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, 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: 3061–5. PMID 13762462..mw-parser-output cite.citation{font-style:inherit}.mw-parser-output q{quotes:"""""""'""'"}.mw-parser-output code.cs1-code{color:inherit;background:inherit;border:inherit;padding:inherit}.mw-parser-output .cs1-lock-free a{background:url("//upload.wikimedia.org/wikipedia/commons/thumb/6/65/Lock-green.svg/9px-Lock-green.svg.png")no-repeat;background-position:right .1em center}.mw-parser-output .cs1-lock-limited a,.mw-parser-output .cs1-lock-registration a{background:url("//upload.wikimedia.org/wikipedia/commons/thumb/d/d6/Lock-gray-alt-2.svg/9px-Lock-gray-alt-2.svg.png")no-repeat;background-position:right .1em center}.mw-parser-output .cs1-lock-subscription a{background:url("//upload.wikimedia.org/wikipedia/commons/thumb/a/aa/Lock-red-alt-2.svg/9px-Lock-red-alt-2.svg.png")no-repeat;background-position:right .1em center}.mw-parser-output .cs1-subscription,.mw-parser-output .cs1-registration{color:#555}.mw-parser-output .cs1-subscription span,.mw-parser-output .cs1-registration span{border-bottom:1px dotted;cursor:help}.mw-parser-output .cs1-hidden-error{display:none;font-size:100%}.mw-parser-output .cs1-visible-error{font-size:100%}.mw-parser-output .cs1-subscription,.mw-parser-output .cs1-registration,.mw-parser-output .cs1-format{font-size:95%}.mw-parser-output .cs1-kern-left,.mw-parser-output .cs1-kern-wl-left{padding-left:0.2em}.mw-parser-output .cs1-kern-right,.mw-parser-output .cs1-kern-wl-right{padding-right:0.2em}
  


• 
  Meyer K, Rapport MM (1952). "Hyaluronidases". Advances in Enzymology and Related Subjects of Biochemistry. 13: 199&ndash, 236. PMID 14943668.
  


• 
  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&ndash, 306. doi:10.1016/0003-9861(68)90138-0. PMID 5642600.