Biomaterial Database

Tinkering with antibiotic resistance: chloramphenicol acetyltransferase and its substrates. 1988

W V Shaw, and P Day, and A Lewendon, and I A Murray

Department of Biochemistry, University of Leicester, U.K.

UI	MeSH Term	Description	Entries
D009154	Mutation	Any detectable and heritable change in the genetic material that causes a change in the GENOTYPE and which is transmitted to daughter cells and to succeeding generations.	Mutations
D002702	Chloramphenicol Resistance	Nonsusceptibility of bacteria to the action of CHLORAMPHENICOL, a potent inhibitor of protein synthesis in the 50S ribosomal subunit where amino acids are added to nascent bacterial polypeptides.	Chloramphenicol Resistances
D001665	Binding Sites	The parts of a macromolecule that directly participate in its specific combination with another molecule.	Combining Site,Binding Site,Combining Sites,Site, Binding,Site, Combining,Sites, Binding,Sites, Combining
D013379	Substrate Specificity	A characteristic feature of enzyme activity in relation to the kind of substrate on which the enzyme or catalytic molecule reacts.	Specificities, Substrate,Specificity, Substrate,Substrate Specificities
D015500	Chloramphenicol O-Acetyltransferase	An enzyme that catalyzes the acetylation of chloramphenicol to yield chloramphenicol 3-acetate. Since chloramphenicol 3-acetate does not bind to bacterial ribosomes and is not an inhibitor of peptidyltransferase, the enzyme is responsible for the naturally occurring chloramphenicol resistance in bacteria. The enzyme, for which variants are known, is found in both gram-negative and gram-positive bacteria. EC 2.3.1.28.	CAT Enzyme,Chloramphenicol Acetyltransferase,Chloramphenicol Transacetylase,Acetyltransferase, Chloramphenicol,Chloramphenicol O Acetyltransferase,Enzyme, CAT,O-Acetyltransferase, Chloramphenicol,Transacetylase, Chloramphenicol