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Literature summary extracted from
- Human mitochondrial MTHFD2 is a dual redox cofactor-specific methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase (2017), Cancer Metab., 5, 11 .
Cloned(Commentary)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 1.5.1.5 | 6His-tagged enzyme is expressed in Escherichia coli | Homo sapiens |
| 1.5.1.15 | 6His-tagged enzyme is expressed in Escherichia coli | Homo sapiens |
| 3.5.4.9 | 6His-tagged enzyme is expressed in Escherichia coli | Homo sapiens |
KM Value [mM]
| EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 1.5.1.5 | 0.123 | - |
5,10-methylenetetrahydropteroylglutamate | pH 8.0, 30°C, at saturating concentrations of NADP+ (6.0 mM) | Homo sapiens |  |
| 1.5.1.5 | 0.133 | - |
5,10-methylenetetrahydropteroylglutamate | pH 8.0, 30°C, at saturating concentrations of NAD+ (1.0 mM) | Homo sapiens | |
| 1.5.1.5 | 0.302 | - |
5,10-methylenetetrahydropteroylpentaglutamate | pH 8.0, 30°C, at saturating concentrations of NADP+ (6.0 mM) | Homo sapiens | |
| 1.5.1.5 | 0.359 | - |
5,10-methylenetetrahydropteroylpentaglutamate | pH 8.0, 30°C, at saturating concentrations of NAD+ (1.0 mM) | Homo sapiens | |
| 1.5.1.15 | 0.123 | - |
5,10-methylenetetrahydropteroylglutamate | pH 8.0, 30°C, at saturating concentrations of NADP+ (6.0 mM) | Homo sapiens | |
| 1.5.1.15 | 0.133 | - |
5,10-methylenetetrahydropteroylglutamate | pH 8.0, 30°C, at saturating concentrations of NAD+ (1.0 mM) | Homo sapiens | |
| 1.5.1.15 | 0.302 | - |
5,10-methylenetetrahydropteroylpentaglutamate | pH 8.0, 30°C, at saturating concentrations of NADP+ (6.0 mM) | Homo sapiens | |
| 1.5.1.15 | 0.359 | - |
5,10-methylenetetrahydropteroylpentaglutamate | pH 8.0, 30°C, at saturating concentrations of NAD+ (1.0 mM) | Homo sapiens | |
Localization
| EC Number | Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|---|
| 1.5.1.5 | mitochondrion | - |
Homo sapiens | 5739 | - |
| 1.5.1.15 | mitochondrion | - |
Homo sapiens | 5739 | - |
| 3.5.4.9 | mitochondrion | - |
Homo sapiens | 5739 | - |
Molecular Weight [Da]
| EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|---|
| 1.5.1.5 | 36700 | - |
- |
Homo sapiens |
| 1.5.1.15 | 36700 | - |
- |
Homo sapiens |
| 3.5.4.9 | 36700 | - |
- |
Homo sapiens |
Natural Substrates/ Products (Substrates)
| EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 1.5.1.5 | 5,10-methylenetetrahydrofolate + NADP+ | Homo sapiens | - |
5,10-methenyltetrahydrofolate + NADPH + H+ | - |
? | |
| 1.5.1.15 | 5,10-methylenetetrahydrofolate + NADP+ | Homo sapiens | - |
5,10-methenyltetrahydrofolate + NADPH + H+ | - |
? | |
| 1.5.1.15 | 5,10-methylenetetrahydrofolate + NADP+ | Homo sapiens | - |
5,10-methenyltetrahydrofolate + NADPH + H+ | ? | - |
|
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 1.5.1.5 | Homo sapiens | P13995 | - |
- |
| 1.5.1.5 | Homo sapiens | Q9H903 | - |
- |
| 1.5.1.15 | Homo sapiens | P13995 | - |
- |
| 1.5.1.15 | Homo sapiens | Q9H903 | - |
- |
| 3.5.4.9 | Homo sapiens | P13995 | - |
- |
| 3.5.4.9 | Homo sapiens | Q9H903 | - |
- |
Purification (Commentary)
| EC Number | Purification (Comment) | Organism |
|---|---|---|
| 1.5.1.5 | - |
Homo sapiens |
| 1.5.1.15 | - |
Homo sapiens |
| 3.5.4.9 | - |
Homo sapiens |
Source Tissue
