Aminoglycoside binding and catalysis specificity of aminoglycoside 2 ''-phosphotransferase IVa: A thermodynamic, structural and kinetic study

摘要

Background: Aminoglycoside O-phosphotransferases make up a large class of bacterial enzymes that is widely distributed among pathogens and confer a high resistance to several clinically used aminoglycoside antibiotics. Aminoglycoside 2 ''-phosphotransferase IVa, APH(2 '')-IVa, is an important member of this class, but there is little information on the thermodynamics of aminoglycoside binding and on the nature of its rate-limiting step.