Chloramphenicol acetyltransferase (or CAT) is a bacterial enzyme that detoxifies the antibiotic chloramphenicol and is responsible for chloramphenicol resistance in bacteria.[1] This enzyme covalently attaches an acetyl group from acetyl-CoA to chloramphenicol, which prevents chloramphenicol from binding to ribosomes.
Application
CAT is used as a reporter system to measure the level of a promoter or its tissue-specific expression. The CAT assay involves monitoring acetylation of radioactive chloramphenicol on a TCA plate because acetylation significantly changes migration rate.[vague]
References
- ^ Shaw WV, Packman LC, Burleigh BD, Dell A, Morris HR, Hartley BS (1979). "Primary structure of a chloramphenicol acetyltransferase specified by R plasmids". Nature 282 (5741): 870–2. PMID 390404.
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