| EC Number | Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|---|
| 1.5.1.5 | carcinoma cell | highly expressed in many cancer types | Homo sapiens | - |
| 1.5.1.5 | 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 | - |
| 1.5.1.15 | carcinoma cell | highly expressed in many cancer types | Homo sapiens | - |
| 1.5.1.15 | 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 | - |
| 3.5.4.9 | carcinoma cell | highly expressed in many cancer types | Homo sapiens | - |
| 3.5.4.9 | 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)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 1.5.1.5 | 5,10-methylenetetrahydrofolate + NADP+ | - |
Homo sapiens | 5,10-methenyltetrahydrofolate + NADPH + H+ | - |
? | |
| 1.5.1.5 | 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+ | - |
? | |
| 1.5.1.5 | 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+ | - |
? | |
| 1.5.1.5 | 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+ | - |
? | |
| 1.5.1.5 | 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+ | - |
? | |
| 1.5.1.5 | 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+ | - |
? | |
| 1.5.1.5 | 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+ | - |
? | |
| 1.5.1.5 | 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+ | - |
? | |
| 1.5.1.5 | 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+ | - |
? | |
| 1.5.1.15 | 5,10-methylenetetrahydrofolate + NADP+ | - |
Homo sapiens | 5,10-methenyltetrahydrofolate + NADPH + H+ | - |
? | |
| 1.5.1.15 | 5,10-methylenetetrahydrofolate + NADP+ | - |
Homo sapiens | 5,10-methenyltetrahydrofolate + NADPH + H+ | ? | - |
|
| 1.5.1.15 | 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+ | - |
? | |
| 1.5.1.15 | 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+ | - |
? | |
| 1.5.1.15 | 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+ | - |
? | |
| 1.5.1.15 | 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+ | - |
? | |
| 1.5.1.15 | 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+ | - |
? | |
| 1.5.1.15 | 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+ | - |
? | |
| 1.5.1.15 | 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+ | - |
? | |
| 1.5.1.15 | 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
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 1.5.1.5 | 5,10-CH2-THF dehydrogenase | - |
Homo sapiens |
| 1.5.1.5 | methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase | - |
Homo sapiens |
| 1.5.1.5 | MTHFD2 | - |
Homo sapiens |
| 1.5.1.5 | MTHFD2L | - |
Homo sapiens |
| 1.5.1.15 | 5,10-CH2-THF dehydrogenase | - |
Homo sapiens |
| 1.5.1.15 | methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase | - |
Homo sapiens |
| 1.5.1.15 | MTHFD2 | - |
Homo sapiens |
| 1.5.1.15 | MTHFD2L | - |
Homo sapiens |
| 3.5.4.9 | methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase | - |
Homo sapiens |
| 3.5.4.9 | MTHFD2 | - |
Homo sapiens |
| 3.5.4.9 | MTHFD2L | - |
Homo sapiens |
Turnover Number [1/s]
| EC Number | Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 1.5.1.5 | 1.5 | - |
5,10-methylenetetrahydropteroylglutamate | pH 8.0, 30°C, at saturating concentrations of NADP+ (6.0 mM) | Homo sapiens | |
| 1.5.1.5 | 6.4 | - |
5,10-methylenetetrahydropteroylpentaglutamate | pH 8.0, 30°C, at saturating concentrations of NADP+ (6.0 mM) | Homo sapiens | |
