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Literature summary for 1.5.1.54 extracted from

  • Zuo, C.; Jolly, A.L.; Nikolova, A.P.; Satzer, D.I.; Cao, S.; Sanchez, J.S.; Ballou, D.P.; Trimmer, E.E.
    A role for glutamine 183 in the folate oxidative half-reaction of methylenetetrahydrofolate reductase from Escherichia coli (2018), Arch. Biochem. Biophys., 642, 63-74 .
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
structures of the enzyme complexes of wild-type with NADH and mutant E28Q with methytetrahydrofolate. Residue Gln183 makes key hydrogen-bonding interactions with both NADH and folate in their respective halfreactions Escherichia coli

Protein Variants

Protein Variants Comment Organism
Q183A in the reductive half-reaction, NADH binding affinity and the rate of flavin reduction are not hindered by the mutation. Q183A exhibits a 6-10fold lower rate of folate reduction and binds methylentetrahydrofolate with 7-fold lower affinity Escherichia coli
Q183E in the reductive half-reaction, NADH binding affinity and the rate of flavin reduction are not hindered by the mutation and Gln183 plays a minor in the oxidative half-reaction. The mutant displays catalytic constants within 3fold of the wild-type enzyme Escherichia coli

Inhibitors

Inhibitors Comment Organism Structure
5,10-methylenetetrahydrofolate substrate inhibition Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.0004
-
5,10-methylenetetrahydrofolate wild-type, pH 7.2, 4┬░C Escherichia coli
0.0035
-
NADH wild-type, pH 7.2, 4┬░C Escherichia coli
0.0066
-
NADH mutant Q183E, pH 7.2, 4┬░C Escherichia coli
0.01
-
NADH mutant Q183A, pH 7.2, 4┬░C Escherichia coli
0.104
-
5,10-methylenetetrahydrofolate mutant Q183A, pH 7.2, 4┬░C Escherichia coli
0.108
-
5,10-methylenetetrahydrofolate mutant Q183E, pH 7.2, 4┬░C Escherichia coli

Organism

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

Substrates and Products (Substrate)

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

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.29
-
NADH mutant Q183A, pH 7.2, 4┬░C Escherichia coli
2.2
-
NADH wild-type, pH 7.2, 4┬░C Escherichia coli
2.7
-
NADH mutant Q183E, pH 7.2, 4┬░C Escherichia coli

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
0.061
-
5,10-methylenetetrahydrofolate wild-type, pH 7.2, 4┬░C Escherichia coli
0.094
-
5,10-methylenetetrahydrofolate mutant Q183E, pH 7.2, 4┬░C Escherichia coli