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Literature summary 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

EC Number Inhibitors Comment Organism Structure
2.3.1.21 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
2.3.1.21 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
2.3.1.21 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

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

Natural Substrates/ Products (Substrates)

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

Organism

EC Number Organism UniProt Comment Textmining
2.3.1.21 Rattus norvegicus
-
-
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining
2.3.1.21 liver
-
 Rattus norvegicus
-

Substrates and Products (Substrate)

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