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Literature summary for 2.3.1.21 extracted from

  • Kerner, J.; Distler, A.M.; Minkler, P.; Parland, W.; Peterman, S.M.; Hoppel, C.L.
    Phosphorylation of rat liver mitochondrial carnitine palmitoyltransferase-I: effect on the kinetic properties of the enzyme (2004), J. Biol. Chem., 279, 41104-41113.
    View publication on PubMed

Inhibitors

Inhibitors Comment Organism Structure
malonyl-CoA phosphorylation of the CKII site in the C-terminal end of CPT-I leads to decreased malonyl-CoA sensitivity Rattus norvegicus

Localization

Localization Comment Organism GeneOntology No. Textmining
mitochondrial outer membrane
-
Rattus norvegicus 5741
-
mitochondrion outer membrane Rattus norvegicus 5739
-

Organism

Organism UniProt Comment Textmining
Rattus norvegicus P32198
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
phosphoprotein phosphoralytion of hepatic CPT-I is a mechanism for control of fatty acid oxidation. Phosphorylation of the CKII site in the C-terminal end of CPT-I leads to decreased malonyl-CoA sensitivity and increased catalytic activity Rattus norvegicus

Source Tissue

Source Tissue Comment Organism Textmining
liver
-
Rattus norvegicus
-

Synonyms

Synonyms Comment Organism
carnitine palmitoyltransferase-I
-
Rattus norvegicus
CPT-IL
-
Rattus norvegicus