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Literature summary for 2.3.1.21 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
Search for more literature for 2.3.1.21

Inhibitors

Inhibitors Comment Organism Structure
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

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
-
 CoA + L-acylcarnitine
-
 ?

Organism

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

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
-
 ?

Subunits

Subunits Comment Organism
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