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InterPro: IPR016288 1, 4-beta cellobiohydrolase

Protein matchesHelp
UniProtKB
Matches:
254 proteins
AccessionHelp IPR016288 Beta_cellobiohydrolase
TypeHelp Family
SignaturesHelp
InterPro RelationshipsHelp
Contains IPR001524 Glycoside hydrolase, family 6, conserved site
GO Term annotationHelp
Process GO:0030245 cellulose catabolic process
Function GO:0004553 hydrolase activity, hydrolyzing O-glycosyl compounds
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.

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.

Structural linksHelp
SCOP: c.6.1.1
CATH: 3.20.20.40
Database linksHelp
Enzyme: EC:3.2.1

Taxonomic coverageHelp

Overlapping InterPro entriesHelp
IPR016288 Numbers of overlapping proteins Average numbers of overlapping amino acids

Example proteinsHelp
P07987 Exoglucanase 2

P26222 Endoglucanase E-2

More proteins


Example Proteins Key


InterPro entry accession number/name and structure databases Colour code
IPR001524 Glycoside hydrolase, family 6, conserved site
IPR012291 Cellulose-binding family II/chitobiase, carbohydrate-binding domain
IPR017909 Twin arginine translocation signal, Tat
IPR016288 1, 4-beta cellobiohydrolase
IPR008965 Carbohydrate-binding
IPR000254 Cellulose-binding domain, fungal
IPR001919 Cellulose-binding domain, family II, bacterial type
IPR018366 Carbohydrate-binding type-2, conserved site
PDB Chain
ModBase
CATH Domain
SWISS-MODEL
SCOP 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

Additional ReadingHelp
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
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
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
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
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
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
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