Literature summary for 2.3.1.28 extracted from

Tanaka, H.; Izaki, K.; Takahashi, H.
Some properties of chloramphenicol acetyltransferase, with particular reference to the mechanism of inhibition by basic triphenylmethane dyes (1974), J. Biochem., 76, 1009-1019.

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Inhibitors

Inhibitors	Comment	Organism	Structure
Crystal violet	strong, competitive for chloramphenicol, non-competitive for acetyl-CoA	Escherichia coli
ethyl violet	strong, competitive for chloramphenicol, non-competitive for acetyl-CoA	Escherichia coli

KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
0.033	-	chloramphenicol	-	Escherichia coli
0.083	-	acetyl-CoA	-	Escherichia coli

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	-	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
acetyl-CoA + chloramphenicol	-	Escherichia coli	CoA + chloramphenicol 3-acetate	-	?

Ki Value [mM]

Ki Value [mM]	Ki Value maximum [mM]	Inhibitor	Comment	Organism	Structure
additional information	-	additional information	-	Escherichia coli

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Release 2023.1 (January 2023)