PROSITE documentation PDOC00093Chloramphenicol acetyltransferase active site
Chloramphenicol O-acetyltransferase (CAT) (EC 2.3.1.28) [1] catalyzes the acetyl-CoA dependent acetylation of chloramphenicol (Cm), an antibiotic which inhibits prokaryotic peptidyltransferase activity. Acetylation of Cm by CAT inactivates the antibiotic. A histidine residue, located in the C-terminal section of the enzyme, plays a central role in its catalytic mechanism. We derived a signature pattern from the region surrounding this active site residue.
Note:There is a second family of CAT [2], evolutionary unrelated to the main family described above. These CAT belong to the bacterial hexapeptide-repeat containing-transferases family (see <PDOC00094>).
Last update:November 1997 / Text revised.
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PROSITE method (with tools and information) covered by this documentation:
| 1 | Authors | Shaw W.V. Leslie A.G.W. |
| Title | Chloramphenicol acetyltransferase. | |
| Source | Annu. Rev. Biophys. Biophys. Chem. 20:363-386(1991). | |
| PubMed ID | 1867721 |
| 2 | Authors | Parent R. Roy P.H. |
| Title | The chloramphenicol acetyltransferase gene of Tn2424: a new breed of cat. | |
| Source | J. Bacteriol. 174:2891-2897(1992). | |
| PubMed ID | 1314803 |
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