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 |
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 |
EC Number | Inhibitors | Comment | Organism | Structure |
---|---|---|---|---|
1.5.1.20 | 5,10-methylenetetrahydrofolate | - |
Escherichia coli |
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 |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
1.5.1.20 | Escherichia coli | P0AEZ1 | - |
- |
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 | - |
? |
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 |
EC Number | Cofactor | Comment | Organism | Structure |
---|---|---|---|---|
1.5.1.20 | NAD+ | - |
Escherichia coli | |
1.5.1.20 | NADH | - |
Escherichia coli |
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 |