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1.5.1.15: methylenetetrahydrofolate dehydrogenase (NAD+)

This is an abbreviated version!
For detailed information about methylenetetrahydrofolate dehydrogenase (NAD+), go to the full flat file.

Word Map on EC 1.5.1.15

Reaction

5,10-methylenetetrahydrofolate
+
NAD+
=
5,10-methenyltetrahydrofolate
+
NADH
+
H+

Synonyms

5,10-CH2-THF dehydrogenase, 5,10-methylenetetrahydrofolate reductase, bifunctional N5,N10-methylene-H4F dehydrogenase/N5,N10-methenyltetrahydrofolate cyclohydrolase, FolD, methenyltetrahydrofolate cyclohydrolase, methylenetetrahydrofolate dehydrogenase (NAD+-dependent), methylenetetrahydrofolate dehydrogenase-cyclohydrolase, methylenetetrahydrofolate dehydrogenase-methenyltetrahydrofolate cyclohydrolase, methylenetetrahydrofolate dehydrogenase/cyclohydrolase, methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase, methylenetetrahydrofolate reductase, methyleneTHF dehydrogenase, Mg2+-/phosphate-dependent dehydrogenase, Mg2+/NAD-dependent methylenetetrahydrofolate dehydrogenase, More, MSMEG_6596, MSMEG_6649, MTD, MTHFD2, MTHFD2L, MTHFR, MTHFR1, MTHFR2, NAD+-dependent methylene-H4F dehydrogenase, NAD-dependent dehydrogenase-cyclohydrolase, NADH-oxidizing methylenetetrahydrofolate reductase, NMDMC

ECTree

     1 Oxidoreductases
         1.5 Acting on the CH-NH group of donors
             1.5.1 With NAD+ or NADP+ as acceptor
                1.5.1.15 methylenetetrahydrofolate dehydrogenase (NAD+)

General Information

General Information on EC 1.5.1.15 - methylenetetrahydrofolate dehydrogenase (NAD+)

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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
-
the Escherichia coli enzyme differs from the characterized pig, human, and yeast MTHFRs (EC 1.5.1.5) in its preference for NADH over NADPH as substrate and by the absence of a regulatory domain. Structures of Ered(wild-type)-NADH and Eox(Glu28Gln)-CH3-H4folate complexes reveal that the ligands occupy partially overlapping sites at the si face of the FAD. Thus, the binding of one substrate to the enzyme prevents the binding of the other substrate, consistent with the ping-pong bi-bi kinetic mechanism. But the structures reveal that the active site conformations of NADH and CH3-H4folate are remarkably different
malfunction
metabolism
physiological function
additional information
-
a role for residue glutamine 183 in the folate oxidative half-reaction of methylenetetrahydrofolate reductase from Escherichia coli. Residue Gln183 may participate in NADH binding, based on the hydrogen bonding interactions between the Gln side chain and the carboxamide of NADH observed in the X-ray structure