Organism | UniProt | Comment | Textmining |
---|---|---|---|
Escherichia coli | P0AEZ1 | cf. EC 1.5.1.20 | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
5,10-methylenetetrahydrofolate + NADH + H+ | - |
Escherichia coli | 5-methyltetrahydrofolate + NAD+ | - |
? | |
NAD+ + menadiol | reaction of EC 1.6.5.2 | Escherichia coli | NADH + H+ + menadione | - |
r | |
NADH + H+ + menadione | reaction of EC 1.6.5.2 | Escherichia coli | NAD+ + menadiol | - |
r |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
FAD | midpoint potential of the enzyme-bound flavin is -237 mV | Escherichia coli |
General Information | Comment | Organism |
---|---|---|
metabolism | the half-reactions proceed at rates sufficiently fast to account for overall turnover, the enzyme is kinetically competent to catalyze these oxidoreductions by a ping-pong Bi-Bi mechanism. Reoxidation of the reduced flavin by CH2-H4folate is substantially rate limiting in the physiological NADH-CH2-H4folate oxidoreductase reaction. In the NADH-menadione oxidoreductase reaction, the reduction of the flavin by NADH is rate limiting as is the reduction of flavin by CH3-H4folate in the CH3-H4folate-menadione oxidoreductase reaction | Escherichia coli |