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Literature summary for 2.3.1.28 extracted from

  • Van der Schueren, J.; Robben, J.; Goossens, K.; Heremans, K.; Volckaert, G.
    Identification of local carboxy-terminal hydrophobic interactions essential for folding or stability of chloramphenicol acetyltransferase (1996), J. Mol. Biol., 256, 878-888.
    View publication on PubMed

Protein Variants

Protein Variants Comment Organism
C214A 95% of the in vivo produced mutant polypeptide is soluble compared to 90% for the wild-type enzyme. Mutant enzyme loses 31% of activity after 30 min at 65°C compared to 15% for the wild-type enzyme Escherichia coli
C214D 50% of the in vivo produced mutant polypeptide is soluble compared to 90% for the wild-type enzyme. Mutant enzyme loses 85% of activity after 30 min at 65°C compared to 15% for the wild-type enzyme Escherichia coli
C214E 75% of the in vivo produced mutant polypeptide is soluble compared to 90% for the wild-type enzyme. Mutant enzyme loses 84% of activity after 30 min at 65°C compared to 15% for the wild-type enzyme Escherichia coli
C214F/G219S 95% of the in vivo produced mutant polypeptide is soluble compared to 90% for the wild-type enzyme. Mutant enzyme loses 81% of activity after 30 min at 65°C compared to 15% for the wild-type enzyme Escherichia coli
C214G 80% of the in vivo produced mutant polypeptide is soluble compared to 90% for the wild-type enzyme. Mutant enzyme loses 44% of activity after 30 min at 65°C compared to 15% for the wild-type enzyme Escherichia coli
C214L 100% of the in vivo produced mutant polypeptide is soluble compared to 90% for the wild-type enzyme. Mutant enzyme loses 33% of activity after 30 min at 65°C compared to 15% for the wild-type enzyme Escherichia coli
C214P 95% of the in vivo produced mutant polypeptide is soluble compared to 90% for the wild-type enzyme. Mutant enzyme loses 88% of activity after 30 min at 65°C compared to 15% for the wild-type enzyme Escherichia coli
C214Q 95% of the in vivo produced mutant polypeptide is soluble compared to 90% for the wild-type enzyme. Mutant enzyme loses 73% of activity after 30 min at 65°C compared to 15% for the wild-type enzyme Escherichia coli
C214R 55% of the in vivo produced mutant polypeptide is soluble compared to 90% for the wild-type enzyme. Mutant enzyme loses 84% of activity after 30 min at 65°C compared to 15% for the wild-type enzyme Escherichia coli
C214S 95% of the in vivo produced mutant polypeptide is soluble compared to 90% for the wild-type enzyme. Mutant enzyme loses 32% of activity after 30 min at 65°C compared to 15% for the wild-type enzyme Escherichia coli
C214T 90% of the in vivo produced mutant polypeptide is soluble compared to 90% for the wild-type enzyme. Mutant enzyme loses 59% of activity after 30 min at 65°C compared to 15% for the wild-type enzyme Escherichia coli
C214V 95% of the in vivo produced mutant polypeptide is soluble compared to 90% for the wild-type enzyme. Mutant enzyme loses 45% of activity after 30 min at 65°C compared to 15% for the wild-type enzyme Escherichia coli
C214W 50% of the in vivo produced mutant polypeptide is soluble compared to 90% for the wild-type enzyme. Mutant enzyme loses 70% of activity after 30 min at 65 C compared to 15% for the wild-type enzyme Escherichia coli
C214Y 90% of the in vivo produced mutant polypeptide is soluble compared to 90% for the wild-type enzyme. Mutant enzyme loses 81% of activity after 30 min at 65°C compared to 15% for the wild-type enzyme Escherichia coli
additional information in soluble CATI(1-211)(X3) mutants nearly all amino acid residues are tolerated at position 212 and 213. This reflects the relative lack of impotance of these residues in the folding and/or stabilization of CAT. Substitutions at position 214 do not dramatically alter the biological activity of wild-type CATI Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
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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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