Identification of Functional Amino Acids in the Macrolide 2′-Phosphotransferase II
- 1 August 1999
- journal article
- research article
- Published by American Society for Microbiology in Antimicrobial Agents and Chemotherapy
- Vol. 43 (8) , 2063-2065
- https://doi.org/10.1128/aac.43.8.2063
Abstract
Macrolide 2′-phosphotransferase [MPH(2′)] transfers the γ 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.Keywords
This publication has 26 references indexed in Scilit:
- Identification ofEscherichia coliclinical isolates producing macrolide 2′-phosphotransferase by a highly sensitive detection methodFEMS Microbiology Letters, 1998
- Spectinomycin Kinase from Legionella pneumophilaJournal of Biological Chemistry, 1998
- Cloning and nucleotide sequence of themphBgene for macrolide 2′-phosphotransferase II inEscherichia coliFEMS Microbiology Letters, 1996
- Mechanism of aminoglycoside 3'-phosphotransferase type IIIa: His188 is not a phosphate-accepting residueChemistry & Biology, 1996
- Purification and characterization of macrolide 2′-phosphotransferase type II from a strain of Escherichia coli highly resistant to macrolide antibioticsFEMS Microbiology Letters, 1992
- Site-specific mutations of conserved C-terminal residues in aminoglycoside 3′-phosphotransferase II: Phenotypic and structural analysis of mutant enzymesBiochemical and Biophysical Research Communications, 1992
- Altered substrate specificity by substitutions at Tyr218 in bacterial aminoglycoside 3′-phosphotransferase-IIFEMS Microbiology Letters, 1992
- Altered substrate specificity by substitutions at Tyr218 in bacterial aminoglycoside 3′-phosphotransferase-IIFEMS Microbiology Letters, 1992
- Purification and characterization of chromosomal streptomycin adenylyltransferase from derivatives ofBacillus subtilisMarburg 168FEMS Microbiology Letters, 1987
- Repression of porin synthesis by salicylate in Escherichia coli, Klebsiella pneumoniae and Serratia marcescensFEMS Microbiology Letters, 1987