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Literature summary for 4.1.3.42 extracted from

  • Grady, S.R.; Wang, J.K.; Dekker, E.E.
    Steady-state kinetics and inhibition studies of the aldol condensation reaction catalized by bovine liver and Escherichia coli 2-keto-4-hydroxyglutarate aldolase (1981), Biochemistry, 20, 2497-2502.
    View publication on PubMed

Inhibitors

Inhibitors Comment Organism Structure
2-Ketoglutarate
-
Escherichia coli
acetaldehyde Ki: 11 mM Escherichia coli
chloride 41% inhibition at 40 mM Escherichia coli
citrate Ki: 7.5 mM Escherichia coli
glyoxylate bovine enzyme inhibited at lower concentrations than E. coli enzyme Escherichia coli
Halides
-
Escherichia coli
Hydroxypyruvate Ki: 0.0125 mM Escherichia coli
additional information
-
Escherichia coli
NaBr 48% inhibition at 20 mM Escherichia coli
NaCl 38% inhibition at 20 mM Escherichia coli
NaF 19% inhibition at 20 mM Escherichia coli
NaI 59% inhibition at 20 mM Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information
-
Escherichia coli
14.3
-
glyoxylate
-
Escherichia coli
45
-
pyruvate
-
Escherichia coli

Metals/Ions

Metals/Ions Comment Organism Structure
additional information no requirement Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information mechanism Escherichia coli ?
-
?

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
0.0125
-
Hydroxypyruvate
-
Escherichia coli
7.5
-
citrate
-
Escherichia coli