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Literature summary for 2.3.1.28 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
Search for more literature for 2.3.1.28

Cloned(Commentary)

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

Protein Variants

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

KM Value [mM]

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

Organism

Organism UniProt Comment Textmining
Bacillus pumilus
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Bacillus pumilus

Specific Activity [micromol/min/mg]

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

Substrates and Products (Substrate)

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

Synonyms

Synonyms Comment Organism
cat-86
-
 Bacillus pumilus

Temperature Stability [°C]

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