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Literature summary for 2.3.1.7 extracted from

  • Hsiao, Y.S.; Jogl, G.; Tong, L.
    Structural and biochemical studies of the substrate selectivity of carnitine acetyltransferase (2004), J. Biol. Chem., 279, 31584-31589.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
residues 30-626 expressed as His-tag fusion protein in Escherichia coli Mus musculus

Crystallization (Commentary)

Crystallization (Comment) Organism
M564G and F565A mutant enzymes crystallized by sitting-drop vapor diffusion method Mus musculus

Protein Variants

Protein Variants Comment Organism
F565A used for crystallization, only minor effect on protein structure, increased activity with acetyl-CoA Mus musculus
M564A used for crystallization, decreased activity with acetyl-CoA and butyryl-CoA Mus musculus
M564G used for crystallization, dramatic changes in protein structure, decreased activity with acetyl-CoA and butyryl-CoA, strongly increased activity with hexanoyl-CoA Mus musculus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
acetyl-CoA + carnitine Mus musculus modulates acetyl-CoA and CoA availability for a wide range of acyl-transfer reactions, involved in fatty acid metabolism CoA + O-acetylcarnitine
-
r

Organism

Organism UniProt Comment Textmining
Mus musculus
-
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant enzyme using His-tag Mus musculus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
acetyl-CoA + carnitine
-
Mus musculus CoA + O-acetylcarnitine
-
r
acetyl-CoA + carnitine modulates acetyl-CoA and CoA availability for a wide range of acyl-transfer reactions, involved in fatty acid metabolism Mus musculus CoA + O-acetylcarnitine
-
r
butyryl-CoA + carnitine
-
Mus musculus CoA + O-butyrylcarnitine
-
r

Subunits

Subunits Comment Organism
monomer wild type and mutant enzymes Mus musculus