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Description

Chloramphenicol acetyltransferase (UniProt: P62577, also known as EC:2.3.1.28, CAT) is encoded by the Cat gene (Gene ID: 59683728) in E. coli. Chloramphenicol acetyltransferase is an enzyme that catalyzes the acetyl-S-CoA-dependent acetylation of chloramphenicol at the 3-hydroxyl group leading to the production of 3-acetoxy chloramphenicol that does not bind to bacterial ribosomes and does not inhibit peptidyltransferase activity. It displays high stability in cells and has a half-life of about 48 hours. A highly reactive histidine residue has been implicated in the catalytic mechanism. CAT is shown to be an effector of chloramphenicol resistance in bacteria. Its synthesis is shown to be constitutive in E. coli and other Gram-negative bacteria that harbor plasmids bearing the structural gene for the enzyme. However, in Gram-positive bacteria such as staphylococci and streptococci it is synthesized only in the presence of chloramphenicol and related compounds. (Ref.:Shaw WH. (1983). CRC Crit. Rev. Biochem. 14(1), 1-46)., This mouse monoclonal Anti-Chloramphenicol Acetyltransferase, clone CAT-1, Cat. No. MAB3678-I is tested for use in Immunocytochemistry and Western Blotting and Immunofluorescence, for the detection of Chloramphenicol acetyltransferase.