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Heparin lyase

From Wikipedia, the free encyclopedia
heparin lyase
Identifiers
EC no.4.2.2.7
CAS no.9025-39-2
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO
Search
PMCarticles
PubMedarticles
NCBIproteins

The enzyme heparin lyase (EC 4.2.2.7) catalyzes the following process:

Eliminative cleavage of polysaccharides containing (1→4)-linked D-glucuronate or L-iduronate residues and (1→4)-α-linked 2-sulfoamino-2-deoxy-6-sulfo-D-glucose residues to give oligosaccharides with terminal 4-deoxy-α-D-gluc-4-enuronosyl groups at their non-reducing ends

This enzyme belongs to the family of lyases, specifically those carbon-oxygen lyases acting on polysaccharides. The systematic name of this enzyme class is heparin lyase. Other names in common use include heparin eliminase, and heparinase.

References

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  • Hovingh P, Linker A (1970). "The enzymatic degradation of heparin and heparitin sulfate. 3 Purification of a heparitinase and a heparinase from flavobacteria". J. Biol. Chem. 245 (22): 6170–5. PMID 5484472.