| 1.5.1.5 | 12.4 | - |
5,10-methylenetetrahydropteroylglutamate | pH 8.0, 30°C, at saturating concentrations of NAD+ (1.0 mM) | Homo sapiens | |
| 1.5.1.5 | 15.4 | - |
5,10-methylenetetrahydropteroylpentaglutamate | pH 8.0, 30°C, at saturating concentrations of NAD+ (1.0 mM) | Homo sapiens | |
| 1.5.1.15 | 1.5 | - |
5,10-methylenetetrahydropteroylglutamate | pH 8.0, 30°C, at saturating concentrations of NADP+ (6.0 mM) | Homo sapiens | |
| 1.5.1.15 | 6.4 | - |
5,10-methylenetetrahydropteroylpentaglutamate | pH 8.0, 30°C, at saturating concentrations of NADP+ (6.0 mM) | Homo sapiens | |
| 1.5.1.15 | 12.4 | - |
5,10-methylenetetrahydropteroylglutamate | pH 8.0, 30°C, at saturating concentrations of NAD+ (1.0 mM) | Homo sapiens | |
| 1.5.1.15 | 15.4 | - |
5,10-methylenetetrahydropteroylpentaglutamate | pH 8.0, 30°C, at saturating concentrations of NAD+ (1.0 mM) | Homo sapiens | |
Cofactor
| EC Number | Cofactor | Comment | Organism | Structure |
|---|---|---|---|---|
| 1.5.1.5 | 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 | |
| 1.5.1.5 | 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 | |
| 1.5.1.5 | 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 | |
| 1.5.1.5 | 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 | |
| 1.5.1.15 | 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 | |
| 1.5.1.15 | 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 | |
| 1.5.1.15 | 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 | |
| 1.5.1.15 | 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
| EC Number | General Information | Comment | Organism |
|---|---|---|---|
| 1.5.1.5 | 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 |
| 1.5.1.15 | 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 |
| 3.5.4.9 | metabolism | the enzyme is involved in folate pathway. It is involved in mitochondrial NADPH production | Homo sapiens |
kcat/KM [mM/s]
| EC Number | kcat/KM Value [1/mMs-1] | kcat/KM Value Maximum [1/mMs-1] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 1.5.1.5 | 12 | - |
5,10-methylenetetrahydropteroylglutamate | pH 8.0, 30°C, at saturating concentrations of NADP+ (6.0 mM) | Homo sapiens | |
| 1.5.1.5 | 21 | - |
5,10-methylenetetrahydropteroylpentaglutamate | pH 8.0, 30°C, at saturating concentrations of NADP+ (6.0 mM) | Homo sapiens | |
| 1.5.1.5 | 43 | - |
5,10-methylenetetrahydropteroylpentaglutamate | pH 8.0, 30°C, at saturating concentrations of NAD+ (1.0 mM) | Homo sapiens | |
| 1.5.1.5 | 93 | - |
5,10-methylenetetrahydropteroylglutamate | pH 8.0, 30°C, at saturating concentrations of NAD+ (1.0 mM) | Homo sapiens | |
| 1.5.1.15 | 12 | - |
5,10-methylenetetrahydropteroylglutamate | pH 8.0, 30°C, at saturating concentrations of NADP+ (6.0 mM) | Homo sapiens | |
| 1.5.1.15 | 21 | - |
5,10-methylenetetrahydropteroylpentaglutamate | pH 8.0, 30°C, at saturating concentrations of NADP+ (6.0 mM) | Homo sapiens | |
| 1.5.1.15 | 43 | - |
5,10-methylenetetrahydropteroylpentaglutamate | pH 8.0, 30°C, at saturating concentrations of NAD+ (1.0 mM) | Homo sapiens | |
| 1.5.1.15 | 93 | - |
5,10-methylenetetrahydropteroylglutamate | pH 8.0, 30°C, at saturating concentrations of NAD+ (1.0 mM) | Homo sapiens | |
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