BRENDA - Enzyme Database
show all sequences of 1.5.1.5

Human mitochondrial MTHFD2 is a dual redox cofactor-specific methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase

Shin, M.; Momb, J.; Appling, D.R.; Cancer Metab. 5, 11 (2017)

Data extracted from this reference:

Cloned(Commentary)
Cloned (Commentary)
Organism
6His-tagged enzyme is expressed in Escherichia coli
Homo sapiens
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
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
Commentary
Organism
GeneOntology No.
Textmining
mitochondrion
-
Homo sapiens
5739
-
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
36700
-
-
Homo sapiens
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
ID
5,10-methylenetetrahydrofolate + NADP+
Homo sapiens
-
5,10-methenyltetrahydrofolate + NADPH + H+
-
-
?
Organism
Organism
UniProt
Commentary
Textmining
Homo sapiens
P13995
-
-
Homo sapiens
Q9H903
-
-
Purification (Commentary)
Purification (Commentary)
Organism
-
Homo sapiens
Source Tissue
Source Tissue
Commentary
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
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
Substrate Product ID
5,10-methylenetetrahydrofolate + NADP+
-
756334
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
756334
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
756334
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
756334
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
756334
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
756334
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
756334
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
756334
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
756334
Homo sapiens
5,10-methenyltetrahydropteroylpentaglutamate + NADPH + H+
-
-
-
?
Synonyms
Synonyms
Commentary
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
Commentary
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
Commentary
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
Cloned(Commentary) (protein specific)
Commentary
Organism
6His-tagged enzyme is expressed in Escherichia coli
Homo sapiens
Cofactor (protein specific)
Cofactor
Commentary
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
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
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 (protein specific)
Localization
Commentary
Organism
GeneOntology No.
Textmining
mitochondrion
-
Homo sapiens
5739
-
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
36700
-
-
Homo sapiens
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
ID
5,10-methylenetetrahydrofolate + NADP+
Homo sapiens
-
5,10-methenyltetrahydrofolate + NADPH + H+
-
-
?
Purification (Commentary) (protein specific)
Commentary
Organism
-
Homo sapiens
Source Tissue (protein specific)
Source Tissue
Commentary
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) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
ID
5,10-methylenetetrahydrofolate + NADP+
-
756334
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
756334
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
756334
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
756334
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
756334
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
756334
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
756334
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
756334
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
756334
Homo sapiens
5,10-methenyltetrahydropteroylpentaglutamate + NADPH + H+
-
-
-
?
Turnover Number [1/s] (protein specific)
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
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
General Information
General Information
Commentary
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
General Information (protein specific)
General Information
Commentary
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
Commentary
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
KCat/KM [mM/s] (protein specific)
KCat/KM Value [1/mMs-1]
KCat/KM Value Maximum [1/mMs-1]
Substrate
Commentary
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
Other publictions for EC 1.5.1.5
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Synonyms
Temperature Optimum [°C]
Temperature Range [°C]
Temperature Stability [°C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [°C] (protein specific)
Temperature Range [°C] (protein specific)
Temperature Stability [°C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
755732
Bueno
An assessment of three human ...
Homo sapiens
Acta Crystallogr. Sect. F
75
148-152
2019
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1
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1
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1
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757625
Sah
Utilisation of 10-formyldihyd ...
Escherichia coli, Escherichia coli K12
Microbiology
164
982-991
2018
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1
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1
2
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3
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1
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1
1
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1
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1
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1
2
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1
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4
1
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1
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1
1
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757773
Hitzel
Oxidized phospholipids regula ...
Homo sapiens
Nat. Commun.
9
2292
2018
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1
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1
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1
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1
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1
1
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756334
Shin
Human mitochondrial MTHFD2 is ...
Homo sapiens
Cancer Metab.
5
11
2017
-
-
2
-
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-
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4
2
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2
2
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2
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2
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3
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10
-
5
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4
-
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4
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-
2
4
-
-
-
-
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4
2
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2
2
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2
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3
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10
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4
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2
2
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4
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1
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1
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392324
Paukert
Formyl-methyl-methylenetetrahy ...
Ovis aries
J. Biol. Chem.
251
5104-5111
1976
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2
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3
1
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4
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1
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1
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1
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2
1
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1
1
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392308
Harvey
Regulation in the folate pathw ...
Escherichia coli, Escherichia coli B / ATCC 11303
Adv. Enzyme Regul.
13
99-124
1975
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3
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2
-
177
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2
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2
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392311
O'Brien
Purification and characterizat ...
Moorella thermoacetica
J. Biol. Chem.
248
403-408
1973
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1
2
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1
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3
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1
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1
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1
2
1
1
1
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1
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392319
MacKenzie
Co-purification of three folat ...
Sus scrofa
Biochem. Biophys. Res. Commun.
53
1088-1095
1973
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1
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1
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392328
Yoshida
Comparative study on major pat ...
Bos taurus, Elaphe quadrivirgata, Gallus gallus bankiva, Ovis aries
J. Biochem.
72
1503-1516
1972
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8
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4
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4
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8
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4
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8
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4
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4
8
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4
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392326
Cossins
-
Plant N5,N10-methylenetetrahyd ...
Pisum sativum
Phytochemistry
9
1463-1471
1970
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1
3
3
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1
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3
1
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1
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1
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3
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3
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1
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3
1
1
2
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1
1
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392306
Albrecht
Methylenetetrahydrofolate dehy ...
Enterococcus faecium
J. Bacteriol.
95
1779-1789
1968
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1
5
2
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1
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3
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1
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1
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1
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1
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1
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5
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2
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1
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1
1
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1
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392310
Uyeda
Enzymes of clostridial purine ...
Clostridium cylindrosporum
J. Biol. Chem.
242
4378-4385
1967
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1
1
4
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1
1
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1
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1
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1
1
3
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1
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4
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1
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1
1
3
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1
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392312
Dalal
Purification of 5,10-methylene ...
Salmonella enterica subsp. enterica serovar Typhimurium, Salmonella enterica subsp. enterica serovar Typhimurium LT2
J. Biol. Chem.
242
3636-3640
1967
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1
3
2
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2
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45
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1
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1
2
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1
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1
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1
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1
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2
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1
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2
1
2
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1
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392316
Yeh
Purification and properties of ...
Bos taurus
Biochim. Biophys. Acta
105
279-291
1965
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1
6
3
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1
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1
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1
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1
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1
3
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1
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1
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1
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1
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6
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3
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1
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1
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1
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1
3
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1
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1
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392313
Ramasastri
5,10-Methylenetetrahydrofolic ...
Saccharomyces cerevisiae
J. Biol. Chem.
237
1982-1988
1962
5
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1
5
2
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1
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1
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1
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1
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1
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1
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1
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1
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1
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5
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1
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1
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5
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2
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1
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1
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1
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1
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