| EC |
4.2.2.1 |
| Accepted name: |
hyaluronate lyase |
| Reaction: |
Cleaves hyaluronate chains at a β-D-GlcNAc-(1→4)-β-D-GlcA bond, ultimately breaking the polysaccharide down to 3-(4-deoxy-β-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine. |
| Other name(s): |
hyaluronidase (ambiguous); glucuronoglycosaminoglycan lyase (ambiguous); spreading factor; mucinase (ambiguous) |
| Systematic name: |
hyaluronate lyase |
| Comments: |
The enzyme catalyses the degradation of hyaluronan by a β-elimination reaction. Also acts on chondroitin. The product is more systematically known as 3-(4-deoxy-α-L-threo-hex-4-enopyranosyluronic acid)-2-acetamido-2-deoxy-D-glucose |
| Links to other databases: |
BRENDA, EXPASY, Gene, KEGG, MetaCyc, PDB, CAS registry number: 37259-53-3 |
| References: |
| 1. |
Linker, A., Hoffman, P., Meyer, K., Sampson, P. and Korn, E.D. The formation of unsaturated disacharides from mucopoly-saccharides and their cleavage to α-keto acid by bacterial enzymes. J. Biol. Chem. 235 (1960) 3061. [PMID: 13762462] |
| 2. |
Meyer, K. and Rapport, M.M. Hyaluronidases. Adv. Enzymol. Relat. Subj. Biochem. 13 (1952) 199–236. [PMID: 14943668] |
| 3. |
Moran, F., Nasuno, S. and Starr, M.P. Extracellular and intracellular polygalacturonic acid trans-eliminases of Erwinia carotovora. Arch. Biochem. Biophys. 123 (1968) 298–306. [DOI] [PMID: 5642600] |
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| [EC 4.2.2.1 created 1961 as EC 4.2.99.1, transferred 1972 to EC 4.2.2.1, modified 2001] |
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