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Literature summary for 2.3.1.28 extracted from

  • Day, P.J.; Murray, I.A.; Shaw, W.V.
    Properties of hybrid active sites in oligomeric proteins: kinetic and ligand binding studies with chloramphenicol acetyltransferase trimers (1995), Biochemistry, 34, 6416-6422.
    View publication on PubMed
Search for more literature for 2.3.1.28

Protein Variants

Protein Variants Comment Organism
CATIII (F24A/Y25F/L29A) Km-value for acetyl-CoA is 0.095 mM compared to 0.093 mM for wild-type CATIII, Km-value for chloramphenicol is 0.023 mM compared to 0.012 mM for the wild-type CATIII, turnover number is 30% of the wild-type enzyme CAT III Escherichia coli
CATIII(K14E/H195A/K217A) no activity Escherichia coli
CATIII(Q92C/N146F/Y169F/I172V) Km-value for acetyl-CoA is 0.165 mM compared to 0.093 mM for wild-type CATIII, Km-value for chloramphenicol is 0.02 mM compared to 0.012 mM for the wild-type CATIII, turnover number is 60% of the wild-type enzyme CAT III Escherichia coli
K14/K217E Km-value for acetyl-CoA is 0.166 mM compared to 0.093 mM for wild-type CATIII, Km-value for chloramphenicol is 0.017 mM compared to 0.012 mM for the wild-type CATIII, turnover number is 87% of the wild-type enzyme CAT III Escherichia coli
[CATI (H195A)]2[CATIII(K14E/K217E)] hybrid trimer, Km-value for acetyl-CoA is 0.072 mM compared to 0.093 mM for wild-type CATIII, Km-value for chloramphenicol is 0.018 mM compared to 0.012 mM for the wild-type CATIII, turnover number is 14% of the wild-type enzyme CAT III Escherichia coli
[CATIII]2[CATIII(K14E/H195A/K217A)] Km-value for acetyl-CoA is 0.143 mM compared to 0.093 mM for wild-type CATIII, Km-value for chloramphenicol is 0.016 mM compared to 0.012 mM for the wild-type CATIII, turnover number is 80% of the wild-type enzyme CAT III Escherichia coli
[CATIII][CATIII(K14E/H195A/K217A)]2 Km-value for acetyl-CoA is 0.198 mM compared to 0.093 mM for wild-type CATIII, Km-value for chloramphenicol is 0.02 mM compared to 0.012 mM for the wild-type CATIII, turnover number is 82% of the wild-type enzyme CAT III Escherichia coli
[CATI][CATIII(K14E/H195A/K217E)]2 hybrid trimer, Km-value for acetyl-CoA is 0.107 mM compared to 0.093 mM for wild-type CATIII, Km-value for chloramphenicol is 0.02 mM compared to 0.012 mM for the wild-type CATIII, turnover number is 50% of the wild-type enzyme CAT III Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.011
-
 chloramphenicol enzyme variant CAT I Escherichia coli
0.012
-
 chloramphenicol enzyme variant CAT III Escherichia coli
0.055
-
 acetyl-CoA enzyme variant CAT I Escherichia coli
0.093
-
 acetyl-CoA enzyme variant CATIII Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Escherichia coli

Substrates and Products (Substrate)

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

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
additional information
-
 additional information
-
 Escherichia coli