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J. Biol. Chem., Vol. 282, Issue 51, 36777-36781, December 21, 2007

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Minireview

Hyaluronan Synthases: A Decade-plus of Novel Glycosyltransferases^*

From the Department of Biochemistry and Molecular Biology and the Oklahoma Center for Medical Glycobiology, University of Oklahoma Health Sciences Center, Oklahoma City, Oklahoma 73104

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.

^* This minireview will be reprinted in the 2007 Minireview Compendium, which will be available in January, 2008. This work was supported by National Institutes of Health Grants GM35978 (to P. H. W.) and GM56497 (to P. L. D.) and National Science Foundation Grant MCB-9876193 (to P. L. D.).

The on-line version of this article (available at http://www.jbc.org) contains supplemental Figs. 1 and 2.

¹ To whom correspondence may be addressed. Tel.: 405-271-2227; Fax: 405-271-3092; E-mail: paul-weigel{at}ouhsc.edu or paul-deangelis{at}ouhsc.edu.

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