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J Biol Chem. 2007 Dec 21;282(51):36777-81. Epub 2007 Nov 1.

Hyaluronan synthases: a decade-plus of novel glycosyltransferases.

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  • 1Department of Biochemistry and Molecular Biology and the Oklahoma Center for Medical Glycobiology, University of Oklahoma Health Sciences Center, Oklahoma City, Oklahoma 73104, USA. paul-weigel@ouhsc.edu

Abstract

Hyaluronan synthases (HASs) are glycosyltransferases that catalyze polymerization of hyaluronan found in vertebrates and certain microbes. HASs transfer two distinct monosaccharides in different linkages and, in certain cases, participate in polymer transfer out of the cell. In contrast, the vast majority of glycosyltransferases form only one sugar linkage. Although our understanding of HAS biochemistry is still incomplete, very good progress has been made since the first genetic identification of a HAS in 1993. New enzymes have been discovered, and some molecular details have emerged. Important findings are the lipid dependence of Class I HASs, the function of HASs as protein monomers, and the elucidation of mechanisms of synthesis by Class II HAS. We propose three classes of HASs based on differences in protein sequences, predicted membrane topologies, potential architectures, mechanisms, and direction of polymerization.

PMID:
17981795
DOI:
10.1074/jbc.R700036200
[PubMed - indexed for MEDLINE]
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