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Literature summary for 2.3.1.137 extracted from

  • Cronin, C.N.
    The conserved serine-threonine-serine motif of the carnitine acyltransferases is involved in carnitine binding and transition-state stabilization: a site-directed mutagenesis study (1997), Biochem. Biophys. Res. Commun., 238, 784-789.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
cloned and expressed in Escherichia coli Bos taurus

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.000206
-
decanoyl-CoA mutant AAA-COT Bos taurus
0.00138
-
decanoyl-CoA purified enzyme, wild-type COT Bos taurus
0.00139
-
decanoyl-CoA mutant ATS-COT Bos taurus
0.00588
-
decanoyl-CoA mutant AAS-COT Bos taurus
0.00762
-
decanoyl-CoA mutant SAS-COT Bos taurus
0.0513
-
decanoyl-CoA mutant STA-COT Bos taurus
0.0819
-
decanoyl-CoA wild-type COT Bos taurus
0.0948
-
L-carnitine mutant ATS-COT Bos taurus
0.303
-
decanoyl-CoA mutant SAA-COT Bos taurus
0.373
-
decanoyl-CoA mutant ATA-COT Bos taurus
0.6
-
palmitoyl-CoA mutant SAA-COT Bos taurus
0.794
-
decanoyl-CoA mutant AAA-COT Bos taurus
0.992
-
L-carnitine mutant AAS-COT Bos taurus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
acyl-CoA + L-carnitine Bos taurus central role in fatty acid metabolism acyl-L-carnitine + CoA
-
r
acyl-L-carnitine + CoA Bos taurus
-
acyl-CoA + L-carnitine
-
r

Organism

Organism UniProt Comment Textmining
Bos taurus O19094 bovine
-

Purification (Commentary)

Purification (Comment) Organism
recombinant enzyme Bos taurus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
acyl-CoA + L-carnitine
-
Bos taurus acyl-L-carnitine + CoA
-
r
acyl-CoA + L-carnitine central role in fatty acid metabolism Bos taurus acyl-L-carnitine + CoA
-
r
acyl-L-carnitine + CoA
-
Bos taurus acyl-CoA + L-carnitine
-
r
octanoyl-CoA + L-carnitine
-
Bos taurus CoA + L-octanoylcarnitine
-
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