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Literature summary for 2.3.1.21 extracted from

  • Hostetler, H.A.; Lupas, D.; Tan, Y.; Dai, J.; Kelzer, M.S.; Martin, G.G.; Woldegiorgis, G.; Kier, A.B.; Schroeder, F.
    Acyl-CoA binding proteins interact with the acyl-CoA binding domain of mitochondrial carnitine palmitoyl transferase I (2011), Mol. Cell. Biochem., 355, 135-148.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Rattus norvegicus

Protein Variants

Protein Variants Comment Organism
additional information recombinant expression of the cytoplasmic C-terminal region of liver CPTI. The C-terminal 89 residues are sufficient for high affinity binding of long chain fatty acid-CoA and direct interaction with several cytoplasmic long chain fatty acid-CoA binding proteins, leading to enhanced enzymic activity Rattus norvegicus
W391A mutation alters secondary structure, leading to decreased binding affinity for long chain fatty acid-CoA, and almost completely abolishes enzymic activity Rattus norvegicus
W452A mutation alters secondary structure, leading to decreased binding affinity for long chain fatty acid-CoA, and almost completely abolishes enzymic activity Rattus norvegicus

Localization

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

Organism

Organism UniProt Comment Textmining
Rattus norvegicus P32198 isoform CPT1a
-

Source Tissue

Source Tissue Comment Organism Textmining
liver
-
Rattus norvegicus
-

Synonyms

Synonyms Comment Organism
CPTi
-
Rattus norvegicus