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Literature summary extracted from

  • Davies, M.N.; Kjalarsdottir, L.; Thompson, J.W.; Dubois, L.G.; Stevens, R.D.; Ilkayeva, O.R.; Brosnan, M.J.; Rolph, T.P.; Grimsrud, P.A.; Muoio, D.M.
    The acetyl group buffering action of carnitine acetyltransferase offsets macronutrient-induced lysine acetylation of mitochondrial proteins (2016), Cell Rep., 14, 243-254.
    View publication on PubMedView publication on EuropePMC

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.3.1.7 acyl-CoA + L-carnitine Mus musculus
-
 CoA + O-acylcarnitine
-
 r

Organism

EC Number Organism UniProt Comment Textmining
2.3.1.7 Mus musculus
-
-
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining
2.3.1.7 gastrocnemius
-
 Mus musculus
-
2.3.1.7 quadriceps
-
 Mus musculus
-
2.3.1.7 skeletal muscle
-
 Mus musculus
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.3.1.7 acyl-CoA + L-carnitine
-
 Mus musculus CoA + O-acylcarnitine
-
 r

Synonyms

EC Number Synonyms Comment Organism
2.3.1.7 carnitine acetyltransferase
-
 Mus musculus
2.3.1.7 CRAT
-
 Mus musculus

General Information

EC Number General Information Comment Organism
2.3.1.7 malfunction enzyme deficiency increases tissue acetyl-CoA levels and susceptibility to diet-induced lysine acetylation of broad-ranging mitochondrial proteins, coincident with diminished whole body glucose control Mus musculus
2.3.1.7 physiological function the enzyme plays a role in modulating the muscle acetylproteome Mus musculus