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Literature summary extracted from

  • Chirakkal, H.; Ford, G.C.; Moir, A.
    Analysis of a conserved hydrophobic pocket important for the thermostability of Bacillus pumilus chloramphenicol acetyltransferase (CAT-86) (2001), Protein Eng., 14, 161-166.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.3.1.28 cloning of mutant cat-86 in pTB361 and transformation of Escherichia coli JM109 Bacillus pumilus

Protein Variants

EC Number Protein Variants Comment Organism
2.3.1.28 A203G mutant enzyme is less stable than wild-type enzyme Bacillus pumilus
2.3.1.28 A203I mutant enzyme is more thermostable than wild-type Bacillus pumilus
2.3.1.28 I191V mutant enzyme is less stable than wild-type enzyme Bacillus pumilus
2.3.1.28 Y33F/A203V mutant enzyme is more thermostable than wild-type Bacillus pumilus

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.3.1.28 0.025
-
chloramphenicol wild-type enzyme Bacillus pumilus
2.3.1.28 0.028
-
acetyl-CoA wild-type enzyme Bacillus pumilus

Organism

EC Number Organism UniProt Comment Textmining
2.3.1.28 Bacillus pumilus
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.3.1.28
-
Bacillus pumilus

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
2.3.1.28 330
-
-
Bacillus pumilus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.3.1.28 acetyl-CoA + chloramphenicol
-
Bacillus pumilus CoA + chloramphenicol 3-acetate
-
?

Synonyms

EC Number Synonyms Comment Organism
2.3.1.28 cat-86
-
Bacillus pumilus

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
2.3.1.28 55
-
30 min, 82% loss of activity, wild-type enzyme Bacillus pumilus