EzCatDB: M00134

DB codeM00134
RLCP classification1.32.5000.73
CATH domainDomain 13.20.20.80Catalytic domain
Domain 23.10.50.10
Domain 32.60.40.30
Domain 42.60.40.30
Domain 52.10.10.20
E.C.3.2.1.14
CSA1itx

CATH domainRelated DB codes (homologues)
2.10.10.20D00501
2.60.40.30M00124,M00129,M00136,M00149,M00192
3.10.50.10T00063
3.20.20.80S00202,S00210,S00748,S00906,S00907,S00911,S00912,S00915,M00160,D00479,S00204,S00205,S00206,S00207,S00203,S00208,S00209,S00211,S00213,S00214,M00113,T00307,D00165,D00166,D00169,D00176,D00501,D00502,D00503,D00844,D00861,D00864,M00026,M00112,M00193,M00346,T00057,T00062,T00063,T00066,T00067

Enzyme Name
Swiss-protKEGG

P20533
Protein nameChitinase A1chitinase
chitodextrinase
1,4-beta-poly-N-acetylglucosaminidase
poly-beta-glucosaminidase
beta-1,4-poly-N-acetyl glucosamidinase
poly[1,4-(N-acetyl-beta-D-glucosaminide)] glycanohydrolase
SynonymsEC 3.2.1.14

KEGG pathways
MAP codePathways
MAP00530Aminosugars metabolism

Swiss-prot:Accession NumberP20533
Entry nameCHIA1_BACCI
ActivityRandom hydrolysis of N-acetyl-beta-D- glucosaminide (1->4)-beta-linkages in chitin and chitodextrins.
Subunit
Subcellular location
Cofactor


SubstratesProducts
KEGG-idC00461C00851C00001C03518C00140
CompoundChitinChitodextrinH2ON-Acetyl-D-glucosaminideN-Acetyl-D-glucosamine
Typeamide group,polysaccharideamide group,polysaccharideH2Oamide group,carbohydrateamide group,carbohydrate
1itxA01UnboundUnbound
UnboundUnbound
1itxA02UnboundUnbound
UnboundUnbound
1k85AUnboundUnbound
UnboundUnbound
1ed7AUnboundUnbound
UnboundUnbound

Active-site residues
resource
(T00063)
pdbCatalytic residues
1itxA01ASP 202;GLU 204;TYR 279;ASP 280
1itxA02
1k85A
1ed7A

References for Catalytic Mechanism
ReferencesSectionsNo. of steps in catalysis
[8]p.853-854

