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InterPro: IPR000400 Glycoside hydrolase, family 46

Protein matchesHelp
UniProtKB
Matches:
59 proteins
AccessionHelp IPR000400 Glyco_hydro_46
TypeHelp Family
SignaturesHelp
GO Term annotationHelp
Process GO:0005975 carbohydrate metabolic process
Function GO:0016977 chitosanase activity
Component GO:0005576 extracellular region
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 46 GH46 comprises enzymes with only one known activity; chitosanase (EC:3.2.1.132).

Chitosanase enzymes catalyse the endohydrolysis of beta-1,4-linkages between N-acetyl-D-glucosamine and D-glucosamine residues in a partly acetylated chitosan.

Structural linksHelp
SCOP: d.2.1.7
Database linksHelp
PDBe-motif: PS60000
Enzyme: EC:3.2.1.132
CAZy: GH46
PROSITE doc: PDOC60000
PANDIT: PF01374
Blocks: IPB000400
Pfam Clan: CL0037.10

Taxonomic coverageHelp

Example proteinsHelp
P33665 Chitosanase

More proteins


Example Proteins Key


InterPro entry accession number/name and structure databases Colour code
IPR000400 Glycoside hydrolase, family 46
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

Additional ReadingHelp
Marcotte EM, Monzingo AF, Ernst SR, Brzezinski R, Robertus JD.
X-ray structure of an anti-fungal chitosanase from streptomyces N174.
Nat. Struct. Biol. 3 1996 155-62 [PubMed: 8564542]
http://dx.doi.org/10.1038/nsb0296-155
Fukamizo T, Amano S, Yamaguchi K, Yoshikawa T, Katsumi T, Saito J, Suzuki M, Miki K, Nagata Y, Ando A.
Bacillus circulans MH-K1 chitosanase: amino acid residues responsible for substrate binding.
J. Biochem. 138 2005 563-9 [PubMed: 16272568]
http://dx.doi.org/10.1093/jb/mvi156
Henrissat B, Bairoch A.
Updating the sequence-based classification of glycosyl hydrolases.
Biochem. J. 316 ( Pt 2) 1996 695-6 [PubMed: 8687420]
http://www.pubmedcentral.nih.gov/picrender.fcgi?tool=EBI&pubmedid=8687420&action=stream&blobtype=pdf
Saito JI, Nagata Y, Ando A, Kita A, Miki K.
Crystallization and preliminary X-ray crystallographic analysis of chitosanase from Bacillus circulans MH-K1.
Acta Crystallogr. D Biol. Crystallogr. 51 1995 856-7 [PubMed: 15299827]
http://dx.doi.org/10.1107/S090744499500268X
Saito J, Kita A, Higuchi Y, Nagata Y, Ando A, Miki K.
Crystal structure of chitosanase from Bacillus circulans MH-K1 at 1.6-A resolution and its substrate recognition mechanism.
J. Biol. Chem. 274 1999 30818-25 [PubMed: 10521473]
http://dx.doi.org/10.1074/jbc.274.43.30818
Tremblay H, Blanchard J, Brzezinski R.
A common molecular signature unifies the chitosanases belonging to families 46 and 80 of glycoside hydrolases.
Can. J. Microbiol. 46 2000 952-5 [PubMed: 11068683]
http://dx.doi.org/10.1139/cjm-46-10-952
Fukamizo T, Brzezinski R.
Chitosanase from Streptomyces sp. strain N174: a comparative review of its structure and function.
Biochem. Cell Biol. 75 1997 687-96 [PubMed: 9599657]
http://dx.doi.org/10.1139/bcb-75-6-687
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InterPro 23.1