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Literature summary for 2.3.1.21 extracted from

  • Murthy, M.S.R.; Ramsay, R.R.; Pande, S.V.
    Carnitine analogues and carnitine palmitoyltransferases (1990), Biochem. Soc. Trans., 18, 604-605.
    View publication on PubMed

Inhibitors

Inhibitors Comment Organism Structure
L-aminocarnitine ability to act as substrate or inhibitor of CPT is dependent on the nature of CPT and on the chain length of the acyl-CoA cosubstrate Rattus norvegicus
L-sulfocarnitine ability to act as substrate or inhibitor of CPT is dependent on the nature of CPT and on the chain length of the acyl-CoA cosubstrate Rattus norvegicus
thiolcarnitine ability to act as substrate or inhibitor of CPT is dependent on the nature of CPT and on chain length of the acyl-CoA cosubstrate Rattus norvegicus

Localization

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

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
acyl-CoA + L-carnitine Rattus norvegicus enzyme has a key function in regulation of fatty acid beta-oxidation CoA + L-acylcarnitine
-
?

Organism

Organism UniProt Comment Textmining
Rattus norvegicus
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
liver
-
Rattus norvegicus
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
acyl-CoA + L-carnitine
-
Rattus norvegicus CoA + L-acylcarnitine
-
r
acyl-CoA + L-carnitine enzyme has a key function in regulation of fatty acid beta-oxidation Rattus norvegicus CoA + L-acylcarnitine
-
?