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Search The CSA
PDB ID
UNIPROT ID
EC Number

Catalytic Site Atlas

CSA LITERATURE entry for 1cb8

E.C. namechondroitin AC lyase
SpeciesFlavobacterium heparinum ()
E.C. Number (IntEnz) 4.2.2.5
CSA Homologues of 1cb8There are 40 Homologs
CSA Entries With UniProtID Q59288
CSA Entries With EC Number 4.2.2.5
PDBe Entry 1cb8
PDBSum Entry 1cb8
MACiE Entry 1cb8

Literature Report

IntroductionThis enzyme from Flavobacterium heparinum is highly activated to chondroitin 4-sulfate and chondroitin 6-sulfate. These are glycosaminoglycans (GAGs) which are major components of the extracellular matrix. The enzyme consists of two domains, a C-terminal domain containing a 4-beta-sheet sandwich, and an N-terminal domain containing the putative active site which is made up of alpha-helices.
MechansimMechanism unknown. His225 may act as a catalytic general base. Arg288 and Arg292 are thought to interact with the substrate.
Reaction

Catalytic Sites for 1cb8

Annotated By Reference To The Literature - Site 2 (Perform Site Search)
ResidueChainNumberUniProtKB NumberFunctional PartFunctionTargetDescription
TyrA234234macie:sideChain
HisA225225macie:sideChain
ArgA288288macie:sideChain

Literature References

Notes:
Féthière J
Crystal structure of chondroitin AC lyase, a representative of a family of glycosaminoglycan degrading enzymes.
J Mol Biol 1999 288 635-647
PubMed: 10329169
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