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Literature summary for 1.5.1.54 extracted from

  • Trimmer, E.E.; Ballou, D.P.; Matthews, R.G.
    Methylenetetrahydrofolate reductase from Escherichia coli elucidation of the kinetic mechanism by steady-state and rapid-reaction studies (2001), Biochemistry, 40, 6205-6215 .
    View publication on PubMed

Organism

Organism UniProt Comment Textmining
Escherichia coli P0AEZ1 cf. EC 1.5.1.20
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
5,10-methylenetetrahydrofolate + NADH + H+
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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
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r

Cofactor

Cofactor Comment Organism Structure
FAD midpoint potential of the enzyme-bound flavin is -237 mV Escherichia coli

General Information

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