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Literature summary extracted from

  • Cordente, A.G.; Lopez-Vinas, E.; Vazquez, M.I.; Swiegers, J.H.; Pretorius, I.S.; Gomez-Puertas, P.; Hegardt, F.G.; Asins, G.; Serra, D.
    Redesign of carnitine acetyltransferase specificity by protein engineering (2004), J. Biol. Chem., 279, 33899-33908.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.3.1.7 expressed in Saccharomyces cerevisiae and Escherichia coli Rattus norvegicus
2.3.1.137 expression of wild-type and G553M mutant enzymes in an enzyme-deficient Saccharomyces cerevisiae strain Rattus norvegicus

Protein Variants

EC Number Protein Variants Comment Organism
2.3.1.7 E347A complete loss of activity Rattus norvegicus
2.3.1.7 H343A complete loss of activity Rattus norvegicus
2.3.1.7 M564A lowered activity with acetyl-CoA, increased activity with longer chain acyl-CoAs Rattus norvegicus
2.3.1.7 M564G lowered activity with acetyl-CoA, increased activity with longer chain acyl-CoAs, 1250-fold increase in activity with myristoyl-CoA Rattus norvegicus
2.3.1.137 G553M site-directed mutagenesis, the mutant enzyme shows altered substrate specificity: highly reduced activity with medium- and long-chain acyl-CoAs and increased activity with acetyl-CoA and butanoyl-CoA compared to the wild-type enzyme Rattus norvegicus
2.3.1.137 additional information the carnitine acetyl-transferase, specific for acetyl-CoA/short-chain acyl-CoAs, can be modified to an enzyme with elevated carnitine octanoyltransferase activity by mutation of Met564 to Gly, overview Rattus norvegicus

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.3.1.7 0.011
-
 octanoyl-CoA M564G mutant enzyme from yeast, pH 7.8, 30°C Rattus norvegicus
2.3.1.7 0.015
-
 butyryl-CoA M564G mutant enzyme from yeast, pH 7.8, 30°C Rattus norvegicus
2.3.1.7 0.022
-
 hexanoyl-CoA M564G mutant enzyme from yeast, pH 7.8, 30°C Rattus norvegicus
2.3.1.7 0.023
-
 acetyl-CoA recombinant enzyme from yeast, pH 7.8, 30°C Rattus norvegicus
2.3.1.7 0.025
-
 octanoyl-CoA recombinant enzyme from yeast, pH 7.8, 30°C Rattus norvegicus
2.3.1.7 0.03
-
 butyryl-CoA recombinant enzyme from yeast, pH 7.8, 30°C Rattus norvegicus
2.3.1.7 0.032
-
 acetyl-CoA M564G mutant enzyme from yeast, pH 7.8, 30°C Rattus norvegicus
2.3.1.7 0.033
-
 hexanoyl-CoA recombinant enzyme from yeast, pH 7.8, 30°C Rattus norvegicus
2.3.1.7 0.086
-
 carnitine M564G mutant enzyme from yeast with octanoyl-CoA as second substrate, pH 7.8, 30°C Rattus norvegicus
2.3.1.7 0.164
-
 carnitine M564G mutant enzyme from yeast with hexanoyl-CoA as second substrate, pH 7.8, 30°C Rattus norvegicus
2.3.1.7 0.17
-
 carnitine M564G mutant enzyme from yeast with butyryl-CoA as second substrate, pH 7.8, 30°C Rattus norvegicus
2.3.1.7 0.203
-
 carnitine recombinant enzyme from yeast with acetyl-CoA as second substrate, pH 7.8, 30°C Rattus norvegicus
2.3.1.7 0.22
-
 carnitine recombinant enzyme from yeast with butyryl-CoA as second substrate, pH 7.8, 30°C Rattus norvegicus
2.3.1.7 0.339
-
 carnitine M564G mutant enzyme from yeast with acetyl-CoA as second substrate, pH 7.8, 30°C Rattus norvegicus
2.3.1.7 0.567
-
 carnitine recombinant enzyme from yeast with hexanoyl-CoA as second substrate, pH 7.8, 30°C Rattus norvegicus
2.3.1.7 0.964
-
 carnitine recombinant enzyme from yeast with octanoyl-CoA as second substrate, pH 7.8, 30°C Rattus norvegicus

