title: Nonlinear steady-state kinetics of chloramphenicol acetyltransferase.
abstract: Steady-state kinetic analysis of chloramphenicol acetyltransferase showed that medium effects (higher temperatures or pH, higher ionic strengths, or lower values for dielectric constant) altered the kinetic behaviour of the enzyme with acetyl-CoA as substrate, but did not significantly affect behaviour with chloramphenicol. This was manifest as an increase in the degree of the rate equation to a 2:2 function. This is interpreted in terms of perturbations to the enzyme at or near the acetyl-CoA binding region of the enzyme.
authors.affiliation: Department of Microbiology, School of Animal and Microbial Sciences, University of Reading, Whiteknights, Great Britain.
authors.forename: M J
authors.initials: MJ
authors.lastname: Crabbe
authors.forename: D
authors.initials: D
authors.lastname: Goode
mesh_terms: D000105:Acetyl Coenzyme A / Q000378:metabolism*; D002701:Chloramphenicol / Q000378:metabolism; D015500:Chloramphenicol O-Acetyltransferase / Q000378:metabolism*; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D009994:Osmolar Concentration; D013696:Temperature
chemical_list: D002701:Chloramphenicol; D000105:Acetyl Coenzyme A; D015500:Chloramphenicol O-Acetyltransferase