Aminoglycoside-modifying enzymes: mechanisms of catalytic processes and inhibition

This publication has 65 references indexed in Scilit:

• Biologically Important Conformations of Aminoglycoside Antibiotics Bound to an Aminoglycoside 3‘-Phosphotransferase as Determined by Transferred Nuclear Overhauser Effect Spectroscopy
  Biochemistry, 1997
• Mechanism of aminoglycoside 3'-phosphotransferase type IIIa: His188 is not a phosphate-accepting residue
  Chemistry & Biology, 1996
• Purification, characterization, and investigation of the mechanism of aminoglycoside 3'-phosphotransferase type Ia
  Biochemistry, 1995
• Kinetic Mechanism of Aminoglycoside Phosphotransferase Type IIIa
  Journal of Biological Chemistry, 1995
• Molecular structure of kanamycin nucleotidyltransferase determined to 3.0-.ANG. resolution
  Biochemistry, 1993
• Nucleotide sequence of Acinetobacter baumannii aphA‐6 gene: evolutionary and functional implications of sequence homologies with nucleotide‐binding proteins, kinases and other aminoglycoside‐modifying enzymes
  Molecular Microbiology, 1988
• Substrate specificities and structure-activity relationships for the nucleotidylation of antibiotics catalyzed by aminoglycoside nucleotidyltransferase 2"-I
  Biochemistry, 1988
• Alternative substrate and inhibition kinetics of aminoglycoside nucleotidyltransferase 2''-I in support of a Theorell-Chance kinetic mechanism
  Biochemistry, 1988
• Substrate specificites and structure-activity relationships for acylation of antibiotics catalyzed by kanamycin acetyltransferase
  Biochemistry, 1984
• In Vitro Antibacterial Activity of the Aminoglycoside Antibiotics
  Clinical Infectious Diseases, 1983