Literature summary for 2.3.1.28 extracted from

Voloshchuk, N.; Lee, M.X.; Zhu, W.W.; Tanrikulu, I.C.; Montclare, J.K.
Fluorinated chloramphenicol acetyltransferase thermostability and activity profile: Improved thermostability by a single-isoleucine mutant (2007), Bioorg. Med. Chem. Lett., 17, 5907-5911.

Search for more literature for 2.3.1.28

Protein Variants

Protein Variants	Comment	Organism
L158I	fluorinated mutant expressed in trifluoroleucine shows enhanced thermostability compared to CAT T (CAT expressed in trifluoroleucine), suggesting that trifluoroleucine at position 158 contributes to a portion of the observed loss in thermostability upon global fluorination. Relative activity: 89% (non-fluorinated mutant), 51.7% (fluorinated mutant)	Escherichia coli
L208I	fluorinated mutant expressed in trifluoroleucine shows loss in thermostability	Escherichia coli
L821I	fluorinated mutant expressed in trifluoroleucine shows loss in thermostability	Escherichia coli
additional information	residue-specific incorporation of T into chloramphenicol acetyltransferase (CAT) results in a loss of thermostability. Relative activity: 34.6% (fluorinated CAT)	Escherichia coli

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	-	-	-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg]	Specific Activity Maximum [µmol/min/mg]	Comment	Organism
additional information	-	relative activity: 94.9% (wild-type), 34.6% (fluorinated CAT), 89% (mutant L158I), 51.7% (fluorinated mutant L158I)	Escherichia coli

Substrates and Products (Substrate)

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

Synonyms

Synonyms	Comment	Organism
CAT	-	Escherichia coli
chloramphenicol acetyltransferase	-	Escherichia coli

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Release 2026.1 (March 2026)