Hyaluronate lyase

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hyaluronate lyase
Identifiers
EC number 4.2.2.1
CAS number 37259-53-3
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 / EGO

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.

Structural studies[edit]

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.

References[edit]

  • 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: 3061–5. PMID 13762462. 
  • 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 (2): 298–306. doi:10.1016/0003-9861(68)90138-0. PMID 5642600.