references
[1]
CommentsMUTAGENESIS.
Medline ID93366760
PubMed ID8103047
JournalJ Biol Chem
Year1993
Volume268
Pages18567-72
AuthorsWatanabe T, Kobori K, Miyashita K, Fujii T, Sakai H, Uchida M, Tanaka H
TitleIdentification of glutamic acid 204 and aspartic acid 200 in chitinase A1 of Bacillus circulans WL-12 as essential residues for chitinase activity.
Related Swiss-protP20533
[2]
PubMed ID7765724
JournalBiosci Biotechnol Biochem
Year1994
Volume58
Pages2283-5
AuthorsWatanabe T, Uchida M, Kobori K, Tanaka H
TitleSite-directed mutagenesis of the Asp-197 and Asp-202 residues in chitinase A1 of Bacillus circulans WL-12.
[3]
PubMed ID8168626
JournalFEBS Lett
Year1994
Volume343
Pages177-80
AuthorsArmand S, Tomita H, Heyraud A, Gey C, Watanabe T, Henrissat B
TitleStereochemical course of the hydrolysis reaction catalyzed by chitinases A1 and D from Bacillus circulans WL-12.
[4]
PubMed ID8045877
JournalJ Bacteriol
Year1994
Volume176
Pages4465-72
AuthorsWatanabe T, Ito Y, Yamada T, Hashimoto M, Sekine S, Tanaka H
TitleThe roles of the C-terminal domain and type III domains of chitinase A1 from Bacillus circulans WL-12 in chitin degradation.
[5]
PubMed ID10913612
JournalFEBS Lett
Year2000
Volume476
Pages194-7
AuthorsHonda Y, Tanimori S, Kirihata M, Kaneko S, Tokuyasu K, Hashimoto M, Watanabe T, Fukamizo T
TitleKinetic analysis of the reaction catalyzed by chitinase A1 from Bacillus circulans WL-12 toward the novel substrates, partially N-deacetylated 4-methylumbelliferyl chitobiosides.
[6]
CommentsX-ray crystallography
PubMed ID10788483
JournalJ Biol Chem
Year2000
Volume275
Pages13654-61
AuthorsIkegami T, Okada T, Hashimoto M, Seino S, Watanabe T, Shirakawa M
TitleSolution structure of the chitin-binding domain of Bacillus circulans WL-12 chitinase A1.
Related PDB1ed7
[7]
PubMed ID11297738
JournalFEBS Lett
Year2001
Volume494
Pages74-8
AuthorsWatanabe T, Ishibashi A, Ariga Y, Hashimoto M, Nikaidou N, Sugiyama J, Matsumoto T, Nonaka T
TitleTrp122 and Trp134 on the surface of the catalytic domain are essential for crystalline chitin hydrolysis by Bacillus circulans chitinase A1.
Related PDB1itx
[8]
PubMed ID11742103
JournalProtein Eng
Year2001
Volume14
Pages845-55
AuthorsNagano N, Porter CT, Thornton JM
TitleThe (betaalpha)(8) glycosidases: sequence and structure analyses suggest distant evolutionary relationships.
[9]
PubMed ID11821923
JournalCurr Microbiol
Year2002
Volume44
Pages167-72
AuthorsWiwat C, Thepouyporn A, Siwayaprahm P, Bhumiratana A
TitleCloning, sequencing, and expression of a chitinase-encoding gene from Bacillus circulans No. 4.1.
[10]
PubMed ID11801254
JournalFEBS Lett
Year2002
Volume510
Pages201-5
AuthorsImai T, Watanabe T, Yui T, Sugiyama J
TitleDirectional degradation of beta-chitin by chitinase A1 revealed by a novel reducing end labelling technique.
[11]
PubMed ID11926993
JournalJ Biochem (Tokyo)
Year2002
Volume131
Pages557-64
AuthorsSasaki C, Yokoyama A, Itoh Y, Hashimoto M, Watanabe T, Fukamizo T
TitleComparative study of the reaction mechanism of family 18 chitinases from plants and microbes.
[12]
PubMed ID11600504
JournalJ Biol Chem
Year2002
Volume277
Pages1388-97
AuthorsJee JG, Ikegami T, Hashimoto M, Kawabata T, Ikeguchi M, Watanabe T, Shirakawa M
TitleSolution structure of the fibronectin type III domain from Bacillus circulans WL-12 chitinase A1.
Related PDB1k85

comments
This enzyme belongs to chitinase class-II (glycosyl hydrolase family-18).
This enzyme is composed of N-terminal catalytic domain, two fibronectin type-III domains and C-terminal chitin-binding domain. The PDB structures, 1itx, 1k85, and 1ed7 correspond to the catalytic domain, the second fibronectin type-III domain, and chitin-binding domain, respectively.
According to the literature [8], in glycosylase family-18, there are two types of enzymes with different catalytic mechanisms, chitinase (PDB; 1ctn) and hevamine (2hvm). The former enzyme uses two acidic residue as catalytic residues, whilst the latter has only one catalytic residue, using a moiety of its substrate as a catalytic group during the catalysis. The catalytic domain of this enzyme is similar to chitinase, rather than hevamine, since it has two acidic residues, which can be superimposed to those of chitinase (T00063).
However, more recent study proposed that Tyr279, which is conserved throughout the family-18, instead of Asp280, can be involved in catalysis (T00063).
Although this enzyme has a different domain composition from chitinase, these enzymes must have the same catalytic mechanism.

createdupdated
2004-03-192010-12-03
Copyright: Nozomi Nagano, JST & CBRC-AIST
Funded by PRESTO/Japan Science and Technology Corporation (JST) (December 2001 - November 2004)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2005 - March 2006)
Funded by Grant-in-Aid for Scientific Research (B)/Japan Society for the Promotion of Science (JSPS) (April 2005 - March 2008)
Funded by BIRD/Japan Science and Technology Corporation (JST) (September 2005 - September 2010)
Funded by BIRD/Japan Science and Technology Corporation (JST) (October 2007 - September 2010)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2011 - March 2012)

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