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Literature summary for 1.5.1.54 extracted from

  • Trimmer, E.E.; Ballou, D.P.; Ludwig, M.L.; Matthews, R.G.
    Folate activation and catalysis in methylenetetrahydrofolate reductase from Escherichia coli roles for aspartate 120 and glutamate 28 (2001), Biochemistry, 40, 6216-6226 .
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
modeling of the methyltetrahydrofolate product into the enzyme active site and shows 150fold decreased activity Escherichia coli

Protein Variants

Protein Variants Comment Organism
D120N mutant is reduced by NADH 30% more rapidly than the wild-type enzyme Escherichia coli
E28Q mutant is unable to catalyze the reduction of 5,10-methylentetrahydrofolate and is inactive in the physiological oxidoreductase reaction. The mutant is able to bind methyltetrahydrofolate, but reduction of the FAD cofactor is not observed Escherichia coli

Inhibitors

Inhibitors Comment Organism Structure
NADH
-
Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.0005
-
5,10-methylenetetrahydrofolate wild-type, cosubstrate NADH, pH 7.2, 25┬░C Escherichia coli
0.005
-
NADH mutant D120N, pH 7.2, 25┬░C Escherichia coli
0.017
-
NADH mutant D120N, cosubstrate menadione, pH 7.2, 25┬░C Escherichia coli
0.02
-
NADH wild-type, pH 7.2, 25┬░C Escherichia coli
0.027
-
5,10-methylenetetrahydrofolate mutant D120N, cosubstrate NADH, pH 7.2, 25┬░C Escherichia coli
0.066
-
NADH wild-type, cosubstrate menadione, pH 7.2, 25┬░C Escherichia coli
0.08
-
NADH mutant E28Q, cosubstrate menadione, pH 7.2, 25┬░C Escherichia coli
0.085
-
5-methyltetrahydrofolate wild-type, cosubstrate menadione, pH 7.2, 25┬░C Escherichia coli
0.106
-
5-methyltetrahydrofolate mutant D120N, cosubstrate menadione, pH 7.2, 25┬░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+
-
?
5-methyltetrahydrofolate + menadione
-
Escherichia coli 5,10-methylenetetrahydrofolate + menadiol
-
?
NADH + H+ + menadione
-
Escherichia coli NAD+ + menadiol
-
?

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.0002
-
NADH mutant E28Q, pH 7.2, 25┬░C Escherichia coli
0.0002
-
menadione mutant E28Q, pH 7.2, 25┬░C Escherichia coli
0.0104
-
NADH wild-type, pH 7.2, 25┬░C Escherichia coli
0.057
-
NADH mutant D120N, pH 7.2, 25┬░C Escherichia coli
0.087
-
menadione mutant D120N, pH 7.2, 25┬░C Escherichia coli
0.2
-
NADH mutant E28Q, cosubstrate menadione, pH 7.2, 25┬░C Escherichia coli
3.2
-
menadione wild-type, pH 7.2, 25┬░C Escherichia coli
54
-
NADH mutant D120N, cosubstrate menadione, pH 7.2, 25┬░C Escherichia coli
55
-
NADH wild-type, cosubstrate menadione, pH 7.2, 25┬░C Escherichia coli

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
0.012
-
NADH wild-type, cosubstrate menadione, pH 7.2, 25┬░C Escherichia coli
0.04
-
NADH mutant D120N, cosubstrate menadione, pH 7.2, 25┬░C Escherichia coli