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Literature summary for 2.3.3.16 extracted from

  • Duckworth, H.W.; Nguyen, N.T.; Gao, Y.; Donald, L.J.; Maurus, R.; Ayed, A.; Bruneau, B.; Brayer, G.D.
    Enzyme-substrate complexes of allosteric citrate synthase: evidence for a novel intermediate in substrate binding (2013), Biochim. Biophys. Acta, 1834, 2546-2553.
    View publication on PubMed

Protein Variants

Protein Variants Comment Organism
G181E the mutant shows reduced activity compared to the wild type enzyme and is not inhibited by NADH Escherichia coli
R306L inactive Escherichia coli
T204R the mutant shows reduced activity compared to the wild type enzyme and is not inhibited by NADH Escherichia coli

Inhibitors

Inhibitors Comment Organism Structure
NADH about 95% inhibition at 0.1 mM Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.0105
-
oxaloacetate mutant enzyme G181E, pH and temperature not specified in the publication Escherichia coli
0.011
-
oxaloacetate wild type enzyme, pH and temperature not specified in the publication Escherichia coli
0.69
-
acetyl-CoA mutant enzyme G181E, pH and temperature not specified in the publication Escherichia coli
0.75
-
acetyl-CoA wild type enzyme, pH and temperature not specified in the publication Escherichia coli
1.01
-
acetyl-CoA mutant enzyme T204R, pH and temperature not specified in the publication Escherichia coli

Metals/Ions

Metals/Ions Comment Organism Structure
K+ activates Escherichia coli

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
47885
-
6 * 47885, calculated from amino acid sequence Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
acetyl-CoA + H2O + oxaloacetate Escherichia coli
-
citrate + CoA
-
?

Organism

Organism UniProt Comment Textmining
Escherichia coli P0ABH7
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
acetyl-CoA + H2O + oxaloacetate
-
Escherichia coli citrate + CoA
-
?

Subunits

Subunits Comment Organism
homohexamer 6 * 47885, calculated from amino acid sequence Escherichia coli

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
17
-
acetyl-CoA mutant enzyme T204R, pH and temperature not specified in the publication Escherichia coli
18
-
acetyl-CoA mutant enzyme G181E, pH and temperature not specified in the publication Escherichia coli
44
-
acetyl-CoA wild type enzyme, pH and temperature not specified in the publication Escherichia coli