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(6R,S)-5,10-methylenetetrahydrofolate + NADP+
5,10-methenyltetrahydrofolate + NADPH + H+
monofunctional enzyme, no methenyltetrahydrofolate cyclohydrolase activity
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-
?
5,10-methylene tetrahydrofolate + NAD+
5,10-methenyl tetrahydrofolate + NADH + H+
-
bifunctional enzyme exhibits dehydrogenase and cyclohydrogenase activities
-
-
r
5,10-methylene tetrahydrofolate + NADP+
5,10-methenyl tetrahydrofolate + NADPH
-
trifunctional enzyme exhibits synthetase, dehydrogenase and cyclohydrolase activities
-
-
r
5,10-methylene tetrahydrofolate + NADP+
5,10-methenyl tetrahydrofolate + NADPH + H+
5,10-methylene tetrahydrofolate + NADP+
5,10-methenyltetrahydrofolate + NADPH
dehydrogenase activity of MTHFD1
-
-
r
5,10-methylene-tetrahydrofolate + NAD+
5,10-methenyl-tetrahydrofolate + NADH
-
combined cofactors NAD+, Mg2+, and phosphate mimic the binding of NADP+ in NADP(+)-dependent dehydrogenase
50-60% channeled to the cyclohydrolase to form formyltetrahydrofolate
-
r
5,10-methylene-tetrahydrofolate + NADP+
5,10-methenyl-tetrahydrofolate + NADPH + H+
5,10-methylenetetrahydrofolate + NAD+
5,10-methenyltetrahydrofolate + NADH + H+
5,10-methylenetetrahydrofolate + NADP+
5,10-methenyltetrahydrofolate + NADPH + H+
5,10-methylenetetrahydropteroate + NADP+
5,10-methenyltetrahydropteroate + NADPH
-
-
-
-
?
5,10-methylenetetrahydropteroylglutamate + NAD+
5,10-methenyltetrahydropteroylglutamate + NADH + H+
5,10-methylenetetrahydropteroylglutamate + NADP+
5,10-methenyltetrahydropteroylglutamate + NADPH + H+
5,10-methylenetetrahydropteroylpentaglutamate + NAD+
5,10-methenyltetrahydropteroylpentaglutamate + NADH + H+
5,10-methylenetetrahydropteroylpentaglutamate + NADP+
5,10-methenyltetrahydropteroylpentaglutamate + NADPH + H+
5,10-methylenetetrahydropteroylpoly-L-glutamate + NADP+
5,10-methenyltetrahydropteroylpoly-L-glutamate + NADPH + H+
5,10-methylenetetrahydropteroyltriglutamate + NADP+
5,10-methenyltetrahydropteroyltriglutamate + NADPH
DL-tetrahydrofolic acid + NADP+
?
-
-
-
-
?
DL-tetrahydropteroyl-L-aspartate + NADP+
?
-
-
-
-
?
formaldehyde + NADP+
?
-
-
-
-
?
tetrahydropteroylglutamic acid + NADP+
?
-
-
-
-
?
tetrahydropteroylpentaglutamate + NADP+
?
-
-
-
-
?
additional information
?
-
5,10-methylene tetrahydrofolate + NADP+
5,10-methenyl tetrahydrofolate + NADPH + H+
-
trifunctional enzyme exhibits synthetase, dehydrogenase and cyclohydrogenase activities
-
-
r
5,10-methylene tetrahydrofolate + NADP+
5,10-methenyl tetrahydrofolate + NADPH + H+
-
DH activity
-
-
r
5,10-methylene-tetrahydrofolate + NADP+
5,10-methenyl-tetrahydrofolate + NADPH + H+
-
-
the cyclohydrolase forms formyltetrahydrofolate
-
r
5,10-methylene-tetrahydrofolate + NADP+
5,10-methenyl-tetrahydrofolate + NADPH + H+
-
-
10-formyl tetrahydrofolate (10-CHO-THF)is the product of subsequently active methenyltetrahydrofolate cyclohydrolase, ATP-dependent formate-tetrahydrofolate ligase catalyzes an alternative one step reaction from tetrahydrofolate + format to 10-formyl tetrahydrofolate
-
?
5,10-methylenetetrahydrofolate + NAD+
5,10-methenyltetrahydrofolate + NADH + H+
-
-
-
-
?
5,10-methylenetetrahydrofolate + NAD+
5,10-methenyltetrahydrofolate + NADH + H+
-
-
-
r
5,10-methylenetetrahydrofolate + NAD+
5,10-methenyltetrahydrofolate + NADH + H+
-
-
-
r
5,10-methylenetetrahydrofolate + NAD+
5,10-methenyltetrahydrofolate + NADH + H+
-
-
-
-
r
5,10-methylenetetrahydrofolate + NAD+
5,10-methenyltetrahydrofolate + NADH + H+
-
-
-
r
5,10-methylenetetrahydrofolate + NADP+
5,10-methenyltetrahydrofolate + NADPH + H+
-
-
-
-
?
