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Literature summary for 1.5.1.20 extracted from

  • 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 (1999), J. Biol. Chem., 274, 36089-36096.
    View publication on PubMed

Activating Compound

Activating Compound Comment Organism Structure
S-adenosylmethionine stimulates Arabidopsis sp.

Cloned(Commentary)

Cloned (Comment) Organism
two MTHFR genes, a cDNAs encoding functional MTHFR is cloned, sequenced and expressed in Saccharomyces cerevisiae Zea mays
two MTHFR genes, two cDNAs encoding functional MTHFRs are cloned, sequenced and expressed in Saccharomyces cerevisiae at high levels Arabidopsis sp.

Inhibitors

Inhibitors Comment Organism Structure
additional information not inhibited by S-adenosylmethionine Arabidopsis sp.
additional information not inhibited by S-adenosylmethionine Escherichia coli
additional information not inhibited by S-adenosylmethionine Zea mays

Localization

Localization Comment Organism GeneOntology No. Textmining
cytosol
-
Arabidopsis sp. 5829
-
cytosol
-
Zea mays 5829
-

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
33000
-
4 * 33000 Escherichia coli
66000
-
2 * 66000, SDS-PAGE Arabidopsis sp.
66400
-
x * 66400, calculated from the nucleotide sequence Zea mays
141000
-
gel filtration Arabidopsis sp.

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
5,10-methylenetetrahydrofolate + NADH Escherichia coli
-
5-methyltetrahydrofolate + NAD+
-
?
5,10-methylenetetrahydrofolate + NADH Arabidopsis sp. folate-mediated one-carbon metabolism 5-methyltetrahydrofolate + NAD+
-
r
5,10-methylenetetrahydrofolate + NADH Zea mays folate-mediated one-carbon metabolism 5-methyltetrahydrofolate + NAD+
-
r

Organism

Organism UniProt Comment Textmining
Arabidopsis sp.
-
ecotype Columbia, expression in Saccharomyces cerevisiae
-
Escherichia coli
-
-
-
Zea mays Q9SE94 expression in Saccharomyces cerevisiae
-

Purification (Commentary)

Purification (Comment) Organism
643fold purification of recombinant enzyme, expressed in Saccharomyces cerevisiae Arabidopsis sp.

Source Tissue

Source Tissue Comment Organism Textmining
leaf
-
Arabidopsis sp.
-
leaf
-
Zea mays
-
root
-
Arabidopsis sp.
-
root
-
Zea mays
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
6.92
-
recombinant enzyme Arabidopsis sp.

Storage Stability

Storage Stability Organism
on ice, 3 h, loss of about 50% of activity Arabidopsis sp.

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
5,10-methylenetetrahydrofolate + NADH
-
Escherichia coli 5-methyltetrahydrofolate + NAD+
-
?
5,10-methylenetetrahydrofolate + NADH folate-mediated one-carbon metabolism Arabidopsis sp. 5-methyltetrahydrofolate + NAD+
-
r
5,10-methylenetetrahydrofolate + NADH folate-mediated one-carbon metabolism Zea mays 5-methyltetrahydrofolate + NAD+
-
r
5,10-methylenetetrahydrofolate + reduced acceptor reverse reaction: menadione as electron acceptor Escherichia coli 5-methyltetrahydrofolate + oxidized acceptor
-
r
5,10-methylenetetrahydrofolate + reduced acceptor reverse reaction: menadione as electron acceptor Arabidopsis sp. 5-methyltetrahydrofolate + oxidized acceptor
-
r
5,10-methylenetetrahydrofolate + reduced acceptor reverse reaction: menadione as electron acceptor Zea mays 5-methyltetrahydrofolate + oxidized acceptor
-
r
5,10-methylenetetrahydrofolate + reduced acceptor prefers NADH as reductant Escherichia coli 5-methyltetrahydrofolate + oxidized acceptor
-
r
5,10-methylenetetrahydrofolate + reduced acceptor forward reaction: strong preference of NADH over NADPH Arabidopsis sp. 5-methyltetrahydrofolate + oxidized acceptor
-
r
5,10-methylenetetrahydrofolate + reduced acceptor forward reaction: strong preference of NADH over NADPH Zea mays 5-methyltetrahydrofolate + oxidized acceptor
-
r

Subunits

Subunits Comment Organism
? x * 66400, calculated from the nucleotide sequence Zea mays
dimer 2 * 66000, SDS-PAGE Arabidopsis sp.
homotetramer 4 * 33000 Escherichia coli

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
assay at Escherichia coli
37
-
assay at Arabidopsis sp.
37
-
assay at Zea mays

Cofactor

Cofactor Comment Organism Structure
NADH
-
Escherichia coli
NADH strong preference of NADH over NADPH as reductant Arabidopsis sp.
NADH strong preference of NADH over NADPH as reductant Zea mays