Glycoside hydrolase family 27

Melibiase
crystal structure of rice alpha-galactosidase
Identifiers
Symbol	Melibiase
Pfam	PF02065
Pfam clan	CL0058
InterPro	IPR000111
SCOP2	1ktc / SCOPe / SUPFAM
CAZy	GH27
Available protein structures: Pfam   structures / ECOD   PDB RCSB PDB; PDBe; PDBj PDBsum structure summary

In molecular biology, glycoside hydrolase family 27 is a family of glycoside hydrolases.

Glycoside 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 >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

• GH27 in CAZypedia

References

1. 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.
2. 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.
3. "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.
4. "Home". CAZy.org. Retrieved 2018-03-06.
5. 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.
6. "Glycoside Hydrolase Family 27". CAZypedia.org. Retrieved 2018-03-06.
7. 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.
8. 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. ISBN   9780470122815. PMID   4561015.{{cite book}}: |journal= ignored (help)
9. 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.
10. 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