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Stereochemical Divergence of Polyprenol Phosphate Glycosyltransferases

Author(s)
Eichler, Jerry; Imperiali, Barbara
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Abstract
In the three domains of life, lipid-linked glycans contribute to various cellular processes ranging from protein glycosylation to glycosylphosphatidylinositol anchor biosynthesis to peptidoglycan assembly. In generating many of these glycoconjugates, phosphorylated polyprenol-based lipids are charged with single sugars by polyprenol phosphate glycosyltransferases. The resultant substrates serve as glycosyltransferase donors, complementing the more common nucleoside diphosphate sugars. It had been accepted that these polyprenol phosphate glycosyltransferases acted similarly, given their considerable sequence homology. Recent findings, however, suggest that matters may not be so simple. In this Opinion we propose that the stereochemistry of sugar addition by polyprenol phosphate glycosyltransferases is not conserved across evolution, even though the GT-A fold that characterizes such enzymes is omnipresent. Keywords: dolichol phosphate, dolichol phosphate glucose synthase, dolichol phosphate mannose synthase, polyprenol phosphate, protein glycosylation, stereochemistry
Date issued
2018-01
URI
http://hdl.handle.net/1721.1/119846
Department
Massachusetts Institute of Technology. Department of Biology; Massachusetts Institute of Technology. Department of Chemistry
Journal
Trends in Biochemical Sciences
Publisher
Elsevier
Citation
Eichler, Jerry, and Barbara Imperiali. “Stereochemical Divergence of Polyprenol Phosphate Glycosyltransferases.” Trends in Biochemical Sciences 43, no. 1 (January 2018): 10–17.
Version: Author's final manuscript
ISSN
0968-0004

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