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Literature summary for 2.3.3.16 extracted from

  • Nguyen, N.T.; Maurus, R.; Stokell, D.J.; Ayed, A.; Duckworth, H.W.; Brayer, G.D.
    Comparative analysis of folding and substrate binding sites between regulated hexameric type II citrate synthases and unregulated dimeric type I enzymes (2001), Biochemistry, 40, 13177-13187.
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
hanging drop vapour diffusion method, from 2-2.3 M ammonium sulfate, 2% v/v polyethylene glycol 400, 0.1 M HEPS, pH 6.0, X-ray diffraction analysis, structure determination and modeling: 3 identical dimer units arranged about a central 3-fold axis Escherichia coli

Inhibitors

Inhibitors Comment Organism Structure
additional information allosteric inhibition mechanism, structure relationship Escherichia coli
NADH allosteric; CS II, strong and specific allosteric inhibition Escherichia coli

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
additional information
-
amino acid sequence alignment Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli P0ABH7 isozyme CS II
-

Purification (Commentary)

Purification (Comment) Organism
-
Escherichia coli

Reaction

Reaction Comment Organism Reaction ID
acetyl-CoA + H2O + oxaloacetate = citrate + CoA mechanism Escherichia coli
acetyl-CoA + H2O + oxaloacetate = citrate + CoA active site Escherichia coli

Substrates and Products (Substrate)

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

Subunits

Subunits Comment Organism
More subunit organization and crystal structure, amino acid residues involved in subunit interaction Escherichia coli