Literature summary for 2.3.1.21 extracted from

Lopez-Vinas, E.; Bentebibel, A.; Gurunathan, C.; Morillas, M.; de Arriaga, D.; Serra, D.; Asins, G.; Hegardt, F.G.; Gomez-Puertas, P.
Definition by functional and structural analysis of two malonyl-CoA sites in carnitine palmitoyltransferase 1A (2007), J. Biol. Chem., 282, 18212-18224.

Search for more literature for 2.3.1.21

Cloned(Commentary)

Cloned (Comment)	Organism
expression of wild-type and mutant isozyme CPT1A in Saccharomyces cerevisiae	Homo sapiens

Protein Variants

Protein Variants	Comment	Organism
A478G	site-directed mutagenesis, the mutant shows decreased sensitivity to malonyl-CoA compared to the wild-type enzyme	Homo sapiens
E26K	site-directed mutagenesis, the mutant shows decreased sensitivity to malonyl-CoA compared to the wild-type enzyme	Homo sapiens
E26K/K561E	site-directed mutagenesis, the double mutant shows the same sensitivity to malonyl-CoA compared to the wild-type enzyme	Homo sapiens
K561E	site-directed mutagenesis, the mutant shows decreased sensitivity to malonyl-CoA compared to the wild-type enzyme	Homo sapiens
M593S	site-directed mutagenesis, the mutant is insensitive to malonyl-CoA	Homo sapiens
R243T	site-directed mutagenesis, the mutant shows highly decreased sensitivity to malonyl-CoA compared to the wild-type enzyme	Homo sapiens
R243T/A478G	site-directed mutagenesis, the mutant shows highly decreased sensitivity to malonyl-CoA compared to the wild-type enzyme	Homo sapiens

Inhibitors

Inhibitors	Comment	Organism	Structure
malonyl-CoA	IC50: 0.0073 mM for the recombinant wild-type isozyme CPT1A, IC50: 0.0384 mM for CPT1A mutant R243T, IC50 values of other mutants, overview, determination of two binding sites, the A site and the O site, the latter involved residue Arg243, binding structure, interactions between N- and C-terminal residues are involved in malonyl-CoA binding to the A site, isozyme CPT1A in malonyl-CoA molecular docking, overview	Homo sapiens

KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
0.007	-	palmitoyl-CoA	30°C, recombinant CPT1A mutant R243T	Homo sapiens
0.056	-	L-carnitine	30°C, recombinant CPT1A mutant R243T	Homo sapiens
0.135	-	L-carnitine	30°C, recombinant wildtype isozyme CPT1A	Homo sapiens
0.4	-	palmitoyl-CoA	30°C, recombinant wildtype isozyme CPT1A	Homo sapiens

Localization

Localization	Comment	Organism	GeneOntology No.	Textmining
mitochondrion	-	Homo sapiens	5739	-

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
palmitoyl-CoA + L-carnitine	Homo sapiens	-	CoA + L-palmitoylcarnitine	-	?

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	-	isozyme CPT1A	-

Source Tissue

Source Tissue	Comment	Organism	Textmining
liver	isozyme CPT1A	Homo sapiens	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
palmitoyl-CoA + L-carnitine	-	Homo sapiens	CoA + L-palmitoylcarnitine	-	?

Synonyms

Synonyms	Comment	Organism
carnitine palmitoyltransferase 1A	-	Homo sapiens
CPT1	-	Homo sapiens

Temperature Optimum [°C]

Temperature Optimum [°C]	Temperature Optimum Maximum [°C]	Comment	Organism
30	-	assay at	Homo sapiens

Ki Value [mM]

Ki Value [mM]	Ki Value maximum [mM]	Inhibitor	Comment	Organism	Structure
additional information	-	additional information	inhibition kinetics with malonyl-CoA	Homo sapiens

IC50 Value

IC50 Value	IC50 Value Maximum	Comment	Organism	Inhibitor	Structure
0.0073	0.0384	IC50: 0.0073 mM for the recombinant wild-type isozyme CPT1A, IC50: 0.0384 mM for CPT1A mutant R243T, IC50 values of other mutants, overview, determination of two binding sites, the A site and the O site, the latter involved residue Arg243, binding struct	Homo sapiens	malonyl-CoA

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Release 2023.1 (January 2023)