Hyaluronate lyase

From Wikipedia, the free encyclopedia

In enzymology, a hyaluronate lyase (EC 4.2.2.1) is an enzyme that catalyzes the chemical reaction

Cleaves hyaluronate chains at a beta-D-GalNAc-(1->4)-beta-D-GlcA bond, ultimately breaking the polysaccharide down to 3-(4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine

This enzyme belongs to the family of lyases, specifically those carbon-oxygen lyases acting on polysaccharides. The systematic name of this enzyme class is hyaluronate lyase. Other names in common use include hyaluronidase [but cf. internal_xref(ec_num(3,2,1,35)), (hyalurononglucosaminidase) and internal_xref(ec_num(3,2,1,36)), (hyaluronoglucuronidase)], glucuronoglycosaminoglycan lyase, spreading factor, and mucinase.

1 Structural studies
2 References
3 External links
- 3.1 Gene Ontology (GO) codes

[edit] Structural studies

As of late 2007, 27 structures have been solved for this class of enzymes, with PDB accession codes 1C82, 1EGU, 1F1S, 1F9G, 1I8Q, 1LOH, 1LXK, 1LXM, 1N7N, 1N7O, 1N7P, 1N7Q, 1N7R, 1OJM, 1OJN, 1OJO, 1OJP, 1W3Y, 2BRP, 2BRV, 2BRW, 2C3F, 2DP5, 2PK1, 2YVV, 2YW0, and 2YX2.

[edit] References

IUBMB entry for 4.2.2.1
BRENDA references for 4.2.2.1 (Recommended.)
PubMed references for 4.2.2.1
PubMed Central references for 4.2.2.1
Google Scholar references for 4.2.2.1
Linker A, Hoffman P, Meyer K, Sampson P and Korn ED (1960). "The formation of unsaturated disacharides from mucopoly-saccharides and their cleavage to alpha-keto acid by bacterial enzymes". J. Biol. Chem. 235: 3061.
MEYER K, RAPPORT MM (1952). "Hyaluronidases". Adv. Enzymol. Relat. Subj. Biochem. 13: 199–236. PMID 14943668.
Moran F, Nasuno S, Starr MP (1968). "Extracellular and intracellular polygllacturonic acid trans-eliminases of Erwinia carotovora". Arch. Biochem. Biophys. 123: 298–306. PMID 5642600.