Kinetic Characterization of the Glycosyltransferase Module of Staphylococcus aureus PBP2-Reference-Cited by-同舟云学术

Kinetic Characterization of the Glycosyltransferase Module of Staphylococcus aureus PBP2

Published:2005-03-15 Issue:6 Volume:187 Page:2215-2217
ISSN:0021-9193
Container-title:Journal of Bacteriology
language:en
Short-container-title:J Bacteriol

Author:

Barrett Dianah¹,Leimkuhler Catherine¹,Chen Lan²,Walker Deborah³,Kahne Daniel¹,Walker Suzanne²

Affiliation:

1. Department of Chemistry and Chemical Biology, Harvard University, Cambridge

2. Department of Microbiology and Molecular Genetics, Harvard Medical School, Boston, Massachusetts

3. Department of Chemistry, Princeton University, Princeton, New Jersey

Abstract

ABSTRACT We report the heterologous overexpression and purification of Staphylococcus aureus PBP2 and demonstrate efficient glycan polymerization from lipid II in vitro. S. aureus PBP2 is the first purified gram-positive class A penicillin-binding protein to show good transglycosylase activity. This enables further studies on this important class of enzymes.

Publisher

American Society for Microbiology

Subject

Molecular Biology,Microbiology

Link

https://journals.asm.org/doi/pdf/10.1128/JB.187.6.2215-2217.2005

Reference19 articles.

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2. Lipid II Is an Intrinsic Component of the Pore Induced by Nisin in Bacterial Membranes

3. Bugg, T. D. 1999. Bacterial peptidoglycan biosynthesis and its inhibition, p. 241-294. In B. M. Pinto (ed.), Comprehensive natural products chemistry, vol. 3. Elsevier, Oxford, United Kingdom.

4. Chen, L., D. Walker, B. Sun, Y. Hu, S. Walker, and D. Kahne. 2003. Vancomycin analogues active against vanA-resistant strains inhibit bacterial transglycosylase without binding substrate. Proc. Natl. Acad. Sci. USA100:5658-5663.

5. The Glycosyltransferase Domain of Penicillin-Binding Protein 2a from Streptococcus pneumoniae Catalyzes the Polymerization of Murein Glycan Chains

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