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Literature summary for 2.3.3.16 extracted from

  • Stokell, D.J.; Donald, L.J.; Maurus, R.; Nguyen, N.T.; Sadler, G.; Choudhary, K.; Hultin, P.G.; Brayer, G.D.; Duckworth, H.W.
    Probing the roles of key residues in the unique regulatory NADH binding site of type II citrate synthase of Escherichia coli (2003), J. Biol. Chem., 278, 35435-35443.
    View publication on PubMed
Search for more literature for 2.3.3.16

Crystallization (Commentary)

Crystallization (Comment) Organism
hanging-drop vapour-diffusion method from 2.0-2.2 M ammonium sulfate, 2% PEG 400, and 0.1 M Na-HEPES at pH 6.0. the NADH-bound form of mutant R109L is obtained by soaking a variant crystal in a solution containing 1.22 mM NADH, 2.8 M ammonium sulfate, 2% polyethylene glycol 400 and 0.1 M Na-Hepes at pH 6.0 Escherichia coli

Protein Variants

Protein Variants Comment Organism
K167A extremely weak inhibition by NADH. Does not form hexamers in response to NADH, unlike the wild-type enzyme Escherichia coli
R109L extremely weak inhibition by NADH. Great structural change. Both regions - residue 260-311 and 316-342 - are much less mobile than in wild-type enzyme Escherichia coli
R163L extremely weak inhibition by NADH. Does not form hexamers in response to NADH, unlike the wild-type enzyme Escherichia coli

Inhibitors

Inhibitors Comment Organism Structure
NADH inhibition of wild-type enzyme. Inhibition is extremenly weak in mutant enzymes Y145A, R163L, and K167A Escherichia coli
oxaloacetate
-
 Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.003
-
 oxaloacetate mutant enzyme H110A, in presence of 0.1 M KCl Escherichia coli
0.004
-
 oxaloacetate mutant enzyme T204A, in presence of 0.1 M KCl Escherichia coli
0.005
-
 oxaloacetate mutant enzyme R163L, in presence of 0.1 M KCl Escherichia coli
0.007
-
 oxaloacetate mutant enzyme R109L, in presence of 0.1 M KCl Escherichia coli
0.01
-
 oxaloacetate mutant enzyme Q182A, in presence of 0.1 M KCl Escherichia coli
0.017
-
 oxaloacetate mutant enzyme N189A, in presence of 0.1 M KCl Escherichia coli
0.018
-
 oxaloacetate mutant enzyme T111A, in presence of 0.1 M KCl Escherichia coli
0.026
-
 oxaloacetate wild-type enzyme, in presence of 0.1 M KCl Escherichia coli
0.037
-
 oxaloacetate mutant enzyme K167A, in presence of 0.1 M KCl Escherichia coli
0.049
-
 acetyl-CoA mutant enzyme H110A, in presence of 0.1 M KCl Escherichia coli
0.051
-
 oxaloacetate mutant enzyme Y145A, in presence of 0.1 M KCl Escherichia coli
0.056
-
 acetyl-CoA mutant enzyme Q182A, in presence of 0.1 M KCl Escherichia coli
0.069
-
 acetyl-CoA mutant enzyme N189A, in presence of 0.1 M KCl Escherichia coli
0.069
-
 acetyl-CoA mutant enzyme R109L, in presence of 0.1 M KCl Escherichia coli
0.079
-
 acetyl-CoA mutant enzyme T111A, in presence of 0.1 M KCl Escherichia coli
0.08
-
 acetyl-CoA mutant enzyme R163L, in presence of 0.1 M KCl Escherichia coli
0.12
-
 acetyl-CoA wild-type enzyme, in presence of 0.1 M KCl Escherichia coli
0.21
-
 acetyl-CoA mutant enzyme T204A, in presence of 0.1 M KCl Escherichia coli
0.22
-
 acetyl-CoA mutant enzyme K167A, in presence of 0.1 M KCl Escherichia coli
0.23
-
 acetyl-CoA mutant enzyme Y145A, in presence of 0.1 M KCl Escherichia coli

Organism

Organism UniProt Comment Textmining
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
hexamer
-
 Escherichia coli

