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Literature summary for 2.3.1.28 extracted from
- Misfolding of chloramphenicol acetyltransferase due to carboxy-terminal truncation can be corrected by second-site mutations (1998), Protein Eng., 11, 1211-1217.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
- |
Escherichia coli |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| L145F | folding of chloramphenicol acetyltransferase is hampered by deletion of the carboxy-terminal tail including the last residue of the carboxy-terminal alpha-helix. Such truncated CAT polypeptides quantitatively aggregate into cytoplasmic inclusion bodies, which results in absence of chloramphenicol-resistant phenotype for the producing host. Introduction of Phe at amino acid position 145 improves the ability of the protein to fold into a soluble, enzymatically active conformation | Escherichia coli |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Escherichia coli | - |
enzyme form CAT III | - |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| acetyl-CoA + chloramphenicol | - |
Escherichia coli | CoA + chloramphenicol 3-acetate | - |
? |  |
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Release 2023.1 (January 2023)
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