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InterPro: IPR013319 Glycoside hydrolase, family 11/12, catalytic domain
Protein matches
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UniProtKB Matches: 725 proteins |
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Accession
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IPR013319 Glyco_hydro_11/12_cat |
Type
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Domain |
Signatures
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InterPro Relationships
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Parent
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IPR008985 Concanavalin A-like lectin/glucanase
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Found in
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IPR001137 Glycoside hydrolase, family 11
IPR002594 Glycoside hydrolase, family 12
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Contains
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IPR018208 Glycoside hydrolase, family 11, active site
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GO Term annotation
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Function
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GO:0004553 hydrolase activity, hydrolyzing O-glycosyl compounds
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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.
Glycoside hydrolase family 11 GH11 comprises enzymes with only one known activity, xylanase (EC:3.2.1.8), while family 12 GH12 comprises enzymes with two known activities, endoglucanase (EC:3.2.1.4) and xyloglucan hydrolase. This entry represents the catalytic core of family 11 and 12 glycoside hydrolases, which assumes a beta-sandwich structure of complex topology, consisting of 12-14 beta-strands in two sheets.
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Structural links
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Database links
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Additional Reading
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Vandermarliere E, Bourgois TM, Rombouts S, Van Campenhout S, Volckaert G, Strelkov SV, Delcour JA, Rabijns A, Courtin CM.
Crystallographic analysis shows substrate binding at the -3 to +1 active-site subsites and at the surface of glycoside hydrolase family 11 endo-1,4-beta-xylanases.
Biochem. J. 410 2008 71-9
[PubMed: 17983355]
http://dx.doi.org/10.1042/BJ20071128
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Vardakou M, Dumon C, Murray JW, Christakopoulos P, Weiner DP, Juge N, Lewis RJ, Gilbert HJ, Flint JE.
Understanding the structural basis for substrate and inhibitor recognition in eukaryotic GH11 xylanases.
J. Mol. Biol. 375 2008 1293-305
[PubMed: 18078955]
http://dx.doi.org/10.1016/j.jmb.2007.11.007
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Crennell SJ, Cook D, Minns A, Svergun D, Andersen RL, Nordberg Karlsson E.
Dimerisation and an increase in active site aromatic groups as adaptations to high temperatures: X-ray solution scattering and substrate-bound crystal structures of Rhodothermus marinus endoglucanase Cel12A.
J. Mol. Biol. 356 2006 57-71
[PubMed: 16343530]
http://dx.doi.org/10.1016/j.jmb.2005.11.004
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Jiang L, Althoff EA, Clemente FR, Doyle L, Rothlisberger D, Zanghellini A, Gallaher JL, Betker JL, Tanaka F, Barbas CF 3rd, Hilvert D, Houk KN, Stoddard BL, Baker D.
De novo computational design of retro-aldol enzymes.
Science 319 2008 1387-91
[PubMed: 18323453]
http://dx.doi.org/10.1126/science.1152692
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Miyatake H, Hasegawa T, Yamano A.
New methods to prepare iodinated derivatives by vaporizing iodine labelling (VIL) and hydrogen peroxide VIL (HYPER-VIL).
Acta Crystallogr. D Biol. Crystallogr. 62 2006 280-9
[PubMed: 16510975]
http://dx.doi.org/10.1107/S0907444905041909
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InterPro 23.1
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