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Literature summary for 1.5.1.15 extracted from

  • Shin, M.; Momb, J.; Appling, D.R.
    Human mitochondrial MTHFD2 is a dual redox cofactor-specific methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase (2017), Cancer Metab., 5, 11 .
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
6His-tagged enzyme is expressed in Escherichia coli Homo sapiens

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.123
-
5,10-methylenetetrahydropteroylglutamate pH 8.0, 30°C, at saturating concentrations of NADP+ (6.0 mM) Homo sapiens
0.133
-
5,10-methylenetetrahydropteroylglutamate pH 8.0, 30°C, at saturating concentrations of NAD+ (1.0 mM) Homo sapiens
0.302
-
5,10-methylenetetrahydropteroylpentaglutamate pH 8.0, 30°C, at saturating concentrations of NADP+ (6.0 mM) Homo sapiens
0.359
-
5,10-methylenetetrahydropteroylpentaglutamate pH 8.0, 30°C, at saturating concentrations of NAD+ (1.0 mM) Homo sapiens

Localization

Localization Comment Organism GeneOntology No. Textmining
mitochondrion
-
Homo sapiens 5739
-

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
36700
-
-
Homo sapiens

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
5,10-methylenetetrahydrofolate + NADP+ Homo sapiens
-
5,10-methenyltetrahydrofolate + NADPH + H+
-
?
5,10-methylenetetrahydrofolate + NADP+ Homo sapiens
-
5,10-methenyltetrahydrofolate + NADPH + H+ ?
-

Organism

Organism UniProt Comment Textmining
Homo sapiens P13995
-
-
Homo sapiens Q9H903
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Homo sapiens

Source Tissue

Source Tissue Comment Organism Textmining
carcinoma cell highly expressed in many cancer types Homo sapiens
-
embryo both Mthfd2 and Mthfd2l are expressed during embryogenesis but differ in timing of expression. Mthfd2l expression is low in early developmental stages but begins to increase at embryonic day 10.5 and remains elevated through birth while Mthfd2 is expressed more abundantly during early developmental stages and begins to taper off, with little or no expression observed in most adult tissues Homo sapiens
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
5,10-methylenetetrahydrofolate + NADP+
-
Homo sapiens 5,10-methenyltetrahydrofolate + NADPH + H+
-
?
5,10-methylenetetrahydrofolate + NADP+
-
Homo sapiens 5,10-methenyltetrahydrofolate + NADPH + H+ ?
-
5,10-methylenetetrahydropteroylglutamate + NAD+ NAD+-dependent dehydrogenase activity of MTHFD2 is 8.5fold higher than its NADP+-dependent activity Homo sapiens 5,10-methenyltetrahydropteroylglutamate + NADH + H+
-
?
5,10-methylenetetrahydropteroylglutamate + NAD+ NAD+-dependent dehydrogenase activity of MTHFD2L is 3.4fold higher than its NADP+-dependent activity under saturating substrate conditions Homo sapiens 5,10-methenyltetrahydropteroylglutamate + NADH + H+
-
?
5,10-methylenetetrahydropteroylglutamate + NADP+ NAD+-dependent dehydrogenase activity of MTHFD2 is 8.5fold higher than its NADP+-dependent activity Homo sapiens 5,10-methenyltetrahydropteroylglutamate + NADPH + H+
-
?
5,10-methylenetetrahydropteroylglutamate + NADP+ NAD+-dependent dehydrogenase activity of MTHFD2L is 3.4fold higher than its NADP+-dependent activity under saturating substrate conditions Homo sapiens 5,10-methenyltetrahydropteroylglutamate + NADPH + H+
-
?
5,10-methylenetetrahydropteroylpentaglutamate + NAD+ NAD+-dependent dehydrogenase activity of MTHFD2 with the substrate 5,10-methylenetetrahydropteroylglutamate is 8.5fold higher than its NADP+-dependent activity. While the NAD+-dependent activity of MTHFD2 slightly decreases, its maximal NADP+-dependent activity considerably increases with 5,10-methylenetetrahydropteroylpentaglutamate compared to 5,10-methylenetetrahydropteroylglutamate Homo sapiens 5,10-methenyltetrahydropteroylpentaglutamate + NADH + H+
-
?
5,10-methylenetetrahydropteroylpentaglutamate + NAD+ NAD+-dependent dehydrogenase activity of MTHFD2L with the substrate 5,10-methylenetetrahydropteroylglutamate is 3.4fold higher than its NADP+-dependent activity under saturating substrate conditions. While the NAD+-dependent activity of MTHFD2 slightly decreases, its maximal NADP+-dependent activity considerably increases with 5,10-methylenetetrahydropteroylpentaglutamate compared to 5,10-methylenetetrahydropteroylglutamate Homo sapiens 5,10-methenyltetrahydropteroylpentaglutamate + NADH + H+
-
?
5,10-methylenetetrahydropteroylpentaglutamate + NADP+ NAD+-dependent dehydrogenase activity of MTHFD2 with the substrate 5,10-methylenetetrahydropteroylglutamate is 8.5fold higher than its NADP+-dependent activity. While the NAD+-dependent activity of MTHFD2 slightly decreases, its maximal NADP+-dependent activity considerably increases with 5,10-methylenetetrahydropteroylpentaglutamate compared to 5,10-methylenetetrahydropteroylglutamate Homo sapiens 5,10-methenyltetrahydropteroylpentaglutamate + NADPH + H+
-
?
5,10-methylenetetrahydropteroylpentaglutamate + NADP+ NAD+-dependent dehydrogenase activity of MTHFD2L with the substrate 5,10-methylenetetrahydropteroylglutamate is 3.4fold higher than its NADP+-dependent activity under saturating substrate conditions. While the NAD+-dependent activity of MTHFD2 slightly decreases, its maximal NADP+-dependent activity considerably increases with 5,10-methylenetetrahydropteroylpentaglutamate compared to 5,10-methylenetetrahydropteroylglutamate Homo sapiens 5,10-methenyltetrahydropteroylpentaglutamate + NADPH + H+
-
?

