Our deepest condolences go out to his family and friends, and to all those who had the privilege of working with him. Rest in peace, Amos. Your work will live on long after you are gone.
PROSITE documentation PDOC00093Chloramphenicol acetyltransferase active site
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PURL: https://purl.expasy.org/prosite/documentation/PDOC00093
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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