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Literature summary 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)

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

Protein Variants

EC Number Protein Variants Comment Organism
2.3.1.7 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
2.3.1.7 M564G mutant enzyme shows higher activity with medium-chain acyl-CoAs than wild-type enzyme Rattus norvegicus
2.3.1.7 T465V/T467N/R518N 3fold improved catalytic efficiency toward choline (Kcat/Km) compared with that of the wild-type enzyme Rattus norvegicus

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.3.1.7 0.0072
-
 palmitoyl-CoA mutant enzyme D356A/M564G Rattus norvegicus
2.3.1.7 0.023
-
 acetyl-CoA mutant enzyme D356A/M564G Rattus norvegicus
2.3.1.7 0.101
-
 carnitine wild-type enzyme Rattus norvegicus
2.3.1.7 18.1
-
 choline mutant enzyme A106M/T465V/T467N/R518N Rattus norvegicus
2.3.1.7 29
-
 choline mutant enzyme T465V/T467N/R518N Rattus norvegicus
2.3.1.7 86.4
-
 choline wild-type enzyme Rattus norvegicus
2.3.1.7 260
-
 carnitine mutant enzyme T465V/T467N/R518N Rattus norvegicus
2.3.1.7 300
-
 carnitine above, mutant enzyme A106M/T465V/T467N/R518N Rattus norvegicus

Organism

EC Number Organism UniProt Comment Textmining
2.3.1.7 Rattus norvegicus
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.3.1.7
-
 Rattus norvegicus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.3.1.7 acetyl-CoA + carnitine
-
 Rattus norvegicus CoA + O-acetylcarnitine
-
 ?
2.3.1.7 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
-
 ?
2.3.1.7 butyryl-CoA + carnitine wild-type enzyme shows maximal activity towards butyryl-CoA Rattus norvegicus CoA + O-butyrylcarnitine
-
 ?
2.3.1.7 decanoyl-CoA + carnitine
-
 Rattus norvegicus CoA + O-decanoylcarnitine
-
 ?
2.3.1.7 hexanoyl-CoA + carnitine mutant enzymes M564G and D356A/M564G show maximal activity towards hexanoyl-CoA Rattus norvegicus CoA + O-hexanoylcarnitine
-
 ?
2.3.1.7 octanoyl-CoA + carnitine
-
 Rattus norvegicus CoA + O-octanoylcarnitine
-
 ?
2.3.1.7 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]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
2.3.1.7 0.98
-
 carnitine above, mutant enzyme A106M/T465V/T467N/R518N Rattus norvegicus
2.3.1.7 1.58
-
 choline wild-type enzyme Rattus norvegicus
2.3.1.7 2.43
-
 choline mutant enzyme T465V/T467N/R518N Rattus norvegicus
2.3.1.7 2.97
-
 carnitine mutant enzyme T465V/T467N/R518N Rattus norvegicus
2.3.1.7 3.11
-
 choline mutant enzyme A106M/T465V/T467N/R518N Rattus norvegicus
2.3.1.7 86.9
-
 carnitine wild-type enzyme Rattus norvegicus