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Literature summary for 2.3.1.137 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
Search for more literature for 2.3.1.137

Cloned(Commentary)

Cloned (Comment) Organism
expression of wild-type and G553M mutant enzymes in an enzyme-deficient Saccharomyces cerevisiae strain Rattus norvegicus

Protein Variants

Protein Variants Comment Organism
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
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

Localization

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

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
69000
-
 x * 69000, recombinant enzyme, SDS-PAGE Rattus norvegicus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
octanoyl-CoA + L-carnitine Rattus norvegicus
-
 CoA + L-octanoylcarnitine
-
 ?

Organism

Organism UniProt Comment Textmining
Rattus norvegicus
-
-
-

Reaction

Reaction Comment Organism Reaction ID
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

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
-
 acyl-CoA substrate specificity of wild-type and G553M mutant enzymes, overview Rattus norvegicus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
acetyl-CoA + L-carnitine low activity Rattus norvegicus CoA + L-acetylcarnitine
-
 ?
butanoyl-CoA + L-carnitine
-
 Rattus norvegicus CoA + L-butanoylcarnitine
-
 ?
decanoyl-CoA + L-carnitine best substrate Rattus norvegicus CoA + L-decanoylcarnitine
-
 ?
dodecanoyl-CoA + L-carnitine
-
 Rattus norvegicus CoA + L-dodecanoylcarnitine
-
 ?
hexadecanoyl-CoA + L-carnitine low activity Rattus norvegicus CoA + L-hexadecanoylcarnitine
-
 ?
hexanoyl-CoA + L-carnitine best substrate Rattus norvegicus CoA + L-hexanoylcarnitine
-
 ?
additional information acyl-CoA substrate specificity is determined by Gly553 Rattus norvegicus ?
-
 ?
octanoyl-CoA + L-carnitine
-
 Rattus norvegicus CoA + L-octanoylcarnitine
-
 ?
tetradecanoyl-CoA + L-carnitine
-
 Rattus norvegicus CoA + L-tetradecanoylcarnitine
-
 ?

Subunits

Subunits Comment Organism
? x * 69000, recombinant enzyme, SDS-PAGE Rattus norvegicus
More active site structure and substrate positioning modeling for wild-type and G553M mutant enzymes Rattus norvegicus

Synonyms

Synonyms Comment Organism
carnitine octanoyltransferase
-
 Rattus norvegicus
COT
-
 Rattus norvegicus

Temperature Optimum [°C]

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

pH Optimum

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