 |
InterPro: IPR000805 Glycoside hydrolase, family 26
Protein matches
|
UniProtKB Matches: 227 proteins |
|
Accession
|
IPR000805 Glyco_hydro_26 |
Type
|
Family |
Signatures
|
|
InterPro Relationships
|
|
Children
|
IPR016714 Mannan endo-1,4-beta-mannosidase
|
GO Term annotation
|
|
Process
|
GO:0006080 substituted mannan metabolic process
|
|
Function
|
GO:0016985 mannan endo-1,4-beta-mannosidase activity
|
|
InterPro annotation
|
|
Entry Details in BioMart
|
Abstract
|
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 26 GH26 comprises enzymes with only one known activity; mannanase (EC:3.2.1.78).
Family 26 encompasses mainly mannan endo-1,4-beta-mannosidases.
Mannan endo-1,4-beta-mannosidase hydrolyses mannan and galactomannan, but
displays little activity towards other plant cell wall polysaccharides [5]. The enzyme randomly hydrolyses 1,4-beta-D-linkages in mannans, galacto-mannans, glucomannans and galactoglucomannans.
|
Structural links
|
|
Database links
|
Pfam Clan: CL0058.12
|
Publications
|
|
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.
|
Braithwaite KL, Black GW, Hazlewood GP, Ali BR, Gilbert HJ.
A non-modular endo-beta-1,4-mannanase from Pseudomonas fluorescens subspecies cellulosa.
Biochem. J. 305 ( Pt 3) 1005-10 1995
[PubMed: 7848261]
http://www.pubmedcentral.nih.gov/picrender.fcgi?tool=EBI&pubmedid=7848261&action=stream&blobtype=pdf
|
Additional Reading
|
|
Ducros VM, Zechel DL, Murshudov GN, Gilbert HJ, Szabo L, Stoll D, Withers SG, Davies GJ.
Substrate distortion by a beta-mannanase: snapshots of the Michaelis and covalent-intermediate complexes suggest a B(2,5) conformation for the transition state.
Angew. Chem. Int. Ed. Engl. 41 2002 2824-7
[PubMed: 12203498]
http://dx.doi.org/10.1002/1521-3773(20020802)41:15<2824::AID-ANIE2824>3.0.CO;2-G
|
|
Money VA, Smith NL, Scaffidi A, Stick RV, Gilbert HJ, Davies GJ.
Substrate distortion by a lichenase highlights the different conformational itineraries harnessed by related glycoside hydrolases.
Angew. Chem. Int. Ed. Engl. 45 2006 5136-40
[PubMed: 16823793]
http://dx.doi.org/10.1002/anie.200600802
|
|
Jahn M, Stoll D, Warren RA, Szabo L, Singh P, Gilbert HJ, Ducros VM, Davies GJ, Withers SG.
Expansion of the glycosynthase repertoire to produce defined manno-oligosaccharides.
Chem. Commun. (Camb.) 2003 1327-9
[PubMed: 12841226]
http://dx.doi.org/10.1039/b302380j
|
|
Taylor EJ, Goyal A, Guerreiro CI, Prates JA, Money VA, Ferry N, Morland C, Planas A, Macdonald JA, Stick RV, Gilbert HJ, Fontes CM, Davies GJ.
How family 26 glycoside hydrolases orchestrate catalysis on different polysaccharides: structure and activity of a Clostridium thermocellum lichenase, CtLic26A.
J. Biol. Chem. 280 2005 32761-7
[PubMed: 15987675]
http://dx.doi.org/10.1074/jbc.M506580200
|
|
Le Nours J, Anderson L, Stoll D, Stalbrand H, Lo Leggio L.
The structure and characterization of a modular endo-beta-1,4-mannanase from Cellulomonas fimi.
Biochemistry 44 2005 12700-8
[PubMed: 16171384]
http://dx.doi.org/10.1021/bi050779v
|
|
|
InterPro 23.1
|