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Literature summary for 2.3.1.7 extracted from

  • Cordente, A.G.; Lopez-Vinas, E.; Vazquez, M.I.; Gomez-Puertas, P.; Asins, G.; Serra, D.; Hegardt, F.G.
    Mutagenesis of specific amino acids converts carnitine acetyltransferase into carnitine palmitoyltransferase (2006), Biochemistry, 45, 6133-6141.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli or Saccharomyces cerevisiae Rattus norvegicus

Protein Variants

Protein Variants Comment Organism
D356A/M564G shows 6fold higher activity toward palmitoyl-CoA than that of the single mutant M564G and a new activity toward stearoyl-CoA. Mutations convert the enzyme into a pseudo carnitine palmitoyltransferase in terms of substrate specificity Rattus norvegicus
M564G mutant enzyme shows higher activity with medium-chain acyl-CoAs than wild-type enzyme Rattus norvegicus
T465V/T467N/R518N 3fold improved catalytic efficiency toward choline (Kcat/Km) compared with that of the wild-type enzyme Rattus norvegicus

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.0072
-
palmitoyl-CoA mutant enzyme D356A/M564G Rattus norvegicus
0.023
-
acetyl-CoA mutant enzyme D356A/M564G Rattus norvegicus
0.101
-
carnitine wild-type enzyme Rattus norvegicus
18.1
-
choline mutant enzyme A106M/T465V/T467N/R518N Rattus norvegicus
29
-
choline mutant enzyme T465V/T467N/R518N Rattus norvegicus
86.4
-
choline wild-type enzyme Rattus norvegicus
260
-
carnitine mutant enzyme T465V/T467N/R518N Rattus norvegicus
300
-
carnitine above, mutant enzyme A106M/T465V/T467N/R518N Rattus norvegicus

Organism

Organism UniProt Comment Textmining
Rattus norvegicus
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Rattus norvegicus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
acetyl-CoA + carnitine
-
Rattus norvegicus CoA + O-acetylcarnitine
-
?
acetyl-CoA + choline low activity with wild-type enzyme. Mutant enzymes T465V/T467N/R518N and A106M/T465V/T467N/R518N show improved catalytic efficiency toward choline (Kcat/Km) compared with that of the wild type enzyme Rattus norvegicus acetylcholine + CoA
-
?
butyryl-CoA + carnitine wild-type enzyme shows maximal activity towards butyryl-CoA Rattus norvegicus CoA + O-butyrylcarnitine
-
?
decanoyl-CoA + carnitine
-
Rattus norvegicus CoA + O-decanoylcarnitine
-
?
hexanoyl-CoA + carnitine mutant enzymes M564G and D356A/M564G show maximal activity towards hexanoyl-CoA Rattus norvegicus CoA + O-hexanoylcarnitine
-
?
octanoyl-CoA + carnitine
-
Rattus norvegicus CoA + O-octanoylcarnitine
-
?
palmitoyl-CoA + carnitine wild-type enzyme shows no activity, mutant enzymes M564G and D356A/M564G show activity Rattus norvegicus CoA + O-palmitoylcarnitine
-
?

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.98
-
carnitine above, mutant enzyme A106M/T465V/T467N/R518N Rattus norvegicus
1.58
-
choline wild-type enzyme Rattus norvegicus
2.43
-
choline mutant enzyme T465V/T467N/R518N Rattus norvegicus
2.97
-
carnitine mutant enzyme T465V/T467N/R518N Rattus norvegicus
3.11
-
choline mutant enzyme A106M/T465V/T467N/R518N Rattus norvegicus
86.9
-
carnitine wild-type enzyme Rattus norvegicus