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InterPro: IPR017736 Glycoside hydrolase, family 1, beta-glucosidase

Protein matchesHelp
UniProtKB
Matches:
331 proteins
AccessionHelp IPR017736 Glyco_hydro_1_beta-glucosidase
TypeHelp Family
SignaturesHelp
InterPro RelationshipsHelp
Parent IPR001360 Glycoside hydrolase, family 1
Contains IPR013781 Glycoside hydrolase, subgroup, catalytic core
IPR018120 Glycoside hydrolase, family 1, active site
GO Term annotationHelp
Process GO:0030245 cellulose catabolic process
Function GO:0008422 beta-glucosidase activity
InterPro annotation
BioMart Logo Entry Details in BioMart
AbstractHelp

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.

Structural linksHelp
SCOP: c.1.8.4
CATH: 3.20.20.80
Database linksHelp
Enzyme: EC:3.2.1.21

Taxonomic coverageHelp

Overlapping InterPro entriesHelp
IPR017736 Numbers of overlapping proteins Average numbers of overlapping amino acids

Example proteinsHelp
P22073 Beta-glucosidase A

More proteins


Example Proteins Key


InterPro entry accession number/name and structure databases Colour code
IPR013781 Glycoside hydrolase, subgroup, catalytic core
IPR017736 Glycoside hydrolase, family 1, beta-glucosidase
IPR018120 Glycoside hydrolase, family 1, active site
IPR001360 Glycoside hydrolase, family 1
IPR017853 Glycoside hydrolase, catalytic core
PDB Chain
ModBase
SCOP Domain
CATH Domain

PublicationsHelp
1. 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
2. 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
3. Bairoch A.
Classification of glycosyl hydrolase families and index of glycosyl hydrolase entries in SWISS-PROT.
1999
4. Henrissat B, Coutinho PM.
Carbohydrate-Active Enzymes server.
1999
5. 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
6. 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

Additional ReadingHelp
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
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
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
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
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