{PDOC00093}
{PS00100; CAT}
{BEGIN}
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* Chloramphenicol acetyltransferase active site *
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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.

-Consensus pattern: Q-[LIV]-H-H-[SA]-x(2)-D-G-[FY]-H
                    [The second H is the active site residue]
-Sequences known to belong to this class detected by the pattern: ALL.
-Other sequence(s) detected in Swiss-Prot: NONE.

-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.

[ 1] Shaw W.V., Leslie A.G.W.
     "Chloramphenicol acetyltransferase."
     Annu. Rev. Biophys. Biophys. Chem. 20:363-386(1991).
     PubMed=1867721
[ 2] Parent R., Roy P.H.
     "The chloramphenicol acetyltransferase gene of Tn2424: a new breed of
     cat."
     J. Bacteriol. 174:2891-2897(1992).
     PubMed=1314803

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