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Literature summary extracted from

  • Woldegiorgis, G.; Fibich, B.; Contreras, L.; Shrago, E.
    Restoration of malonyl-CoA sensitivity of soluble rat liver mitochondria carnitine palmitoyltransferase by reconstitution with a partially purified malonyl-CoA binding protein (1992), Arch. Biochem. Biophys., 295, 348-351.
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.3.1.21 malonyl-CoA mitochondrial isozyme CPT I, sensitivity against malonyl-CoA is mediated by a 86 kDa malonyl-CoA binding protein complexed with CPT and other proteins of the beta-oxidation, detergent and salt sensitive; regulatory role in vivo 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
-
 CoA + L-acylcarnitine
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.3.1.21 Rattus norvegicus
-
 enzyme form CPT I
-

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
-
 ?

Subunits

EC Number Subunits Comment Organism
2.3.1.21 More rat liver mitochondria carnitine palmitoyltransferase may be composed of an easily dissociable catalytic unit and a malonyl-CoA sensitivity conferring regulatory component Rattus norvegicus