EzCatDB: T00091

DB codeT00091
CATH domainDomain 11.50.10.100Catalytic domain
Domain 22.70.98.10
Domain 32.60.220.10
E.C.4.2.2.5
CSA1cb8


Enzyme Name
Swiss-protKEGG

Q59288
Protein nameChondroitinase-ACchondroitin AC lyase
chondroitinase (ambiguous)
chondroitin sulfate lyase
chondroitin AC eliminase
chondroitin AC lyase
chondroitinase AC
ChnAC
SynonymsEC 4.2.2.5
Chondroitin-AC lyase
Chondroitin sulfate AC lyase
Chondroitin-AC eliminase


Swiss-prot:Accession NumberQ59288
Entry nameCSLA_PEDHE
ActivityEliminative degradation of polysaccharides containing 1,4-beta-D-hexosaminyl and 1,3-beta-D-glucuronosyl linkages to disaccharides containing 4-deoxy-beta-D-gluc-4- enuronosyl groups.
SubunitMonomer.
Subcellular location
CofactorBinds 1 calcium ion per subunit.


CofactorsSubstratesProducts
KEGG-idC00076C00634C00635C00634C04864C00635C04865
CompoundCalciumChondroitin 4-sulfateChondroitin 6-sulfateChondroitin 4-sulfate4-Deoxy-beta-D-gluc-4-enuronosyl-(1,3)-N-acetyl-D-galactosamine 4-sulfateChondroitin 6-sulfate4-Deoxy-beta-D-gluc-4-enuronosyl-(1,3)-N-acetyl-D-galactosamine 6-sulfate
Typedivalent metal (Ca2+, Mg2+)amide group,carbohydrate,carboxyl group,polysaccharide,sulfate groupamide group,carbohydrate,carboxyl group,polysaccharide,sulfate groupamide group,carbohydrate,carboxyl group,polysaccharide,sulfate groupamide group,carboxyl group,polysaccharide,sulfate groupamide group,carbohydrate,carboxyl group,polysaccharide,sulfate groupamide group,carboxyl group,polysaccharide,sulfate group
1cb8A01UnboundUnboundUnboundUnboundUnboundUnboundUnbound
1hm2A01UnboundBound:IDR-ASG-IDR-ASG(chain D)UnboundUnboundUnboundUnboundUnbound
1hm3A01UnboundUnboundUnboundAnalogue:GCU-NAGUnboundAnalogue:GCU-NAGUnbound
1hmuA01UnboundUnboundUnboundUnboundBound:DGC-ASG(chain D)UnboundUnbound
1hmwA01UnboundUnboundAnalogue:GCD-ASG-BDP-NG6(chain D)UnboundUnboundUnboundUnbound
1cb8A02Bound:_CAUnboundUnboundUnboundUnboundUnboundUnbound
1hm2A02Bound:_CAUnboundUnboundUnboundUnboundUnboundUnbound
1hm3A02Bound:_CAUnboundUnboundUnboundUnboundUnboundUnbound
1hmuA02Bound:_CAUnboundUnboundUnboundUnboundUnboundUnbound
1hmwA02Bound:_CAUnboundUnboundUnboundUnboundUnboundUnbound
1cb8A03UnboundUnboundUnboundUnboundUnboundUnboundUnbound
1hm2A03UnboundUnboundUnboundUnboundUnboundUnboundUnbound
1hm3A03UnboundUnboundUnboundUnboundUnboundUnboundUnbound
1hmuA03UnboundUnboundUnboundUnboundUnboundUnboundUnbound
1hmwA03UnboundUnboundUnboundUnboundUnboundUnboundUnbound

Active-site residues
resource
PDB;1cb8 & Swiss-prot;Q59288 & literature [2], [4]
pdbCatalytic residuesCofactor-binding residues
1cb8A01HIS 225;TYR 234;ARG 288

1hm2A01HIS 225;TYR 234;ARG 288

1hm3A01HIS 225;TYR 234;ARG 288

1hmuA01HIS 225;TYR 234;ARG 288

1hmwA01HIS 225;TYR 234;ARG 288

1cb8A02
GLU 405;ASP 407;ASP 416;TYR 417(Calcium binding)
1hm2A02
GLU 405;ASP 407;ASP 416;TYR 417(Calcium binding)
1hm3A02
GLU 405;ASP 407;ASP 416;TYR 417(Calcium binding)
1hmuA02
GLU 405;ASP 407;ASP 416;TYR 417(Calcium binding)
1hmwA02
GLU 405;ASP 407;ASP 416;TYR 417(Calcium binding)
1cb8A03

1hm2A03

1hm3A03

1hmuA03

1hmwA03


References for Catalytic Mechanism
ReferencesSectionsNo. of steps in catalysis
[2]p.2369-2371, Fig.82
[3]Fig.1

references
[1]
CommentsX-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
Medline ID99264394
PubMed ID10329169
JournalJ Mol Biol
Year1999
Volume288
Pages635-47
AuthorsFethiere J, Eggimann B, Cygler M
TitleCrystal structure of chondroitin AC lyase, a representative of a family of glycosaminoglycan degrading enzymes.
Related PDB1cb8
Related Swiss-protQ59288
[2]
CommentsX-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
Medline ID21226222
PubMed ID11327856
JournalBiochemistry
Year2001
Volume40
Pages2359-72
AuthorsHuang W, Boju L, Tkalec L, Su H, Yang HO, Gunay NS, Linhardt RJ, Kim YS, Matte A, Cygler M
TitleActive site of chondroitin AC lyase revealed by the structure of enzyme-oligosaccharide complexes and mutagenesis.
Related PDB1hm2,1hm3,1hmu,1hmw
Related Swiss-protQ59288
[3]
PubMed ID12234466
JournalAnal Biochem
Year2002
Volume308
Pages77-82
AuthorsRye CS, Withers SG
TitleDevelopment of an assay and determination of kinetic parameters for chondroitin AC lyase using defined synthetic substrates.
[4]
PubMed ID12044904
JournalBiochim Biophys Acta
Year2002
Volume1597
Pages260-70
AuthorsCapila I, Wu Y, Rethwisch DW, Matte A, Cygler M, Linhardt RJ
TitleRole of arginine 292 in the catalytic activity of chondroitin AC lyase from Flavobacterium heparinum.
[5]
PubMed ID12175234
JournalJ Am Chem Soc
Year2002
Volume124
Pages9756-67
AuthorsRye CS, Withers SG
TitleElucidation of the mechanism of polysaccharide cleavage by chondroitin AC lyase from Flavobacterium heparinum.
[6]
PubMed ID12076149
JournalJ Org Chem
Year2002
Volume67
Pages4505-12
AuthorsRye CS, Withers SG
TitleSynthesis and evaluation of potential inhibitors of chondroitin AC lyase from Flavobacterium heparinum.

comments
The information on substrate & product was obtained from literature [3].

createdupdated
2004-07-012009-02-26


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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