Glycoside hydrolase family 27 explained
Symbol: | Melibiase |
Melibiase |
Pfam: | PF02065 |
Pfam Clan: | CL0058 |
Interpro: | IPR000111 |
Scop: | 1ktc |
Cazy: | GH27 |
In molecular biology, glycoside hydrolase family 27 is a family of glycoside hydrolases.
Glycoside hydrolases 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]
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 (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)[9] contains a region of about 50 amino acids which is similar to a domain of the eukaryotic alpha-galactosidases. Alpha-N-acetylgalactosaminidase [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
Notes and References
- Henrissat B, Callebaut I, Mornon JP, Fabrega S, Lehn P, Davies G . 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 . 1995 . 7624375 . 10.1073/pnas.92.15.7090 . 41477. 1995PNAS...92.7090H . free .
- Henrissat B, Davies G . Structures and mechanisms of glycosyl hydrolases . Structure . 3 . 9 . 853–859 . 1995 . 8535779 . 10.1016/S0969-2126(01)00220-9. free .
- Web site: Bairoch, A. "Classification of glycosyl hydrolase families and index of glycosyl hydrolase entries in SWISS-PROT". 1999. . 2011-10-04 . 2011-05-25 . https://web.archive.org/web/20110525140109/http://www.expasy.ch/cgi-bin/lists?glycosid.txt . dead .
- Web site: Home. CAZy.org. en. 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. en. 42. D1. D490–D495. 10.1093/nar/gkt1178. 24270786. 0305-1048. 3965031.
- Web site: Glycoside Hydrolase Family 27. CAZypedia.org. en. 2018-03-06.
- CAZypedia Consortium. 2018-12-01. Ten years of CAZypedia: a living encyclopedia of carbohydrate-active enzymes. Glycobiology. 28. 1. 3–8. 10.1093/glycob/cwx089. 1460-2423. 29040563. free.
- Book: Dey PM, Pridham JB . Advances in Enzymology and Related Areas of Molecular Biology . Biochemistry of α-Galactosidases . Adv. Enzymol. Relat. Areas Mol. Biol. . 36 . 91–120 . 1972 . 4561015. 10.1002/9780470122815.ch3 . Advances in Enzymology - and Related Areas of Molecular Biology . 9780470122815 .
- Aslanidis C, Schmid K, Schmitt R . Nucleotide sequences and operon structure of plasmid-borne genes mediating uptake and utilization of raffinose in Escherichia coli . J. Bacteriol. . 171 . 12 . 6753–6763 . 1989 . 2556373 . 210573 . 10.1128/jb.171.12.6753-6763.1989.
- Wang AM, Bishop DF, Desnick RJ . 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 . 1990 . 10.1016/S0021-9258(18)45818-8 . 2174888. free .