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Article

Hyaluronidase activity of human Hyal1 requires active site acidic and tyrosine residues.

The Journal of biological chemistry - 3 Apr 2009

Zhang Ling, Bharadwaj Alamelu G, Casper Andrew, Barkley Joel, Barycki Joseph J, Simpson Melanie A

Abstract excerpt

Hyaluronidases are a family of endolytic glycoside hydrolases that cleave the beta1-4 linkage between N-acetylglucosamine and glucuronic acid in hyaluronan polymers via a substrate-assisted mechanism. In humans, turnover of hyaluronan by this enzyme family is critical for normal extracellular matrix remodeling. However, elevated expression of the Hyal1 isozyme accelerates tumor growth and metastatic progression....

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Identifiers

PMID: 19201751
DOI: 10.1074/jbc.M900210200
PMCID: PMC2666596

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Hyaluronidase activity of human Hyal1 requires active site acidic and tyrosine residues.PMID 19201751Read ↗

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