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InterPro: IPR016288 1, 4-beta cellobiohydrolase
Protein matches
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UniProtKB Matches: 254 proteins |
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Accession
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IPR016288 Beta_cellobiohydrolase |
Type
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Family |
Signatures
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InterPro Relationships
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Contains
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IPR001524 Glycoside hydrolase, family 6, conserved 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: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.
The 1,4-beta cellobiohydrolase family plays a central role in the recycling of plant biomass. The biological conversion of cellulose to glucose generally requires three types of hydrolytic enzymes: Endoglucanases, which cut internal beta-1,4-glucosidic bonds; Exocellobiohydrolases that cut the dissaccharide cellobiose from the non-reducing end of the cellulose polymer chain; and Beta-1,4-glucosidases, which hydrolyze the cellobiose and other short cello-oligosaccharides to glucose.
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Structural links
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Database links
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Additional Reading
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Varrot A, Macdonald J, Stick RV, Pell G, Gilbert HJ, Davies GJ.
Distortion of a cellobio-derived isofagomine highlights the potential conformational itinerary of inverting beta-glucosidases.
Chem. Commun. (Camb.) 2003 946-7
[PubMed: 12744312]
http://dx.doi.org/10.1039/b301592k
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Larsson AM, Bergfors T, Dultz E, Irwin DC, Roos A, Driguez H, Wilson DB, Jones TA.
Crystal structure of Thermobifida fusca endoglucanase Cel6A in complex with substrate and inhibitor: the role of tyrosine Y73 in substrate ring distortion.
Biochemistry 44 2005 12915-22
[PubMed: 16185060]
http://dx.doi.org/10.1021/bi0506730
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Varrot A, Leydier S, Pell G, Macdonald JM, Stick RV, Henrissat B, Gilbert HJ, Davies GJ.
Mycobacterium tuberculosis strains possess functional cellulases.
J. Biol. Chem. 280 2005 20181-4
[PubMed: 15824123]
http://dx.doi.org/10.1074/jbc.C500142200
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Varrot A, Frandsen TP, Driguez H, Davies GJ.
Structure of the Humicola insolens cellobiohydrolase Cel6A D416A mutant in complex with a non-hydrolysable substrate analogue, methyl cellobiosyl-4-thio-beta-cellobioside, at 1.9 A.
Acta Crystallogr. D Biol. Crystallogr. 58 2002 2201-4
[PubMed: 12454501]
http://dx.doi.org/10.1107/S0907444902017006
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Koivula A, Reinikainen T, Ruohonen L, Valkeajarvi A, Claeyssens M, Teleman O, Kleywegt GJ, Szardenings M, Rouvinen J, Jones TA, Teeri TT.
The active site of Trichoderma reesei cellobiohydrolase II: the role of tyrosine 169.
Protein Eng. 9 1996 691-9
[PubMed: 8875646]
http://dx.doi.org/10.1093/protein/9.8.691
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Varrot A, Frandsen TP, von Ossowski I, Boyer V, Cottaz S, Driguez H, Schulein M, Davies GJ.
Structural basis for ligand binding and processivity in cellobiohydrolase Cel6A from Humicola insolens.
Structure 11 2003 855-64
[PubMed: 12842048]
http://dx.doi.org/10.1016/S0969-2126(03)00124-2
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Rouvinen J, Bergfors T, Teeri T, Knowles JK, Jones TA.
Three-dimensional structure of cellobiohydrolase II from Trichoderma reesei.
Science 249 1990 380-6
[PubMed: 2377893]
http://www.sciencemag.org/cgi/content/abstract/249/4967/380
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InterPro 23.1
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