Synonyms

Synonyms Comment Organism
type II citrate synthase
-
 Escherichia coli

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
3 6 acetyl-CoA mutant enzyme Y145A, in presence of 0.1 M KCl Escherichia coli
3 6 oxaloacetate mutant enzyme Y145A, in presence of 0.1 M KCl Escherichia coli
54
-
 acetyl-CoA mutant enzyme T111A, in presence of 0.1 M KCl Escherichia coli
54
-
 oxaloacetate mutant enzyme T111A, in presence of 0.1 M KCl Escherichia coli
67
-
 acetyl-CoA mutant enzyme H110A, in presence of 0.1 M KCl Escherichia coli
67
-
 oxaloacetate mutant enzyme H110A, in presence of 0.1 M KCl Escherichia coli
81
-
 acetyl-CoA wild-type enzyme, in presence of 0.1 M KCl Escherichia coli
81
-
 oxaloacetate wild-type enzyme, in presence of 0.1 M KCl Escherichia coli
84
-
 acetyl-CoA mutant enzyme K167A, in presence of 0.1 M KCl Escherichia coli
84
-
 oxaloacetate mutant enzyme K167A, in presence of 0.1 M KCl Escherichia coli
95
-
 acetyl-CoA mutant enzyme Q182A, in presence of 0.1 M KCl Escherichia coli
95
-
 oxaloacetate mutant enzyme Q182A, in presence of 0.1 M KCl Escherichia coli
108
-
 acetyl-CoA mutant enzyme R163L, in presence of 0.1 M KCl Escherichia coli
108
-
 oxaloacetate mutant enzyme R163L, in presence of 0.1 M KCl Escherichia coli
118
-
 acetyl-CoA mutant enzyme T204A, in presence of 0.1 M KCl Escherichia coli
118
-
 oxaloacetate mutant enzyme T204A, in presence of 0.1 M KCl Escherichia coli
121
-
 acetyl-CoA mutant enzyme R109L, in presence of 0.1 M KCl Escherichia coli
121
-
 oxaloacetate mutant enzyme R109L, in presence of 0.1 M KCl Escherichia coli
124
-
 acetyl-CoA mutant enzyme N189A, in presence of 0.1 M KCl Escherichia coli
124
-
 oxaloacetate mutant enzyme N189A, in presence of 0.1 M KCl Escherichia coli

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
0.0017
-
 NADH mutant enzyme R109L Escherichia coli
0.0028
-
 NADH wild-type enzyme Escherichia coli
0.003
-
 oxaloacetate mutant enzyme H110A, in presence of 0.1 M KCl Escherichia coli
0.004
-
 oxaloacetate mutant enzyme T204A, in presence of 0.1 M KCl Escherichia coli
0.005
-
 oxaloacetate mutant enzyme R163L, in presence of 0.1 M KCl Escherichia coli
0.007
-
 oxaloacetate mutant enzyme R109L, in presence of 0.1 M KCl Escherichia coli
0.01
-
 oxaloacetate mutant enzyme Q182A, in presence of 0.1 M KCl Escherichia coli
0.017
-
 oxaloacetate mutant enzyme N189A, in presence of 0.1 M KCl Escherichia coli
0.018
-
 NADH mutant enzyme Q182A Escherichia coli
0.018
-
 oxaloacetate mutant enzyme T111A, in presence of 0.1 M KCl Escherichia coli
0.026
-
 oxaloacetate wild-type enzyme, in presence of 0.1 M KCl Escherichia coli
0.037
-
 oxaloacetate mutant enzyme K167A, in presence of 0.1 M KCl Escherichia coli
0.051
-
 oxaloacetate mutant enzyme Y145A, in presence of 0.1 M KCl Escherichia coli
0.08
-
 NADH mutant enzyme T111A Escherichia coli
0.121
-
 NADH mutant enzyme H110A Escherichia coli
0.165
-
 NADH mutant enzyme T204A Escherichia coli
0.242
-
 NADH mutant enzyme N189A Escherichia coli
0.4
-
 NADH mutant enzyme R163L Escherichia coli
0.63
-
 NADH mutant enzyme K167A Escherichia coli
0.79
-
 NADH mutant enzyme Y145A Escherichia coli