Escherichia coli". J. Bacteriol. 171 (12): 6753–6763. doi:10.1128/jb.171.12.6753-6763.1989. PMC210573. PMID 2556373.
^Wang AM, Bishop DF, Desnick RJ (1990). "Human alpha-N-acetylgalactosaminidase-molecular cloning, nucleotide sequence, and expression of a full-length cDNA. Homology with human alpha-galactosidase A suggests evolution from a common ancestral gene". J. Biol. Chem. 265 (35): 21859–21866. doi:10.1016/S0021-9258(18)45818-8. PMID 2174888.
This article incorporates text from the public domain Pfam and InterPro: IPR000111
glycoside, hydrolase, family, molecular, biology, glycoside, hydrolase, family, family, glycoside, hydrolases, melibiasecrystal, structure, rice, alpha, galactosidaseidentifierssymbolmelibiasepfampf02065pfam, clancl0058interproipr000111scop21ktc, scope, supfam. In molecular biology glycoside hydrolase family 27 is a family of glycoside hydrolases Melibiasecrystal structure of rice alpha galactosidaseIdentifiersSymbolMelibiasePfamPF02065Pfam clanCL0058InterProIPR000111SCOP21ktc SCOPe SUPFAMCAZyGH27Available protein structures Pfam structures ECOD PDBRCSB PDB PDBe PDBjPDBsumstructure summaryGlycoside hydrolases EC 3 2 1 are a widespread group of enzymes that hydrolyse the glycosidic bond between two or more carbohydrates or between a carbohydrate and a non carbohydrate moiety A classification system for glycoside hydrolases based on sequence similarity has led to the definition of gt 100 different families 1 2 3 This classification is available on the CAZy web site 4 5 and also discussed at CAZypedia an online encyclopedia of carbohydrate active enzymes 6 7 Glycoside hydrolase family 27 together with family 31 and the family 36 alpha galactosidases form the glycosyl hydrolase clan GH D a superfamily of alpha galactosidases alpha N acetylgalactosaminidases and isomaltodextranases which are likely to share a common catalytic mechanism and structural topology Alpha galactosidase EC 3 2 1 22 melibiase 8 catalyzes the hydrolysis of melibiose into galactose and glucose In man the deficiency of this enzyme is the cause of Fabry s disease X linked sphingolipidosis Alpha galactosidase is present in a variety of organisms There is a considerable degree of similarity in the sequence of alpha galactosidase from various eukaryotic species Escherichia coli alpha galactosidase gene melA which requires NAD and magnesium as cofactors is not structurally related to the eukaryotic enzymes by contrast an Escherichia coli plasmid encoded alpha galactosidase gene rafA P16551 9 contains a region of about 50 amino acids which is similar to a domain of the eukaryotic alpha galactosidases Alpha N acetylgalactosaminidase EC 3 2 1 49 10 catalyzes the hydrolysis of terminal non reducing N acetyl D galactosamine residues in N acetyl alpha D galactosaminides In man the deficiency of this enzyme is the cause of Schindler and Kanzaki diseases The sequence of this enzyme is highly related to that of the eukaryotic alpha galactosidases External links editGH27 in CAZypediaReferences edit Henrissat B Callebaut I Mornon JP Fabrega S Lehn P Davies G 1995 Conserved catalytic machinery and the prediction of a common fold for several families of glycosyl hydrolases Proc Natl Acad Sci U S A 92 15 7090 7094 Bibcode 1995PNAS 92 7090H doi 10 1073 pnas 92 15 7090 PMC 41477 PMID 7624375 Henrissat B Davies G 1995 Structures and mechanisms of glycosyl hydrolases Structure 3 9 853 859 doi 10 1016 S0969 2126 01 00220 9 PMID 8535779 Bairoch A Classification of glycosyl hydrolase families and index of glycosyl hydrolase entries in SWISS PROT 1999 Archived from the original on 2011 05 25 Retrieved 2011 10 04 Home CAZy org Retrieved 2018 03 06 Lombard Vincent Golaconda Ramulu Hemalatha Drula Elodie Coutinho Pedro M Henrissat Bernard 2014 01 01 The carbohydrate active enzymes database CAZy in 2013 Nucleic Acids Research 42 D1 D490 D495 doi 10 1093 nar gkt1178 ISSN 0305 1048 PMC 3965031 PMID 24270786 Glycoside Hydrolase Family 27 CAZypedia org Retrieved 2018 03 06 CAZypedia Consortium 2018 12 01 Ten years of CAZypedia a living encyclopedia of carbohydrate active enzymes PDF Glycobiology 28 1 3 8 doi 10 1093 glycob cwx089 ISSN 1460 2423 PMID 29040563 Dey PM Pridham JB 1972 Biochemistry of a Galactosidases Advances in Enzymology and Related Areas of Molecular Biology pp 91 120 doi 10 1002 9780470122815 ch3 ISBN 9780470122815 PMID 4561015 a href Template Cite book html title Template Cite book cite book a journal ignored help Aslanidis C Schmid K Schmitt R 1989 Nucleotide sequences and operon structure of plasmid borne genes mediating uptake and utilization of raffinose in Escherichia coli J Bacteriol 171 12 6753 6763 doi 10 1128 jb 171 12 6753 6763 1989 PMC 210573 PMID 2556373 Wang AM Bishop DF Desnick RJ 1990 Human alpha N acetylgalactosaminidase molecular cloning nucleotide sequence and expression of a full length cDNA Homology with human alpha galactosidase A suggests evolution from a common ancestral gene J Biol Chem 265 35 21859 21866 doi 10 1016 S0021 9258 18 45818 8 PMID 2174888 This article incorporates text from the public domain Pfam and InterPro IPR000111 Portal nbsp Biology Retrieved from https en wikipedia org w index php title Glycoside hydrolase family 27 amp oldid 1172337120, wikipedia, wiki, book, books, library,
