The Role of the Substrate Lipid in Processive Glycan Polymerization by the Peptidoglycan Glycosyltransferases

The peptidoglycan glycosyltransferases (PGTs) catalyze the processive polymerization of a C55 lipid-linked disaccharide (Lipid II) to form peptidoglycan, the main component of the bacterial cell wall. Our ability to understand this reaction has been limited due to challenges identifying the appropri...

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Bibliographic Details
Published inJournal of the American Chemical Society Vol. 132; no. 1; pp. 48 - 49
Main Authors Perlstein, Deborah L, Andrew Wang, Tsung-Shing, Doud, Emma H, Kahne, Daniel, Walker, Suzanne
Format Journal Article
LanguageEnglish
Published United States American Chemical Society 13.01.2010
Subjects
Aquifoliaceae - enzymology
Electrophoresis, Polyacrylamide Gel
Lipid Metabolism
Lipids - chemistry
Peptidoglycan Glycosyltransferase - metabolism
Polymers - chemistry
Polymers - metabolism
Polysaccharides - chemistry
Polysaccharides - metabolism
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Summary:The peptidoglycan glycosyltransferases (PGTs) catalyze the processive polymerization of a C55 lipid-linked disaccharide (Lipid II) to form peptidoglycan, the main component of the bacterial cell wall. Our ability to understand this reaction has been limited due to challenges identifying the appropriate substrate analogues to selectively interrogate the donor (the elongating strand) and acceptor (Lipid II) sites. To address this problem, we have developed an assay using synthetic substrates that can discriminate between the donor and acceptor sites of the PGTs. We have shown that each site has a distinct lipid length preference. We have also established that processive polymerization depends on the length of the lipid attached to the donor.
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ISSN:0002-7863
1520-5126
DOI:10.1021/ja909325m