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Literature summary for 2.3.1.28 extracted from
- Influence of global fluorination on chloramphenicol acetyltransferase activity and stability (2006), Biotechnol. Bioeng., 94, 921-930.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
- |
Escherichia coli |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| additional information | replacement of all the leucine residues in the enzyme chloramphenicol acetyltransferase with the analog, 5',5',5'-trifluoroleucine, results in the maintenance of enzymatic activity under ambient temperatures as well as an enhancement in secondary structure but loss in stability against heat and denaturants or organic co-solvents | Escherichia coli |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Escherichia coli | - |
- |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
- |
Escherichia coli |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| CATI | - |
Escherichia coli |
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Release 2026.1 (March 2026)
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