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Literature summary for 2.3.1.137 extracted from

  • Jogl, G.; Hsiao, Y.S.; Tong, L.
    Crystal structure of mouse carnitine octanoyltransferase and molecular determinants of substrate selectivity (2005), J. Biol. Chem., 280, 738-744.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
overexpression of the His-tagged enzyme in Escherichia coli as soluble protein, expression of enzyme for selenomethionine-labeling in Escherichia coli strain B834(DE3) Mus musculus

Crystallization (Commentary)

Crystallization (Comment) Organism
purified recombinant His-tagged wild-type and mutants M335V and C323M enzymes free or in complex with octanoylcarnitine, sitting drop vapour diffusion method, 4°C, reservoir solution contains 0.1 M HEPES, pH 7.4, 62% v/v 2-methyl-2,4-pentanediol, larger crystals by micro- and macroseeding, cross-seeding of recombinant purified selenomethionine-labeled enzyme, X-ray diffraction structure determination and analysis at 2.0-2.2 A resolution Mus musculus

Protein Variants

Protein Variants Comment Organism
C323M site-directed mutagenesis, crystal structure comparison with the wild-type enzyme, altered acyl-CoA substrate specificity compared to the wild-type enzyme, highly increased specificity for octanoyl-CoA Mus musculus
G553M site-directed mutagenesis, highly reduced activity with altered acyl-CoA substrate specificity compared to the wild-type enzyme Mus musculus
M335A site-directed mutagenesis, reduced activity with altered acyl-CoA substrate specificity compared to the wild-type enzyme Mus musculus
M335V site-directed mutagenesis, crystal structure comparison with the wild-type enzyme, highly reduced activity with altered acyl-CoA substrate specificity compared to the wild-type enzyme Mus musculus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
octanoyl-CoA + L-carnitine Mus musculus
-
CoA + L-octanoylcarnitine
-
r

Organism

Organism UniProt Comment Textmining
Mus musculus Q9DC50
-
-

Purification (Commentary)

Purification (Comment) Organism
soluble recombinant His-tagged wild-type and selenomethionine-labeled enzyme from Escherichia coli by nickel affinity chromatography Mus musculus

Reaction

Reaction Comment Organism Reaction ID
octanoyl-CoA + L-carnitine = CoA + L-octanoylcarnitine acyl-binding hydrophobic pocket structure involving residues G553, C323, and Met335, the acyl-CoA substrate chain length specificity is determined by G553, Met335 is important for catalysis Mus musculus

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
-
substrate specificity of wild-type and mutant enzymes, overview Mus musculus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
acetyl-CoA + L-carnitine low activity Mus musculus CoA + L-acetylcarnitine
-
?
octanoyl-CoA + L-carnitine
-
Mus musculus CoA + L-octanoylcarnitine
-
r
octanoyl-CoA + L-carnitine preferred substrate Mus musculus CoA + L-octanoylcarnitine
-
r
tetradecanoyl-CoA + L-carnitine low activity Mus musculus CoA + L-tetradecanoylcarnitine
-
?

Synonyms

Synonyms Comment Organism
carnitine octanoyltransferase
-
Mus musculus
CrOT
-
Mus musculus
More the enzyme belongs to the carnitine acyltransferase family Mus musculus