DB code: T00091

CATH domain 1.50.10.100 : Glycosyltransferase Catalytic domain
2.70.98.10 : Beta-galactosidase; Chain A, domain 5
2.60.220.10 : Chondroitinase Ac; Chain A, domain 3
E.C. 4.2.2.5
CSA 1cb8
M-CSA 1cb8
MACiE

CATH domain Related DB codes (homologues)

Uniprot Enzyme Name
UniprotKB Protein name Synonyms RefSeq CAZy Pfam
Q59288 Chondroitinase-AC
EC 4.2.2.5
Chondroitin sulfate AC lyase
Chondroitin-AC eliminase
Chondroitin-AC lyase
YP_003091070.1 (Protein)
NC_013061.1 (DNA/RNA sequence)
PL8 (Polysaccharide Lyase Family 8)
PF02278 (Lyase_8)
PF02884 (Lyase_8_C)
PF08124 (Lyase_8_N)
[Graphical View]

KEGG enzyme name
chondroitin AC lyase
chondroitinase (ambiguous)
chondroitin sulfate lyase
chondroitin AC eliminase
chondroitin AC lyase
chondroitinase AC
ChnAC

UniprotKB: Accession Number Entry name Activity Subunit Subcellular location Cofactor
Q59288 CSLA_PEDHE Eliminative 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. Monomer. Binds 1 calcium ion per subunit.

KEGG Pathways
Map code Pathways E.C.

Compound table
Cofactors Substrates Products Intermediates
KEGG-id C00076 C00634 C00635 C00634 C04864 C00635 C04865
E.C.
Compound Calcium Chondroitin 4-sulfate Chondroitin 6-sulfate Chondroitin 4-sulfate 4-Deoxy-beta-D-gluc-4-enuronosyl-(1,3)-N-acetyl-D-galactosamine 4-sulfate Chondroitin 6-sulfate 4-Deoxy-beta-D-gluc-4-enuronosyl-(1,3)-N-acetyl-D-galactosamine 6-sulfate
Type divalent metal (Ca2+, Mg2+) amide group,carbohydrate,carboxyl group,polysaccharide,sulfate group amide group,carbohydrate,carboxyl group,polysaccharide,sulfate group amide group,carbohydrate,carboxyl group,polysaccharide,sulfate group amide group,carboxyl group,polysaccharide,sulfate group amide group,carbohydrate,carboxyl group,polysaccharide,sulfate group amide group,carboxyl group,polysaccharide,sulfate group
ChEBI 29108
15931
16735
PubChem 271
10298166
10298165
1cb8A01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1hm2A01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Bound:IDR-ASG-IDR-ASG (chain D) Unbound Unbound Unbound Unbound Unbound
1hm3A01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Analogue:GCU-NAG Unbound Analogue:GCU-NAG Unbound
1hmuA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Bound:DGC-ASG (chain D) Unbound Unbound
1hmwA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Analogue:GCD-ASG-BDP-NG6 (chain D) Unbound Unbound Unbound Unbound
1cb8A02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:_CA Unbound Unbound Unbound Unbound Unbound Unbound
1hm2A02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:_CA Unbound Unbound Unbound Unbound Unbound Unbound
1hm3A02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:_CA Unbound Unbound Unbound Unbound Unbound Unbound
1hmuA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:_CA Unbound Unbound Unbound Unbound Unbound Unbound
1hmwA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:_CA Unbound Unbound Unbound Unbound Unbound Unbound
1cb8A03 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1hm2A03 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1hm3A03 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1hmuA03 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1hmwA03 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound Unbound

Reference for Active-site residues
resource references E.C.
PDB;1cb8 & Swiss-prot;Q59288 & literature [2], [4]

Active-site residues
PDB Catalytic residues Cofactor-binding residues Modified residues Main-chain involved in catalysis Comment
1cb8A01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 225;TYR 234;ARG 288
1hm2A01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 225;TYR 234;ARG 288
1hm3A01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 225;TYR 234;ARG 288
1hmuA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 225;TYR 234;ARG 288
1hmwA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 225;TYR 234;ARG 288
1cb8A02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain GLU 405;ASP 407;ASP 416;TYR 417(Calcium binding)
1hm2A02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain GLU 405;ASP 407;ASP 416;TYR 417(Calcium binding)
1hm3A02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain GLU 405;ASP 407;ASP 416;TYR 417(Calcium binding)
1hmuA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain GLU 405;ASP 407;ASP 416;TYR 417(Calcium binding)
1hmwA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain GLU 405;ASP 407;ASP 416;TYR 417(Calcium binding)
1cb8A03 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1hm2A03 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1hm3A03 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1hmuA03 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1hmwA03 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain

References for Catalytic Mechanism
References Sections No. of steps in catalysis
[2]
p.2369-2371, Fig.8 2
[3]
Fig.1

References
[1]
Resource
Comments X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
Medline ID 99264394
PubMed ID 10329169
Journal J Mol Biol
Year 1999
Volume 288
Pages 635-47
Authors Fethiere J, Eggimann B, Cygler M
Title Crystal structure of chondroitin AC lyase, a representative of a family of glycosaminoglycan degrading enzymes.
Related PDB 1cb8
Related UniProtKB Q59288
[2]
Resource
Comments X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
Medline ID 21226222
PubMed ID 11327856
Journal Biochemistry
Year 2001
Volume 40
Pages 2359-72
Authors Huang W, Boju L, Tkalec L, Su H, Yang HO, Gunay NS, Linhardt RJ, Kim YS, Matte A, Cygler M
Title Active site of chondroitin AC lyase revealed by the structure of enzyme-oligosaccharide complexes and mutagenesis.
Related PDB 1hm2 1hm3 1hmu 1hmw
Related UniProtKB Q59288
[3]
Resource
Comments
Medline ID
PubMed ID 12234466
Journal Anal Biochem
Year 2002
Volume 308
Pages 77-82
Authors Rye CS, Withers SG
Title Development of an assay and determination of kinetic parameters for chondroitin AC lyase using defined synthetic substrates.
Related PDB
Related UniProtKB
[4]
Resource
Comments
Medline ID
PubMed ID 12044904
Journal Biochim Biophys Acta
Year 2002
Volume 1597
Pages 260-70
Authors Capila I, Wu Y, Rethwisch DW, Matte A, Cygler M, Linhardt RJ
Title Role of arginine 292 in the catalytic activity of chondroitin AC lyase from Flavobacterium heparinum.
Related PDB
Related UniProtKB
[5]
Resource
Comments
Medline ID
PubMed ID 12175234
Journal J Am Chem Soc
Year 2002
Volume 124
Pages 9756-67
Authors Rye CS, Withers SG
Title Elucidation of the mechanism of polysaccharide cleavage by chondroitin AC lyase from Flavobacterium heparinum.
Related PDB
Related UniProtKB
[6]
Resource
Comments
Medline ID
PubMed ID 12076149
Journal J Org Chem
Year 2002
Volume 67
Pages 4505-12
Authors Rye CS, Withers SG
Title Synthesis and evaluation of potential inhibitors of chondroitin AC lyase from Flavobacterium heparinum.
Related PDB
Related UniProtKB

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

Created Updated
2004-07-01 2009-02-26