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Literature summary for 2.3.1.28 extracted from

  • Van der Schueren, J.; Robben, J.; Volckaert, G.
    Misfolding of chloramphenicol acetyltransferase due to carboxy-terminal truncation can be corrected by second-site mutations (1998), Protein Eng., 11, 1211-1217.
    View publication on PubMed
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Cloned(Commentary)

Cloned (Comment) Organism
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 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
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 enzyme form CAT III
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
acetyl-CoA + chloramphenicol
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 Escherichia coli CoA + chloramphenicol 3-acetate
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 ?