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chloramphenicol acetyltransferase
Chloramphenicol acetyltransferase 3CLA transparent.png
Ribbon diagram of the chloramphenicol acetyltransferase trimer with chloramphenicol bound. From PDB 3CLA.
Identifiers
Symbol CAT
Entrez 2847485
UniProt P62577
Other data
EC number 2.3.1.28

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.

References

  1. ^ 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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