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InterPro: IPR017736 Glycoside hydrolase, family 1, beta-glucosidase
Protein matches
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UniProtKB Matches: 331 proteins |
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Accession
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IPR017736 Glyco_hydro_1_beta-glucosidase |
Type
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Family |
Signatures
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InterPro Relationships
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Parent
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IPR001360 Glycoside hydrolase, family 1
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Contains
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IPR013781 Glycoside hydrolase, subgroup, catalytic core
IPR018120 Glycoside hydrolase, family 1, active site
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GO Term annotation
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Process
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GO:0030245 cellulose catabolic process
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Function
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GO:0008422 beta-glucosidase 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.
Glycoside hydrolase family 1 GH1 comprises enzymes with a number of known activities; beta-glucosidase (EC:3.2.1.21); beta-galactosidase (EC:3.2.1.23); 6-phospho-beta-galactosidase (EC:3.2.1.85); 6-phospho-beta-glucosidase (EC:3.2.1.86); lactase-phlorizin hydrolase (EC:3.2.1.62), (EC:3.2.1.108); beta-mannosidase (EC:3.2.1.25); myrosinase (EC:3.2.1.147).
This enzyme represents beta-glucosidase, which catalyses the hydrolysis of terminal, non-reducing beta-D-glucose residues with release of beta-D-glucose [5, 6]. It has a wide substrate specificity for beta-D-glucosides.
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Structural links
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Database links
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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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Sanz-Aparicio J, Hermoso JA, Martinez-Ripoll M, Lequerica JL, Polaina J.
Crystal structure of beta-glucosidase A from Bacillus polymyxa: insights into the catalytic activity in family 1 glycosyl hydrolases.
J. Mol. Biol. 275 491-502 1998
[PubMed: 9466926]
http://dx.doi.org/10.1006/jmbi.1997.1467
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6.
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Yernool DA, McCarthy JK, Eveleigh DE, Bok JD.
Cloning and characterization of the glucooligosaccharide catabolic pathway beta-glucan glucohydrolase and cellobiose phosphorylase in the marine hyperthermophile Thermotoga neapolitana.
J. Bacteriol. 182 5172-9 2000
[PubMed: 10960102]
http://dx.doi.org/10.1128/JB.182.18.5172-5179.2000
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Additional Reading
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Gloster TM, Madsen R, Davies GJ.
Structural basis for cyclophellitol inhibition of a beta-glucosidase.
Org. Biomol. Chem. 5 2007 444-6
[PubMed: 17252125]
http://dx.doi.org/10.1039/b616590g
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Aguilar M, Gloster TM, Garcia-Moreno MI, Ortiz Mellet C, Davies GJ, Llebaria A, Casas J, Egido-Gabas M, Garcia Fernandez JM.
Molecular basis for beta-glucosidase inhibition by ring-modified calystegine analogues.
Chembiochem 9 2008 2612-8
[PubMed: 18833549]
http://dx.doi.org/10.1002/cbic.200800451
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Isorna P, Polaina J, Latorre-Garcia L, Canada FJ, Gonzalez B, Sanz-Aparicio J.
Crystal structures of Paenibacillus polymyxa beta-glucosidase B complexes reveal the molecular basis of substrate specificity and give new insights into the catalytic machinery of family I glycosidases.
J. Mol. Biol. 371 2007 1204-18
[PubMed: 17585934]
http://dx.doi.org/10.1016/j.jmb.2007.05.082
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Gloster TM, Meloncelli P, Stick RV, Zechel D, Vasella A, Davies GJ.
Glycosidase inhibition: an assessment of the binding of 18 putative transition-state mimics.
J. Am. Chem. Soc. 129 2007 2345-54
[PubMed: 17279749]
http://dx.doi.org/10.1021/ja066961g
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Gloster TM, Madsen R, Davies GJ.
Dissection of conformationally restricted inhibitors binding to a beta-glucosidase.
Chembiochem 7 2006 738-42
[PubMed: 16628756]
http://dx.doi.org/10.1002/cbic.200600005
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InterPro 23.1
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