Hyaluronate lyase

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hyaluronate lyase
hyaluronate lyase
Identifiers
EC no.	4.2.2.1
CAS no.	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
PMC
Search
PMC	articles
PubMed	articles
NCBI	proteins

Last updated September 01, 2025

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

Linker A, Hoffman P, Meyer K, Sampson P, Korn ED (1960). "The formation of unsaturated disaccharides from mucopoly-saccharides and their cleavage to alpha-keto acid by bacterial enzymes". Journal of Biological Chemistry. 235 (11): 3061–5. doi: 10.1016/S0021-9258(20)81309-X . PMID 13762462.
Meyer K, Rapport MM (1952). "Hyaluronidases". Advances in Enzymology and Related Areas of Molecular Biology. Advances in Enzymology - and Related Areas of Molecular Biology. Vol. 13. pp. 199–236. doi:10.1002/9780470122587.ch6. ISBN 978-0-470-64614-4. PMID 14943668.{{cite book}}: ISBN / Date incompatibility (help); |journal= ignored (help)
Moran F, Nasuno S, Starr MP (1968). "Extracellular and intracellular polygalalacturonic acid trans-eliminases of Erwinia carotovora". Archives of Biochemistry and Biophysics. 123 (2): 298–306. doi:10.1016/0003-9861(68)90138-0. PMID 5642600.

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v t e Carbon–oxygen lyases (EC 4.2) (primarily dehydratases)
4.2.1: Hydro-Lyases	Carbonic anhydrase Fumarase Aconitase Enolase Alpha Enolase 2 Enoyl-CoA hydratase/3-Hydroxyacyl ACP dehydrase Methylglutaconyl-CoA hydratase Tryptophan synthase Cystathionine beta synthase Porphobilinogen synthase 3-Isopropylmalate dehydratase Urocanase Uroporphyrinogen III synthase Nitrile hydratase
4.2.2: Acting on polysaccharides	Hyaluronate lyase Pectin lyase
4.2.3: Acting on phosphates	Threonine synthase
4.2.99: Other	Carboxymethyloxysuccinate lyase Hydroperoxide lyase

v t e Enzymes
Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Diffusion-limited enzyme Cofactor Enzyme catalysis
Regulation	Allosteric regulation Cooperativity Enzyme inhibitor Enzyme activator
Classification	EC number Enzyme superfamily Enzyme family List of enzymes
Kinetics	Enzyme kinetics Eadie–Hofstee diagram Hanes–Woolf plot Lineweaver–Burk plot Michaelis–Menten kinetics
Types	EC1 Oxidoreductases (list) EC2 Transferases (list) EC3 Hydrolases (list) EC4 Lyases (list) EC5 Isomerases (list) EC6 Ligases (list) EC7 Translocases (list)