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Antimicrobial Agents and Chemotherapy, August 1999, p. 2063-2065, Vol. 43, No. 8
0066-4804/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.

Identification of Functional Amino Acids in the Macrolide 2'-Phosphotransferase II

Kazuo Taniguchi, Akio Nakamura, Kazue Tsurubuchi, Aki Ishii, Koji O'Hara,* and Tetsuo Sawai

Division of Microbial Chemistry, Faculty of Pharmaceutical Sciences, Chiba University, Inage-ku, Chiba 263-8522, Japan

Received 9 November 1998/Returned for modification 21 March 1999/Accepted 27 May 1999

Macrolide 2'-phosphotransferase [MPH(2')] transfers the gamma  phosphate of ATP to the 2'-OH group of macrolide antibiotics. The role of aspartic acids in the putative ATP-binding site of MPH(2')II was investigated through the substitution of alanine for aspartate by site-directed mutagenesis. D200A, D209A, D219A, and D231A mutant strains were unable to inactivate the substrate oleandomycin, while a D227A mutant retained 7% of the activity of the original enzyme.

* Corresponding author. Mailing address: Division of Microbial Chemistry, Faculty of Pharmaceutical Sciences, Chiba University, 1-33 Yayoi-cho, Inage-ku, Chiba 263-8522, Japan. Phone: 81-43-290-2930. Fax: 81-43-290-2929. E-mail: oharak{at}p.chiba-u.ac.jp.

Antimicrobial Agents and Chemotherapy, August 1999, p. 2063-2065, Vol. 43, No. 8
0066-4804/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.


This article has been cited by other articles:

  • Nakamura, A., Miyakozawa, I., Nakazawa, K., O'Hara, K., Sawai, T. (2000). Detection and Characterization of a Macrolide 2'-Phosphotransferase from a Pseudomonas aeruginosa Clinical Isolate. Antimicrob. Agents Chemother. 44: 3241-3242 [Full Text]  


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