Heparin lyase

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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.

[edit] References

• IUBMB entry for 4.2.2.7
• BRENDA references for 4.2.2.7 (Recommended.)
• PubMed references for 4.2.2.7
• PubMed Central references for 4.2.2.7
• Google Scholar references for 4.2.2.7
• 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: 6170–5. PMID 5484472. 

[edit] External links

The CAS registry number for this enzyme class is 9025-39-2.

• IUBMB entry for 4.2.2.7

• KEGG entry for 4.2.2.7

• BRENDA entry for 4.2.2.7

• NiceZyme view of 4.2.2.7

• EC2PDB: PDB structures for 4.2.2.7

• PRIAM entry for 4.2.2.7

• PUMA2 entry for 4.2.2.7

• IntEnz: Integrated Enzyme entry for 4.2.2.7

• MetaCyc entry for 4.2.2.7

• Atomic-resolution structures of enzymes belonging to this class

[edit] Gene Ontology (GO) codes

• EGO entry for GO code 0047488: heparin lyase

• AMIGO entry for GO code 0047488: heparin lyase