Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 2.3.1.28 extracted from

  • Thibault, G.; Guitard, M.; Daigneault, R.
    A study of the enzymatic inactivation of chloramphenicol by highly purified chloramphenicol acetyltransferase (1980), Biochim. Biophys. Acta, 614, 339-349.
    View publication on PubMed
Search for more literature for 2.3.1.28

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
acetyl-CoA + chloramphenicol Escherichia coli enzymatic inactivation of chloramphenicol CoA + chloramphenicol 3-acetate
-
 ?

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
 R-factor-bearing strain W677/HJR 66
-

Purification (Commentary)

Purification (Comment) Organism
-
 Escherichia coli

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
130.6
-
-
 Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
acetyl-CoA + chloramphenicol
-
 Escherichia coli CoA + chloramphenicol 3-acetate
-
 ?
acetyl-CoA + chloramphenicol enzymatic inactivation of chloramphenicol Escherichia coli CoA + chloramphenicol 3-acetate
-
 ?
acetyl-CoA + chloramphenicol 1-acetate the enzyme acetylates specifically at the 3-hydroxy position. The diacetylation is possible only because of non-enzymatic interconversion of chloramphenical 3-acetate to chloramphenicol 1-acetate at higher pH values Escherichia coli CoA + chloramphenicol 1,3-diacetate
-
 ?

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.6
-
-
 Escherichia coli