5,10-methylenetetrahydrofolate + NADP+
5,10-methenyltetrahydrofolate + NADPH + H+
-
-
-
-
?
5,10-methylenetetrahydrofolate + NADP+
5,10-methenyltetrahydrofolate + NADPH + H+
-
-
-
-
?
5,10-methylenetetrahydrofolate + NADP+
5,10-methenyltetrahydrofolate + NADPH + H+
-
-
-
r
5,10-methylenetetrahydrofolate + NADP+
5,10-methenyltetrahydrofolate + NADPH + H+
-
-
-
?
5,10-methylenetetrahydrofolate + NADP+
5,10-methenyltetrahydrofolate + NADPH + H+
-
-
-
?
5,10-methylenetetrahydrofolate + NADP+
5,10-methenyltetrahydrofolate + NADPH + H+
-
-
-
-
?
5,10-methylenetetrahydrofolate + NADP+
5,10-methenyltetrahydrofolate + NADPH + H+
-
-
-
?
5,10-methylenetetrahydrofolate + NADP+
5,10-methenyltetrahydrofolate + NADPH + H+
-
-
-
-
?
5,10-methylenetetrahydrofolate + NADP+
5,10-methenyltetrahydrofolate + NADPH + H+
-
-
-
?
5,10-methylenetetrahydrofolate + NADP+
5,10-methenyltetrahydrofolate + NADPH + H+
the enzyme is involved in the folate recycling pathway
-
-
?
5,10-methylenetetrahydrofolate + NADP+
5,10-methenyltetrahydrofolate + NADPH + H+
-
-
-
-
?
5,10-methylenetetrahydrofolate + NADP+
5,10-methenyltetrahydrofolate + NADPH + H+
-
-
-
?
5,10-methylenetetrahydrofolate + NADP+
5,10-methenyltetrahydrofolate + NADPH + H+
the enzyme is involved in the folate recycling pathway
-
-
?
5,10-methylenetetrahydrofolate + NADP+
5,10-methenyltetrahydrofolate + NADPH + H+
-
-
-
-
?
5,10-methylenetetrahydrofolate + NADP+
5,10-methenyltetrahydrofolate + NADPH + H+
-
-
-
-
?
5,10-methylenetetrahydrofolate + NADP+
5,10-methenyltetrahydrofolate + NADPH + H+
-
-
-
-
r
5,10-methylenetetrahydrofolate + NADP+
5,10-methenyltetrahydrofolate + NADPH + H+
-
-
-
?
5,10-methylenetetrahydrofolate + NADP+
5,10-methenyltetrahydrofolate + NADPH + H+
-
-
-
?
5,10-methylenetetrahydrofolate + NADP+
5,10-methenyltetrahydrofolate + NADPH + H+
-
deuterated folate substrate also
-
-
?
5,10-methylenetetrahydrofolate + NADP+
5,10-methenyltetrahydrofolate + NADPH + H+
-
-
-
-
?
5,10-methylenetetrahydrofolate + NADP+
5,10-methenyltetrahydrofolate + NADPH + H+
-
-
-
-
?
5,10-methylenetetrahydrofolate + NADP+
5,10-methenyltetrahydrofolate + NADPH + H+
-
-
-
r
5,10-methylenetetrahydrofolate + NADP+
5,10-methenyltetrahydrofolate + NADPH + H+
-
-
-
r
5,10-methylenetetrahydrofolate + NADP+
5,10-methenyltetrahydrofolate + NADPH + H+
-
-
-
?
5,10-methylenetetrahydrofolate + NADP+
5,10-methenyltetrahydrofolate + NADPH + H+
-
-
-
-
?
5,10-methylenetetrahydrofolate + NADP+
5,10-methenyltetrahydrofolate + NADPH + H+
-
-
-
-
?
5,10-methylenetetrahydrofolate + NADP+
5,10-methenyltetrahydrofolate + NADPH + H+
-
-
-
r
5,10-methylenetetrahydrofolate + NADP+
5,10-methenyltetrahydrofolate + NADPH + H+
-
-
-
r
5,10-methylenetetrahydrofolate + NADP+
5,10-methenyltetrahydrofolate + NADPH + H+
-
-
-
-
?
5,10-methylenetetrahydrofolate + NADP+
5,10-methenyltetrahydrofolate + NADPH + H+
-
-
-
-
?
5,10-methylenetetrahydrofolate + NADP+
5,10-methenyltetrahydrofolate + NADPH + H+
-
-
-
-
?
5,10-methylenetetrahydrofolate + NADP+
5,10-methenyltetrahydrofolate + NADPH + H+
-
-
-
-
?
5,10-methylenetetrahydrofolate + NADP+
5,10-methenyltetrahydrofolate + NADPH + H+
-
-
-
r
5,10-methylenetetrahydrofolate + NADP+
5,10-methenyltetrahydrofolate + NADPH + H+
-
-
-
-
?
