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Literature summary for 2.3.1.21 extracted from

  • Morillas, M.; Gomez-Puertas, P.; Roca, R.; Serra, D.; Asins, G.; Valencia, A.; Hegardt, F.G.
    Structural model of the catalytic core of carnitine palmitoyltransferase I and carnitine octanoyltransferase (COT). Mutation of CPT 1 histidine 473 and alanine 381 and COT alanine 238 impairs the catalytic activity (2001), J. Biol. Chem., 276, 45001-45008.
    View publication on PubMed
Search for more literature for 2.3.1.21

Cloned(Commentary)

Cloned (Comment) Organism
expression of CPT I in Saccharomyces cerevisiae Rattus norvegicus

Protein Variants

Protein Variants Comment Organism
A381D site-directed mutagenesis, activity is reduced by 86%, Km for acyl-CoA is 6-8fold increased Rattus norvegicus
D454G site-directed mutagenesis, loss of activity Rattus norvegicus
H473A site-directed mutagenesis, active site mutant, no remaining activity Rattus norvegicus
L484P site-directed mutagenesis, loss of activity Rattus norvegicus
additional information CPT I mutant with deletion of Arg395 show no activity Rattus norvegicus
P479L site-directed mutagenesis, loss of activity Rattus norvegicus
R451A site-directed mutagenesis, loss of activity Rattus norvegicus
W391A site-directed mutagenesis, loss of activity Rattus norvegicus
W452A site-directed mutagenesis, loss of activity Rattus norvegicus

Inhibitors

Inhibitors Comment Organism Structure
malonyl-CoA similar inhibition of wild-type CPT I and mutants A381D and H473A Rattus norvegicus

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.0049
-
 palmitoyl-CoA recombinant wild-type CPT I Rattus norvegicus
0.033
-
 palmitoyl-CoA mutant A381D Rattus norvegicus
0.093
-
 L-carnitine mutant A381D Rattus norvegicus
0.129
-
 L-carnitine recombinant wild-type CPT I Rattus norvegicus

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
additional information
-
 amino acid sequence, alignment Rattus norvegicus
additional information
-
 3-dimensional structural model of CPT I active site based on X-ray diffraction analysis data from similar rat enoyl-CoA hydratase 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
-
 CoA + L-acylcarnitine
-
 ?

Organism

Organism UniProt Comment Textmining
Rattus norvegicus
-
 enzyme form CPT I
-

Reaction

Reaction Comment Organism Reaction ID
palmitoyl-CoA + L-carnitine = CoA + L-palmitoylcarnitine active site three-dimensional structure model Rattus norvegicus
a

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
acyl-CoA + L-carnitine
-
 Rattus norvegicus CoA + L-acylcarnitine
-
 ?
palmitoyl-CoA + L-carnitine
-
 Rattus norvegicus CoA + L-palmitoylcarnitine
-
 ?