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Literature summary for 2.3.1.7 extracted from

  • Govindasamy, L.; Kukar, T.; Lian, W.; Pedersen, B.; Gu, Y.; Agbandje-McKenna, M.; Jin, S.; McKenna, R.; Wu, D.
    Structural and mutational characterization of L-carnitine binding to human carnitine acetyltransferase (2004), J. Struct. Biol., 146, 416-424.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expressed as His-tag fusion protein in Escherichia coli Homo sapiens

Crystallization (Commentary)

Crystallization (Comment) Organism
crystallized in the presence of L-carnitine by vapor diffusion method Homo sapiens

Protein Variants

Protein Variants Comment Organism
F545A increases Km for both substrates Homo sapiens
F545Y minor effects on Km for both substrates Homo sapiens
R497Q increases Km for both substrates Homo sapiens
T444A increases Km for both substrates Homo sapiens
Y431A increases Km for both substrates Homo sapiens
Y431F increases Km for both substrates Homo sapiens

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.042
-
acetyl-CoA wild type enzyme, pH 8.0 Homo sapiens
0.064
-
acetyl-CoA F545Y mutant enzyme, pH 8.0 Homo sapiens
0.087
-
acetyl-CoA Y431A mutant enzyme, pH 8.0 Homo sapiens
0.11
-
L-carnitine wild type enzyme, pH 8.0 Homo sapiens
0.12
-
acetyl-CoA R497Q mutant enzyme, pH 8.0 Homo sapiens
0.15
-
L-carnitine F545Y mutant enzyme, pH 8.0 Homo sapiens
0.178
-
acetyl-CoA F545A mutant enzyme, pH 8.0 Homo sapiens
0.188
-
acetyl-CoA T444A mutant enzyme, pH 8.0 Homo sapiens
0.498
-
acetyl-CoA Y431F mutant enzyme, pH 8.0 Homo sapiens
2
-
L-carnitine F545A mutant enzyme, pH 8.0 Homo sapiens
7.5
-
L-carnitine T444A mutant enzyme, pH 8.0 Homo sapiens
11.1
-
L-carnitine Y431A mutant enzyme, pH 8.0 Homo sapiens
25.6
-
L-carnitine R497Q mutant enzyme, pH 8.0 Homo sapiens
35.9
-
L-carnitine Y431F mutant enzyme, pH 8.0 Homo sapiens

Localization

Localization Comment Organism GeneOntology No. Textmining
endoplasmic reticulum
-
Homo sapiens 5783
-
mitochondrial matrix
-
Homo sapiens 5759
-
peroxisome
-
Homo sapiens 5777
-

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
acetyl-CoA + carnitine Homo sapiens 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
Homo sapiens P43155
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant protein using His-tag Homo sapiens

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
acetyl-CoA + carnitine
-
Homo sapiens 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 Homo sapiens CoA + O-acetylcarnitine
-
r

Subunits

Subunits Comment Organism
monomer crystal structure analysis Homo sapiens

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.78
-
acetyl-CoA Y431F mutant enzyme, pH 8.0 Homo sapiens
5.76
-
acetyl-CoA T444A mutant enzyme, pH 8.0 Homo sapiens
8.57
-
acetyl-CoA F545A mutant enzyme, pH 8.0 Homo sapiens
30.5
-
acetyl-CoA F545Y mutant enzyme, pH 8.0 Homo sapiens
38.5
-
acetyl-CoA wild type enzyme, pH 8.0 Homo sapiens
44.2
-
acetyl-CoA Y431A mutant enzyme, pH 8.0 Homo sapiens
94.8
-
acetyl-CoA R497Q mutant enzyme, pH 8.0 Homo sapiens