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
2.3.1.137 mitochondrion
-
 Rattus norvegicus 5739
-
2.3.1.137 peroxisome
-
 Rattus norvegicus 5777
-

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
2.3.1.7 70800
-
 x * 70800, deduced from amino acid sequence Rattus norvegicus
2.3.1.137 69000
-
 x * 69000, recombinant enzyme, SDS-PAGE Rattus norvegicus

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.3.1.7 acetyl-CoA + carnitine Rattus norvegicus modulates acetyl-CoA and CoA availability for a wide range of acyl-transfer reactions, involved in fatty acid metabolism CoA + O-acetylcarnitine
-
 r
2.3.1.137 octanoyl-CoA + L-carnitine Rattus norvegicus
-
 CoA + L-octanoylcarnitine
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.3.1.7 Rattus norvegicus Q704S8
-
-
2.3.1.137 Rattus norvegicus
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.3.1.7 purification of GST-fusion proteins from Escherichia coli Rattus norvegicus

Reaction

EC Number Reaction Comment Organism Reaction ID
2.3.1.137 octanoyl-CoA + L-carnitine = CoA + L-octanoylcarnitine acyl-CoA substrate specificity is determined by Gly553, active site structure and substrate positioning modeling Rattus norvegicus
a

Source Tissue

EC Number Source Tissue Comment Organism Textmining
2.3.1.7 testis
-
 Rattus norvegicus
-

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
2.3.1.137 additional information
-
 acyl-CoA substrate specificity of wild-type and G553M mutant enzymes, overview 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
-
 r
2.3.1.7 acetyl-CoA + carnitine modulates acetyl-CoA and CoA availability for a wide range of acyl-transfer reactions, involved in fatty acid metabolism Rattus norvegicus CoA + O-acetylcarnitine
-
 r
2.3.1.7 butyryl-CoA + carnitine
-
 Rattus norvegicus CoA + O-butyrylcarnitine
-
 r
2.3.1.7 hexanoyl-CoA + carnitine very low activity Rattus norvegicus CoA + O-hexanoylcarnitine
-
 r
2.3.1.7 additional information wild type enzyme is almost inactive towards longer chain fatty acids, some mutations increases activity towards longer chain fatty acids Rattus norvegicus ?
-
 ?
2.3.1.7 octanoyl-CoA + carnitine very low activity Rattus norvegicus CoA + O-octanoylcarnitine
-
 r
2.3.1.137 acetyl-CoA + L-carnitine low activity Rattus norvegicus CoA + L-acetylcarnitine
-
 ?
2.3.1.137 butanoyl-CoA + L-carnitine
-
 Rattus norvegicus CoA + L-butanoylcarnitine
-
 ?
2.3.1.137 decanoyl-CoA + L-carnitine best substrate Rattus norvegicus CoA + L-decanoylcarnitine
-
 ?
2.3.1.137 dodecanoyl-CoA + L-carnitine
-
 Rattus norvegicus CoA + L-dodecanoylcarnitine
-
 ?
2.3.1.137 hexadecanoyl-CoA + L-carnitine low activity Rattus norvegicus CoA + L-hexadecanoylcarnitine
-
 ?
2.3.1.137 hexanoyl-CoA + L-carnitine best substrate Rattus norvegicus CoA + L-hexanoylcarnitine
-
 ?
2.3.1.137 additional information acyl-CoA substrate specificity is determined by Gly553 Rattus norvegicus ?
-
 ?
2.3.1.137 octanoyl-CoA + L-carnitine
-
 Rattus norvegicus CoA + L-octanoylcarnitine
-
 ?
2.3.1.137 tetradecanoyl-CoA + L-carnitine
-
 Rattus norvegicus CoA + L-tetradecanoylcarnitine
-
 ?

Subunits

EC Number Subunits Comment Organism
2.3.1.7 ? x * 70800, deduced from amino acid sequence Rattus norvegicus
2.3.1.137 ? x * 69000, recombinant enzyme, SDS-PAGE Rattus norvegicus
2.3.1.137 More active site structure and substrate positioning modeling for wild-type and G553M mutant enzymes Rattus norvegicus

Synonyms

EC Number Synonyms Comment Organism
2.3.1.137 carnitine octanoyltransferase
-
 Rattus norvegicus
2.3.1.137 COT
-
 Rattus norvegicus

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.3.1.137 30
-
 assay at Rattus norvegicus

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.3.1.137 7.8
-
 assay at Rattus norvegicus