Enzyme

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     1. Oxidoreductases
        1.5 Acting on the CH-NH group of donors
            1.5.1 With NAD+ or NADP+ as acceptor
ID:1.5.1.20
Description:Methylenetetrahydrofolate reductase (NAD(P)H).
Alternative Name: N(5,10)-methylenetetrahydrofolate reductase.
N(5),N(10)-methylenetetrahydrofolate reductase.
MTHFR.
Methylenetetrahydrofolic acid reductase.
Methylenetetrahydrofolate reductase (NADPH).
Methylenetetrahydrofolate reductase (NADPH(2)).
Methylenetetrahydrofolate reductase.
reductase.
Methylenetetrahydrofolate (reduced riboflavin adenine dinucleotide)
phosphate) reductase.
Methylenetetrahydrofolate (reduced nicotinamide adenine dinucleotide
5-methyltetrahydrofolate:NADP(+) oxidoreductase.
5-methyltetrahydrofolate:NAD(+) oxidoreductase.
5-methyltetrahydrofolate:NAD oxidoreductase.
5-methyltetrahydrofolate:(acceptor) oxidoreductase.
5,10-methylenetetrahydropteroylglutamate reductase.
5,10-methylenetetrahydrofolic acid reductase.
5,10-methylenetetrahydrofolate reductase (NADPH).
5,10-methylenetetrahydrofolate reductase (FADH(2)).
5,10-methylenetetrahydrofolate reductase.
5,10-CH(2)-H(4)folate reductase.
Cath: 3.20.20.220;

3D structure

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References

External Links

UniProtKB Enzyme Link: UniProtKB 1.5.1.20
BRENDA Enzyme Link: BRENDA 1.5.1.20
KEGG Enzyme Link: KEGG1.5.1.20
BioCyc Enzyme Link: BioCyc 1.5.1.20
ExPASy Enzyme Link: ExPASy1.5.1.20
EC2PDB Enzyme Link: EC2PDB 1.5.1.20
ExplorEnz Enzyme Link: ExplorEnz 1.5.1.20
PRIAM enzyme-specific profiles Link: PRIAM 1.5.1.20
IntEnz Enzyme Link: IntEnz 1.5.1.20
MEDLINE Enzyme Link: MEDLINE 1.5.1.20
MSA:

1.5.1.20;

Phylogenetic Tree:

1.5.1.20;

Uniprot:
M-CSA:
RHEA:19821 (6S)-5-methyl-5,6,7,8-tetrahydrofolate + NAD(+) = (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + H(+) + NADH
RULE(radius=1) ([*:1]-[CH3;+0:2].[*:3]-[NH;+0:4]-[*:5]).[*:6]-[n+;H0:7]1:[cH;+0:8]:[cH;+0:9]:[cH;+0:10]:[c;H0;+0:11](-[*:12]):[cH;+0:13]:1>>[*:3]-[N;H0;+0:4](-[*:5])-[CH2;+0:2]-[*:1].[*:6]-[N;H0;+0:7]1-[CH;+0:8]=[CH;+0:9]-[CH2;+0:10]-[C;H0;+0:11](-[*:12])=[CH;+0:13]-1
Reaction
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References

TitleAuthorsDatePubMed ID
Purification and properties of NADH-dependent 5, 10-methylenetetrahydrofolate reductase (MetF) from Escherichia coli.Sheppard CA, Trimmer EE, Matthews RG1999 Feb9922232
Purification and properties of methylenetetrahydrofolate reductase from pig liver.Daubner SC, Matthews RG1982 Jan 106975779
Mammalian methylenetetrahydrofolate reductase. Partial purification, properties, and inhibition by S-adenosylmethionine.Kutzbach C, Stokstad EL1971 Dec 154399897
Insights into severe 5,10-methylenetetrahydrofolate reductase deficiency: molecular genetic and enzymatic characterization of 76 patients.Burda P, Schäfer A, Suormala T, Rummel T, Bürer C, Heuberger D, Frapolli M, Giunta C, Sokolová J, Vlášková H, Kožich V, Koch HG, Fowler B, Froese DS, Baumgartner MR2015 Jun25736335
The structure and properties of methylenetetrahydrofolate reductase from Escherichia coli suggest how folate ameliorates human hyperhomocysteinemia.Guenther BD, Sheppard CA, Tran P, Rozen R, Matthews RG, Ludwig ML1999 Apr10201405

RHEA:19817 (6S)-5-methyl-5,6,7,8-tetrahydrofolate + NADP(+) = (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + H(+) + NADPH
RULE(radius=1) ([*:1]-[CH3;+0:2].[*:3]-[NH;+0:4]-[*:5]).[*:6]-[n+;H0:7]1:[cH;+0:8]:[cH;+0:9]:[cH;+0:10]:[c;H0;+0:11](-[*:12]):[cH;+0:13]:1>>[*:3]-[N;H0;+0:4](-[*:5])-[CH2;+0:2]-[*:1].[*:6]-[N;H0;+0:7]1-[CH;+0:8]=[CH;+0:9]-[CH2;+0:10]-[C;H0;+0:11](-[*:12])=[CH;+0:13]-1
Reaction
Core-to-Core More
Core-to-Core More

References

TitleAuthorsDatePubMed ID
Purification and properties of NADH-dependent 5, 10-methylenetetrahydrofolate reductase (MetF) from Escherichia coli.Sheppard CA, Trimmer EE, Matthews RG1999 Feb9922232
Purification and properties of methylenetetrahydrofolate reductase from pig liver.Daubner SC, Matthews RG1982 Jan 106975779
Mammalian methylenetetrahydrofolate reductase. Partial purification, properties, and inhibition by S-adenosylmethionine.Kutzbach C, Stokstad EL1971 Dec 154399897
Insights into severe 5,10-methylenetetrahydrofolate reductase deficiency: molecular genetic and enzymatic characterization of 76 patients.Burda P, Schäfer A, Suormala T, Rummel T, Bürer C, Heuberger D, Frapolli M, Giunta C, Sokolová J, Vlášková H, Kožich V, Koch HG, Fowler B, Froese DS, Baumgartner MR2015 Jun25736335
The structure and properties of methylenetetrahydrofolate reductase from Escherichia coli suggest how folate ameliorates human hyperhomocysteinemia.Guenther BD, Sheppard CA, Tran P, Rozen R, Matthews RG, Ludwig ML1999 Apr10201405