Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary extracted from

  • Lee, M.N.; Takawira, D.; Nikolova, A.P.; Ballou, D.P.; Furtado, V.C.; Phung, N.L.; Still, B.R.; Thorstad, M.K.; Tanner, J.J.; Trimmer, E.E.
    Functional role for the conformationally mobile phenylalanine 223 in the reaction of methylenetetrahydrofolate reductase from Escherichia coli (2009), Biochemistry, 48, 7673-7685.
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.5.1.20 ligand-free mutant F223L and mutant F223L/E28Q in complex with methylenetetrahydrofolate, to 1.65 and 1.7 A resolution, respectively. folate is bound in a catalytically competent conformation, and L223 undergoes a conformational change similar to that observed for F223 in the E28Q-methylenetetrahydrofolate structure Escherichia coli

Protein Variants

EC Number Protein Variants Comment Organism
1.5.1.20 F223A mutation impairs both NADH and methylenetetrahydrofolate binding each 40fold and slows catalysis of both half-reactins less than 2fold Escherichia coli
1.5.1.20 F223L affinity for methylenetetrahydrofolate is unaffeacted. Mutant catalyzes the oxidative half-reaction 3fold faster than wild-type Escherichia coli

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.5.1.20 5,10-methylenetetrahydrofolate
-
 Escherichia coli

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.5.1.20 0.0005
-
 5,10-methylenetetrahydrofolate wild-type, pH 7.2, 25°C Escherichia coli
1.5.1.20 0.008
-
 5,10-methylenetetrahydrofolate mutant F223L, pH 7.2, 25°C Escherichia coli
1.5.1.20 0.02
-
 NADH cosubstrate 5,10-methylenetetrahydrofolate, wild-type, pH 7.2, 25°C Escherichia coli
1.5.1.20 0.066
-
 NADH cosubstrate menadione, wild-type, pH 7.2, 25°C Escherichia coli
1.5.1.20 0.093
-
 5,10-methylenetetrahydrofolate mutant F223A, pH 7.2, 25°C Escherichia coli
1.5.1.20 0.14
-
 NADH cosubstrate 5,10-methylenetetrahydrofolate, mutant F223A, pH 7.2, 25°C Escherichia coli
1.5.1.20 0.236
-
 NADH cosubstrate 5,10-methylenetetrahydrofolate, mutant F223L, pH 7.2, 25°C Escherichia coli
1.5.1.20 0.47
-
 NADH cosubstrate menadione, mutant F223L, pH 7.2, 25°C Escherichia coli
1.5.1.20 0.585
-
 NADH cosubstrate menadione, mutant F223A, pH 7.2, 25°C Escherichia coli

Organism

EC Number Organism UniProt Comment Textmining
1.5.1.20 Escherichia coli P0AEZ1
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.5.1.20 5,10-methylenetetrahydrofolate + NADH
-
 Escherichia coli 5-methyltetrahydrofolate + NAD+
-
 ?
1.5.1.20 NADH + menadione
-
 Escherichia coli NAD+ + reduced menadione
-
 ?

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.5.1.20 10.4
-
 NADH cosubstrate 5,10-methylenetetrahydrofolate, wild-type, pH 7.2, 25°C Escherichia coli
1.5.1.20 14
-
 NADH cosubstrate 5,10-methylenetetrahydrofolate, mutant F223L, pH 7.2, 25°C Escherichia coli
1.5.1.20 21.9
-
 NADH cosubstrate 5,10-methylenetetrahydrofolate, mutant F223A, pH 7.2, 25°C Escherichia coli
1.5.1.20 22
-
 NADH cosubstrate menadione, mutant F223A, pH 7.2, 25°C Escherichia coli
1.5.1.20 31
-
 NADH cosubstrate menadione, mutant F223L, pH 7.2, 25°C Escherichia coli
1.5.1.20 55
-
 NADH cosubstrate menadione, wild-type, pH 7.2, 25°C Escherichia coli

Cofactor

EC Number Cofactor Comment Organism Structure
1.5.1.20 NAD+
-
 Escherichia coli
1.5.1.20 NADH
-
 Escherichia coli

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
1.5.1.20 0.16
-
 5,10-methylenetetrahydrofolate mutant F223L, pH 7.2, 25°C Escherichia coli
1.5.1.20 0.32
-
 5,10-methylenetetrahydrofolate wild-type, pH 7.2, 25°C Escherichia coli