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Literature summary for 2.3.1.28 extracted from
- Some properties of chloramphenicol acetyltransferase, with particular reference to the mechanism of inhibition by basic triphenylmethane dyes (1974), J. Biochem., 76, 1009-1019.
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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