The enzyme hyaluronate lyase ()

catalyzes Catalysis () is the process of increasing the rate of a chemical reaction by adding a substance known as a catalyst (). Catalysts are not consumed in the reaction and remain unchanged after it. If the reaction is rapid and the catalyst recyc ...

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

lyase In biochemistry, a lyase is an enzyme that catalyzes the breaking (an elimination reaction) of various chemical bonds by means other than hydrolysis (a substitution reaction) and oxidation, often forming a new double bond or a new ring structure. ...

s, 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 tertiary structure, structures have been solved for this class of enzymes, with PDB accession codes , , , , , , , , , , , , , , , , , , , , , , , , , , and .

References

* * * EC 4.2.2 Enzymes of known structure {{4.2-enzyme-stub