Any feedback?
Literature summary for 2.3.1.28 extracted from
- A study of the enzymatic inactivation of chloramphenicol by highly purified chloramphenicol acetyltransferase (1980), Biochim. Biophys. Acta, 614, 339-349.
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 |
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
