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Literature summary 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)

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

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.5.1.54 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]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.5.1.54 0.175
-
 NADH pH 7.2, 37°C Escherichia coli
1.5.1.54 0.24
-
 NADH presence of 0.05 mM genistein, pH 7.2, 37°C Escherichia coli
1.5.1.54 0.25
-
 NADH presence of 0.1 mM genistein, pH 7.2, 37°C Escherichia coli

Organism

EC Number Organism UniProt Comment Textmining
1.5.1.54 Escherichia coli P0AEZ1 cf. EC 1.5.1.20
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.5.1.54 5,10-methylenetetrahydrofolate + NADH + H+
-
 Escherichia coli 5-methyltetrahydrofolate + NAD+
-
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