Biology:Hyaluronate lyase
From HandWiki
| hyaluronate lyase | |||||||||
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| 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 / QuickGO | ||||||||
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The enzyme hyaluronate lyase (EC 4.2.2.1) catalyzes the chemical reaction
- Cleaves hyaluronate chains at a β-D-GalNAc-(1→4)-β-D-GlcA bond, ultimately breaking the polysaccharide down to 3-(4-deoxy-β-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 (ambiguous), (hyalurononglucosaminidase) (ambiguous), (hyaluronoglucuronidase)], glucuronoglycosaminoglycan lyase, spreading factor, and mucinase (ambiguous).
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.
References
- "The formation of unsaturated disaccharides from mucopoly-saccharides and their cleavage to alpha-keto acid by bacterial enzymes". Journal of Biological Chemistry 235: 3061–5. 1960. PMID 13762462.
- "Hyaluronidases". Advances in Enzymology and Related Subjects of Biochemistry 13: 199–236. 1952. PMID 14943668.
- "Extracellular and intracellular polygalalacturonic acid trans-eliminases of Erwinia carotovora". Archives of Biochemistry and Biophysics 123 (2): 298–306. 1968. doi:10.1016/0003-9861(68)90138-0. PMID 5642600.
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