Literature summary for 2.3.1.137 extracted from

Morillas, M.; Gomez-Puertas, P.; Rubi, B.; Clotet, J.; Arino, J.; Valencia, A.; Hegardt, F.G.; Serra, D.; Asins, G.
Structural model of a malonyl-CoA-binding site of carnitine octanoyltransferase and carnitine palmitoyltransferase I. Mutational analysis of a malonyl-CoA affinity domain (2002), J. Biol. Chem., 277, 11473-11480.

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KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
0.002	-	decanoyl-CoA	recombinant enzyme expressed in Saccharomyces cerevisiae pYESCOTwt	Rattus norvegicus
0.0107	-	decanoyl-CoA	-	Rattus norvegicus
0.106	-	L-carnitine	mutant A332G	Rattus norvegicus
0.172	-	L-carnitine	recombinant enzyme expressed in Saccharomyces cerevisiae pYESCOTwt	Rattus norvegicus

Natural Substrates/ Products (Substrates)

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

Organism

Organism	UniProt	Comment	Textmining
Rattus norvegicus	P11466	rat	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
acyl-CoA + L-carnitine	-	Rattus norvegicus	acyl-L-carnitine + CoA	-	r

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Release 2023.1 (January 2023)