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Literature summary for extracted from

  • Grabowski, M.; Banecki, B.; Kadzinski, L.; Jakobkiewicz-Banecka, J.; Kazmierkiewicz, R.; Gabig-Ciminska, M.; Wegrzyn, G.; Wegrzyn, A.; Banecka-Majkutewicz, Z.
    Genistein inhibits activities of methylenetetrahydrofolate reductase and lactate dehydrogenase, enzymes which use NADH as a substrate (2015), Biochem. Biophys. Res. Commun., 465, 363-367 .
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
molecular docking of genistein. Gensitein may interfere with the binding site of NADH Escherichia coli


Inhibitors Comment Organism Structure
genistein 0.5 mM, almost complete inhibition. The inhibition is increased when genistein is preincubated with the enzyme and NADH Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
NADH pH 7.2, 37°C Escherichia coli
NADH presence of 0.05 mM genistein, pH 7.2, 37°C Escherichia coli
NADH presence of 0.1 mM genistein, pH 7.2, 37°C Escherichia coli


Organism UniProt Comment Textmining
Escherichia coli P0AEZ1 cf. EC

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
5,10-methylenetetrahydrofolate + NADH + H+
Escherichia coli 5-methyltetrahydrofolate + NAD+