Synonyms

Synonyms Comment Organism
5,10-CH2-THF dehydrogenase
-
Homo sapiens
methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase
-
Homo sapiens
MTHFD2
-
Homo sapiens
MTHFD2L
-
Homo sapiens

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.5
-
5,10-methylenetetrahydropteroylglutamate pH 8.0, 30°C, at saturating concentrations of NADP+ (6.0 mM) Homo sapiens
6.4
-
5,10-methylenetetrahydropteroylpentaglutamate pH 8.0, 30°C, at saturating concentrations of NADP+ (6.0 mM) Homo sapiens
12.4
-
5,10-methylenetetrahydropteroylglutamate pH 8.0, 30°C, at saturating concentrations of NAD+ (1.0 mM) Homo sapiens
15.4
-
5,10-methylenetetrahydropteroylpentaglutamate pH 8.0, 30°C, at saturating concentrations of NAD+ (1.0 mM) Homo sapiens

Cofactor

Cofactor Comment Organism Structure
NAD+ the enzyme exhibits dual redox cofactor specificity, utilizing either NADP+ or NAD+. NAD+-dependent dehydrogenase activity of MTHFD2 with the substrate 5,10-methylenetetrahydropteroylglutamate is 8.5fold higher than its NADP+-dependent activity. While the NAD+-dependent activity of MTHFD2 slightly decreases, its maximal NADP+-dependent activity considerably increases with 5,10-methylenetetrahydropteroylpentaglutamate compared to 5,10-methylenetetrahydropteroylglutamate Homo sapiens
NAD+ the enzyme exhibits dual redox cofactor specificity, utilizing either NADP+ or NAD+. NAD+-dependent dehydrogenase activity of MTHFD2L with the substrate 5,10-methylenetetrahydropteroylglutamat is 3.4fold higher than its NADP+-dependent activity under saturating substrate conditions. While the NAD+-dependent activity of MTHFD2 slightly decreases, its maximal NADP+-dependent activity considerably increases with 5,10-methylenetetrahydropteroylpentaglutamate compared to 5,10-methylenetetrahydropteroylglutamate Homo sapiens
NADP+ the enzyme exhibits dual redox cofactor specificity, utilizing either NADP+ or NAD+. NAD+-dependent dehydrogenase activity of MTHFD2 with the substrate 5,10-methylenetetrahydropteroylglutamate is 8.5fold higher than its NADP+-dependent activity. While the NAD+-dependent activity of MTHFD2 slightly decreases, its maximal NADP+-dependent activity considerably increases with 5,10-methylenetetrahydropteroylpentaglutamate compared to 5,10-methylenetetrahydropteroylglutamate Homo sapiens
NADP+ the enzyme exhibits dual redox cofactor specificity, utilizing either NADP+ or NAD+. NAD+-dependent dehydrogenase activity of MTHFD2L with the substrate 5,10-methylenetetrahydropteroylglutamate is 3.4fold higher than its NADP+-dependent activity under saturating substrate conditions. While the NAD+-dependent activity of MTHFD2 slightly decreases, its maximal NADP+-dependent activity considerably increases with 5,10-methylenetetrahydropteroylpentaglutamate compared to 5,10-methylenetetrahydropteroylglutamate Homo sapiens

General Information

General Information Comment Organism
metabolism the enzyme is involved in folate pathway. It is involved in mitochondrial NADPH production. It is proposed that isoenzyme MTHFD2 may be expressed to boost flux through the mitochondrial folate pathway during early periods of embryogenesis when isoenzyme MTHFD2L alone is not sufficient to support high rates of cell proliferation Homo sapiens

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
12
-
5,10-methylenetetrahydropteroylglutamate pH 8.0, 30°C, at saturating concentrations of NADP+ (6.0 mM) Homo sapiens
21
-
5,10-methylenetetrahydropteroylpentaglutamate pH 8.0, 30°C, at saturating concentrations of NADP+ (6.0 mM) Homo sapiens
43
-
5,10-methylenetetrahydropteroylpentaglutamate pH 8.0, 30°C, at saturating concentrations of NAD+ (1.0 mM) Homo sapiens
93
-
5,10-methylenetetrahydropteroylglutamate pH 8.0, 30°C, at saturating concentrations of NAD+ (1.0 mM) Homo sapiens