| Literature DB >> 10428938 |
K Taniguchi1, A Nakamura, K Tsurubuchi, A Ishii, K O'Hara, T Sawai.
Abstract
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.Entities:
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Year: 1999 PMID: 10428938 PMCID: PMC89416
Source DB: PubMed Journal: Antimicrob Agents Chemother ISSN: 0066-4804 Impact factor: 5.191