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Literature summary for 1.5.1.20 extracted from

  • Roje, S.; Chan, S.Y.; Kaplan, F.; Raymond, R.K.; Horne, D.W.; Appling, D.R.; Hanson, A.D.
    Metabolic endineering in yeast demonstrates that S-adenosylmethionine controls flux through the methylenetetrahydrofolate reductase reaction in vivo (2002), J. Biol. Chem., 277, 4056-4061.
    View publication on PubMed
Search for more literature for 1.5.1.20

Cloned(Commentary)

Cloned (Comment) Organism
expression of chimeric mutant in an enzyme-deficient strain, overexpression of the plant enzyme from Arabidopsis thaliana in an enzyme-deficient strain can complement the mutant and results in 8fold increased accumulation of S-adenosyl-L-methionine, mechanism overview Saccharomyces cerevisiae
overexpression of the wild-type enzyme and the chimeric mutant in a Saccharomyces cerevisiae enzyme-deficient strain, complementation of the enzyme-deficient strain, 8fold increased accumulation of S-adenosyl-L-methionine in case of recombinant wild-type expression in yeast, mechanism overview Arabidopsis thaliana

Protein Variants

Protein Variants Comment Organism
additional information construction of a chimeric enzyme comprising the yeast N-terminal domain and the Arabidopsis thaliana C-terminal domain, recombinant expression in and complementation of an enzyme-deficient mutant strain with altered sensitivity to S-adenosyl-L-methionine and altered cofactor specifcity Arabidopsis thaliana
additional information construction of a chimeric enzyme comprising the yeast N-terminal domain and the Arabidopsis thaliana C-terminal domain, recombinant expression in and complementation of an enzyme-deficient mutant strain with altered sensitivity to S-adenosyl-L-methionine and altered cofactor specifcity Saccharomyces cerevisiae

Inhibitors

Inhibitors Comment Organism Structure
5,10-methylenetetrahydrofolate substrate inhibition Arabidopsis thaliana
5,10-methylenetetrahydrofolate substrate inhibition Saccharomyces cerevisiae
additional information no inhibition by S-adenosyl-L-methionine, which is no feed-back regulator of the methyl group biosynthesis pathway in plants Arabidopsis thaliana
S-adenosyl-L-methionine feed-back regulation of the methyl group biosynthesis pathway in vivo, the chimeric mutant enzyme is insensitive to inhibition by S-adenosyl-L-methionine Saccharomyces cerevisiae

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.0027
-
 NADH recombinant wild-type enzyme, pH 7.2 Arabidopsis thaliana
0.0028
-
 NADH recombinant chimeric mutant enzyme, pH 7.2 Arabidopsis thaliana
0.0028
-
 NADH recombinant chimeric mutant enzyme, pH 7.2 Saccharomyces cerevisiae
0.0073
-
 NADPH recombinant chimeric mutant enzyme, pH 7.2 Arabidopsis thaliana
0.0073
-
 NADPH recombinant chimeric mutant enzyme, pH 7.2 Saccharomyces cerevisiae
0.011
-
 5,10-methylenetetrahydrofolate recombinant enzyme, with NADPH, pH 7.2 Saccharomyces cerevisiae
0.021
-
 NADPH recombinant enzyme, pH 7.2 Saccharomyces cerevisiae
0.106
-
 5,10-methylenetetrahydrofolate recombinant chimeric mutant enzyme, with NADH, pH 7.2 Arabidopsis thaliana
0.106
-
 5,10-methylenetetrahydrofolate recombinant chimeric mutant enzyme, with NADH, pH 7.2 Saccharomyces cerevisiae
0.152
-
 5,10-methylenetetrahydrofolate recombinant chimeric mutant enzyme, with NADPH, pH 7.2 Arabidopsis thaliana
0.152
-
 5,10-methylenetetrahydrofolate recombinant chimeric mutant enzyme, with NADPH, pH 7.2 Saccharomyces cerevisiae
0.287
-
 5,10-methylenetetrahydrofolate recombinant wild-type enzyme, with NADH, pH 7.2 Arabidopsis thaliana

Localization

Localization Comment Organism GeneOntology No. Textmining
cytosol
-
 Arabidopsis thaliana 5829
-

Organism

Organism UniProt Comment Textmining
Arabidopsis thaliana
-
 gene met13
-
Saccharomyces cerevisiae P53128 gene met13
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
5,10-methylenetetrahydrofolate + NAD(P)H NADH is the preferred cofactor of the plant enzyme Arabidopsis thaliana 5-methyltetrahydrofolate + NAD(P)+
-
 r
5,10-methylenetetrahydrofolate + NADH + H+
-
 Arabidopsis thaliana 5-methyltetrahydrofolate + NAD+
-
 r
5,10-methylenetetrahydrofolate + NADH + H+
-
 Saccharomyces cerevisiae 5-methyltetrahydrofolate + NAD+
-
 r
5,10-methylenetetrahydrofolate + NADPH
-
 Saccharomyces cerevisiae 5-methyltetrahydrofolate + NADP+
-
 r

Synonyms

Synonyms Comment Organism
AtMTHFR-1
-
 Arabidopsis thaliana
methylenetetrahydrofolate reductase
-
 Arabidopsis thaliana
methylenetetrahydrofolate reductase
-
 Saccharomyces cerevisiae
MTHFR
-
 Saccharomyces cerevisiae

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.2
-
 assay at Saccharomyces cerevisiae

Cofactor

Cofactor Comment Organism Structure
additional information wild-type shows no activity with NADH/NAD+ Saccharomyces cerevisiae
NAD+ only active with the chimeric mutant enzyme, not with the wild-type Saccharomyces cerevisiae
NAD+ recombinant wild-type and chimeric mutant enzymes Arabidopsis thaliana
NADH only active with the chimeric mutant enzyme, not with the wild-type Saccharomyces cerevisiae
NADH recombinant wild-type and chimeric mutant enzymes Arabidopsis thaliana
NADP+
-
 Saccharomyces cerevisiae
NADP+ poor cofactor for the recombinant wild-type enzyme, but utilized by the chimeric mutant enzyme with activity equal to the activity with NAD+ Arabidopsis thaliana
NADPH dependent on Saccharomyces cerevisiae
NADPH poor cofactor for the recombinant wild-type enzyme, but utilized by the chimeric mutant enzyme with activity equal to the activity with NADH Arabidopsis thaliana

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
0.455
-
 5,10-methylenetetrahydrofolate recombinant enzyme, with NADPH, pH 7.2 Saccharomyces cerevisiae
0.873
-
 5,10-methylenetetrahydrofolate recombinant wild-type enzyme, with NADH, pH 7.2 Arabidopsis thaliana