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The role of the substrate lipid in processive glycan polymerization by the peptidoglycan glycosyltransferases.

ABSTRACT: 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.

SUBMITTER: Perlstein DL

PROVIDER: S-EPMC2830065 | biostudies-literature | 2010 Jan

REPOSITORIES: biostudies-literature

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The role of the substrate lipid in processive glycan polymerization by the peptidoglycan glycosyltransferases.

Perlstein Deborah L DL Wang Tsung-Shing Andrew TS Doud Emma H EH Kahne Daniel D Walker Suzanne S

Journal of the American Chemical Society 20100101 1

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 ...[more]

PMID: 20017480

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