Heparin lyase

heparin lyase
Identifiers
EC number 4.2.2.7
CAS number 9025-39-2
Databases
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum
Gene Ontology AmiGO / QuickGO

In enzymology, a heparin lyase (EC 4.2.2.7) is an enzyme that catalyzes the chemical reaction

Eliminative cleavage of polysaccharides containing 1,4-linked D-glucuronate or L-iduronate residues and 1,4-alpha-linked 2-sulfoamino-2-deoxy-6-sulfo-D-glucose residues to give oligosaccharides with terminal 4-deoxy-alpha-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

    • 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&ndash, 5. PMID 5484472.
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