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InterPro: IPR003385 Glycoside hydrolase, family 77
Protein matches
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UniProtKB Matches: 1114 proteins |
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Accession
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IPR003385 Glyco_hydro_77 |
Type
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Family |
Signatures
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InterPro Relationships
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Contains
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IPR013781 Glycoside hydrolase, subgroup, catalytic core
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GO Term annotation
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Process
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GO:0005975 carbohydrate metabolic process
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Function
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GO:0004134 4-alpha-glucanotransferase activity
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InterPro annotation
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Entry Details in BioMart
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Abstract
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O-Glycosyl 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 glycosyl hydrolases, based on sequence similarity, has led to the definition of 85 different families [1, 2, 3]. This classification is available on the CAZy (CArbohydrate-Active EnZymes) web site [4]. Because the fold of proteins is better conserved than their sequences, some of the families can be grouped in clans.
The enzymes in this entry (EC:2.4.1.25) belong to the glycoside hydrolase family 77 GH77, and transfer a segment of a (1,4)-alpha-D-glucan to a new 4-position in an acceptor, which may be
glucose or (1,4)-alpha-D-glucan [5]. They belong to the disproportionating family of enzymes.
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Structural links
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Database links
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Pfam Clan: CL0058.12
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Publications
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1.
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Henrissat B, Callebaut I, Fabrega S, Lehn P, Mornon JP, 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 7090-4 1995
[PubMed: 7624375]
http://www.pubmedcentral.nih.gov/picrender.fcgi?tool=EBI&pubmedid=7624375&action=stream&blobtype=pdf
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2.
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Davies G, Henrissat B.
Structures and mechanisms of glycosyl hydrolases.
Structure 3 853-9 1995
[PubMed: 8535779]
http://dx.doi.org/10.1016/S0969-2126(01)00220-9
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3.
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Bairoch A.
Classification of glycosyl hydrolase families and index of glycosyl hydrolase entries in SWISS-PROT.
1999
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4.
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Henrissat B, Coutinho PM.
Carbohydrate-Active Enzymes server.
1999
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5.
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Takaha T, Yanase M, Okada S, Smith SM.
Disproportionating enzyme (4-alpha-glucanotransferase; EC 2.4.1.25) of potato. Purification, molecular cloning, and potential role in starch metabolism.
J. Biol. Chem. 268 1391-6 1993
[PubMed: 7678257]
http://intl.jbc.org/cgi/reprint/268/2/1391.pdf
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Additional Reading
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Przylas I, Terada Y, Fujii K, Takaha T, Saenger W, Strater N.
X-ray structure of acarbose bound to amylomaltase from Thermus aquaticus. Implications for the synthesis of large cyclic glucans.
Eur. J. Biochem. 267 2000 6903-13
[PubMed: 11082203]
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Przylas I, Tomoo K, Terada Y, Takaha T, Fujii K, Saenger W, Strater N.
Crystal structure of amylomaltase from thermus aquaticus, a glycosyltransferase catalysing the production of large cyclic glucans.
J. Mol. Biol. 296 2000 873-86
[PubMed: 10677288]
http://dx.doi.org/10.1006/jmbi.1999.3503
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Barends TR, Bultema JB, Kaper T, van der Maarel MJ, Dijkhuizen L, Dijkstra BW.
Three-way stabilization of the covalent intermediate in amylomaltase, an alpha-amylase-like transglycosylase.
J. Biol. Chem. 282 2007 17242-9
[PubMed: 17420245]
http://dx.doi.org/10.1074/jbc.M701444200
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InterPro 23.1
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