Stereochemical Divergence of Polyprenol Phosphate Glycosyltransferases
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TIBS-revised Eichler and Imperiali-2017-withFigs.pdf
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660.42 KB
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Author(s)
Eichler, Jerry
Imperiali, Barbara
Date Issued
January 2018
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
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
MIT Department
Massachusetts Institute of Technology. Department of Biology
Massachusetts Institute of Technology. Department of Chemistry
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Creative Commons Attribution-NonCommercial-NoDerivs License
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DOI of Published Version
https://doi.org/10.1016/j.tibs.2017.10.008
