title: Inhibition kinetics of chloramphenicol acetyltransferase by selected detergents.
abstract: Kinetic analyses indicate that the inhibitory effects of the nonionic detergents Triton X-100 and Nonidet P-40 on chloramphenicol acetyltransferase are exerted by a competitive and a non-competitive mechanism with respect to the substrates chloramphenicol and acetyl-CoA, respectively. Comparison with nonionic detergents without an aromatic moiety like that present in Triton X-100 and Nonidet P-40 suggests that the aromatic groups in these two detergents may compete with chloramphenicol for binding to the hydrophobic, active site in the chloramphenicol acetyltransferase.
authors.affiliation: Section of Biochemistry, Molecular and Cell Biology, Cornell University, Ithaca, NY.
authors.forename: J
authors.initials: J
authors.lastname: Lu
authors.forename: C
authors.initials: C
authors.lastname: Jiang
mesh_terms: D000105:Acetyl Coenzyme A / Q000378:metabolism; D000818:Animals; D001667:Binding, Competitive; D002701:Chloramphenicol / Q000378:metabolism; D015500:Chloramphenicol O-Acetyltransferase / Q000037:antagonists & inhibitors* / Q000235:genetics; D003840:Deoxycholic Acid / Q000494:pharmacology; D003902:Detergents / Q000494:pharmacology*; D004305:Dose-Response Relationship, Drug; D005960:Glucosides / Q000494:pharmacology; D006367:HeLa Cells; D006801:Humans; D007700:Kinetics; D008954:Models, Biological; D017830:Octoxynol / Q000494:pharmacology; D011092:Polyethylene Glycols / Q000494:pharmacology; D011136:Polysorbates / Q000494:pharmacology; D012967:Sodium Dodecyl Sulfate / Q000494:pharmacology; D014162:Transfection
chemical_list: D003902:Detergents; D005960:Glucosides; D011136:Polysorbates; D003840:Deoxycholic Acid; C018619:octyl-beta-D-glucoside; D012967:Sodium Dodecyl Sulfate; D011092:Polyethylene Glycols; C038732:dodecyl glucoside; D002701:Chloramphenicol; D000105:Acetyl Coenzyme A; D017830:Octoxynol; C010615:Nonidet P-40; D015500:Chloramphenicol O-Acetyltransferase