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EC 1.5.1.54: methylenetetrahydrofolate reductase (NADH)

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

Reaction

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

Synonyms

5,10-CH2-H4folate reductase, 5,10-methylenetetrahydrofolate reductase, 5,10-methylenetetrahydrofolate reductase (FADH2), 5,10-methylenetetrahydrofolic acid reductase, 5,10-methylenetetrahydropteroylglutamate reductase, 5-methyltetrahydrofolate:(acceptor) oxidoreductase, metF, methylenetetrahydrofolate (reduced riboflavin adenine dinucleotide) reductase, methylenetetrahydrofolate reductase, methylenetetrahydrofolic acid reductase, MSMEG_6596, MSMEG_6649, MTHFR1, MTHFR2, N5,10-methylenetetrahydrofolate reductase, N5,N10-methylenetetrahydrofolate reductase

ECTree

     1 Oxidoreductases
         1.5 Acting on the CH-NH group of donors
             1.5.1 With NAD+ or NADP+ as acceptor
                EC 1.5.1.541.5.1.54 methylenetetrahydrofolate reductase (NADH)

Reference

Reference on EC 1.5.1.54 - methylenetetrahydrofolate reductase (NADH)

Please use the Reference Search for a specific query.

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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Zuo, C.; Jolly, A.L.; Nikolova, A.P.; Satzer, D.I.; Cao, S.; Sanchez, J.S.; Ballou, D.P.; Trimmer, E.E.
A role for glutamine 183 in the folate oxidative half-reaction of methylenetetrahydrofolate reductase from Escherichia coli
Arch. Biochem. Biophys.
642
63-74
2018
Escherichia coli (P0AEZ1)
Manually annotated by BRENDA team
Grabowski, M.; Banecki, B.; Kadzinski, L.; Jakobkiewicz-Banecka, J.; Kazmierkiewicz, R.; Gabig-Ciminska, M.; Wegrzyn, G.; Wegrzyn, A.; Banecka-Majkutewicz, Z.
Genistein inhibits activities of methylenetetrahydrofolate reductase and lactate dehydrogenase, enzymes which use NADH as a substrate
Biochem. Biophys. Res. Commun.
465
363-367
2015
Escherichia coli (P0AEZ1)
Manually annotated by BRENDA team
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
Biochemistry
40
6205-6215
2001
Escherichia coli (P0AEZ1)
Manually annotated by BRENDA team
Trimmer, E.E.; Ballou, D.P.; Ludwig, M.L.; Matthews, R.G.
Folate activation and catalysis in methylenetetrahydrofolate reductase from Escherichia coli roles for aspartate 120 and glutamate 28
Biochemistry
40
6216-6226
2001
Escherichia coli (P0AEZ1)
Manually annotated by BRENDA team
Trimmer, E.E.; Ballou, D.P.; Galloway, L.J.; Scannell, S.A.; Brinker, D.R.; Casas, K.R.
Aspartate 120 of Escherichia coli methylenetetrahydrofolate reductase evidence for major roles in folate binding and catalysis and a minor role in flavin reactivity
Biochemistry
44
6809-6822
2005
Escherichia coli (P0AEZ1)
Manually annotated by BRENDA team
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
Biochemistry
48
7673-7685
2009
Escherichia coli (P0AEZ1)
Manually annotated by BRENDA team
Wohlfarth, G.; Geerligs, G.; Diekert, G.
Purification and properties of a NADH-dependent 5,10-methylenetetrahydrofolate reductase from Peptostreptococcus productus
Eur. J. Biochem.
192
411-417
1990
Blautia producta, Blautia producta Marburg
Manually annotated by BRENDA team
Sheppard, C.A.; Trimmer, E.E.; Matthews, R.G.
Purification and properties of NADH-dependent 5, 10-methylenetetrahydrofolate reductase (MetF) from Escherichia coli
J. Bacteriol.
181
718-725
1999
Escherichia coli (P0AEZ1)
Manually annotated by BRENDA team
Bertsch, J.; Oeppinger, C.; Hess, V.; Langer, J.; Mueller, V.
Heterotrimeric NADH-oxidizing methylenetetrahydrofolate reductase from the acetogenic bacterium Acetobacterium woodii
J. Bacteriol.
197
1681-1689
2015
Acetobacterium woodii (H6LBX9), Acetobacterium woodii DSM 1030 (H6LBX9)
Manually annotated by BRENDA team
Sah, S.; Lahry, K.; Talwar, C.; Singh, S.; Varshney, U.
Monomeric NADH-oxidizing methylenetetrahydrofolate reductases from Mycobacterium smegmatis lack flavin coenzyme
J. Bacteriol.
202
e00709
2020
Mycolicibacterium smegmatis (A0R6M0), Mycolicibacterium smegmatis (A0R6S0), Mycolicibacterium smegmatis ATCC 700084 (A0R6M0), Mycolicibacterium smegmatis ATCC 700084 (A0R6S0)
Manually annotated by BRENDA team
Roje, S.; Wang, H.; McNeil, S.D.; Raymond, R.K.; Appling, D.R.; Shachar-Hill, Y.; Bohnert, H.J.; Hanson, A.D.
Isolation, characterization, and functional expression of cDNAs encoding NADH-dependent methylenetetrahydrofolate reductase from higher plants
J. Biol. Chem.
274
36089-36096
1999
Arabidopsis thaliana (O80585), Arabidopsis thaliana (Q9SE60), Zea mays (Q9SE94)
Manually annotated by BRENDA team
Roje, S.; Chan, S.Y.; Kaplan, F.; Raymond, R.K.; Horne, D.W.; Appling, D.R.; Hanson, A.D.
Metabolic engineering in yeast demonstrates that S-adenosylmethionine controls flux through the methylenetetrahydrofolate reductase reaction in vivo
J. Biol. Chem.
277
4056-4061
2002
Arabidopsis thaliana (Q9SE60)
Manually annotated by BRENDA team
Lu, C.; Liu, Y.; Li, J.; Liu, L.; Du, G.
Engineering of biosynthesis pathway and NADPH supply for improved L-5-methyltetrahydrofolate production by Lactococcus lactis
J. Microbiol. Biotechnol.
31
154-162
2021
Lactococcus lactis subsp. lactis (A0A0B8QP67)
Manually annotated by BRENDA team
Guenther, B.; Sheppard, C.; Tran, P.; Rozen, R.; Matthews, R.; Ludwig, M.
The structure and properties of methylenetetrahydrofolate reductase from Escherichia coli suggest how folate ameliorates human hyperhomocysteinemia
Nat. Struct. Biol.
6
359-365
1999
Escherichia coli (P0AEZ1)
-
Manually annotated by BRENDA team