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Journal of Bacteriology, March 2005, p. 2215-2217, Vol. 187, No. 6
0021-9193/05/$08.00+0     doi:10.1128/JB.187.6.2215-2217.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.

Kinetic Characterization of the Glycosyltransferase Module of Staphylococcus aureus PBP2

Dianah Barrett,1 Catherine Leimkuhler,1 Lan Chen,2 Deborah Walker,3 Daniel Kahne,1 and Suzanne Walker2*

Department of Chemistry and Chemical Biology, Harvard University, Cambridge,1 Department of Microbiology and Molecular Genetics, Harvard Medical School, Boston, Massachusetts,2 Department of Chemistry, Princeton University, Princeton, New Jersey3

Received 27 September 2004/ Accepted 20 December 2004

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.

* Corresponding author. Mailing Address: Department of Microbiology & Molecular Genetics, Harvard Medical School, 200 Longwood Ave., Boston, MA 02115. Phone: (617) 432-5488. Fax: (617) 496-0215. E-mail: suzanne_walker{at}hms.harvard.edu.

Journal of Bacteriology, March 2005, p. 2215-2217, Vol. 187, No. 6
0021-9193/05/$08.00+0     doi:10.1128/JB.187.6.2215-2217.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.



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