5,10-methylenetetrahydrofolate + NADP+
5,10-methenyltetrahydrofolate + NADPH + H+
-
-
-
?
5,10-methylenetetrahydrofolate + NADP+
5,10-methenyltetrahydrofolate + NADPH + H+
-
-
-
-
?
5,10-methylenetetrahydrofolate + NADP+
5,10-methenyltetrahydrofolate + NADPH + H+
-
-
-
-
?
5,10-methylenetetrahydrofolate + NADP+
5,10-methenyltetrahydrofolate + NADPH + H+
-
-
-
-
?
5,10-methylenetetrahydrofolate + NADP+
5,10-methenyltetrahydrofolate + NADPH + H+
-
-
-
?
5,10-methylenetetrahydropteroylglutamate + NAD+
5,10-methenyltetrahydropteroylglutamate + NADH + H+
NAD+-dependent dehydrogenase activity of MTHFD2 is 8.5fold higher than its NADP+-dependent activity
-
-
?
5,10-methylenetetrahydropteroylglutamate + NAD+
5,10-methenyltetrahydropteroylglutamate + NADH + H+
NAD+-dependent dehydrogenase activity of MTHFD2L is 3.4fold higher than its NADP+-dependent activity under saturating substrate conditions
-
-
?
5,10-methylenetetrahydropteroylglutamate + NADP+
5,10-methenyltetrahydropteroylglutamate + NADPH + H+
NAD+-dependent dehydrogenase activity of MTHFD2 is 8.5fold higher than its NADP+-dependent activity
-
-
?
5,10-methylenetetrahydropteroylglutamate + NADP+
5,10-methenyltetrahydropteroylglutamate + NADPH + H+
NAD+-dependent dehydrogenase activity of MTHFD2L is 3.4fold higher than its NADP+-dependent activity under saturating substrate conditions
-
-
?
5,10-methylenetetrahydropteroylpentaglutamate + NAD+
5,10-methenyltetrahydropteroylpentaglutamate + NADH + H+
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
-
-
?
5,10-methylenetetrahydropteroylpentaglutamate + NAD+
5,10-methenyltetrahydropteroylpentaglutamate + NADH + H+
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
-
-
?
5,10-methylenetetrahydropteroylpentaglutamate + NADP+
5,10-methenyltetrahydropteroylpentaglutamate + NADPH + H+
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
-
-
?
5,10-methylenetetrahydropteroylpentaglutamate + NADP+
5,10-methenyltetrahydropteroylpentaglutamate + NADPH + H+
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
-
-
?
5,10-methylenetetrahydropteroylpoly-L-glutamate + NADP+
5,10-methenyltetrahydropteroylpoly-L-glutamate + NADPH + H+
-
-
-
?
5,10-methylenetetrahydropteroylpoly-L-glutamate + NADP+
5,10-methenyltetrahydropteroylpoly-L-glutamate + NADPH + H+
-
-
-
?
5,10-methylenetetrahydropteroyltriglutamate + NADP+
5,10-methenyltetrahydropteroyltriglutamate + NADPH
-
-
-
-
?
5,10-methylenetetrahydropteroyltriglutamate + NADP+
5,10-methenyltetrahydropteroyltriglutamate + NADPH
-
-
-
-
?
additional information
?
-
-
the recombinant Bombyx mori MTHFD (bmMTHFD) recognizes 5,10-methylenetetrahydrofolate and 5,10-methenyltetrahydrofolate as substrates in the presence of NADP+ as well as NAD+
-
-
-
additional information
?
-
(MTHFD1) is a trifunctional enzyme that interconverts tetrahydrofolate derivatives for nucleotide synthesis
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-
?
additional information
?
-
-
dehydrogenase and cyclohydrogenase activities are contained in the single bifunctional protein DHCH1
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-
?
additional information
?
-
MTHFD2L catalyzes the oxidation of 5,10-methylenetetrahydrofolate (CH2-THF) in adult mammalian mitochondria. Enzyme MTHFD2L is bifunctional, possessing both methylenetetrahydrofolate dehydrogenase and methenyltetrahydrofolate cyclohydrolase activities, cf. EC 3.5.4.9
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-
?
additional information
?
-
-
MTHFD2L catalyzes the oxidation of 5,10-methylenetetrahydrofolate (CH2-THF) in adult mammalian mitochondria. Enzyme MTHFD2L is bifunctional, possessing both methylenetetrahydrofolate dehydrogenase and methenyltetrahydrofolate cyclohydrolase activities, cf. EC 3.5.4.9
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-
?
additional information
?
-
enzyme MTHFD2Luses the mono- and polyglutamylated forms of 5,10-methylenetetrahydrofolate with similar catalytic efficiencies
-
-
?
additional information
?
-
-
enzyme MTHFD2Luses the mono- and polyglutamylated forms of 5,10-methylenetetrahydrofolate with similar catalytic efficiencies
-
-
?
additional information
?
-
MTHFD2L catalyzes the oxidation of 5,10-methylenetetrahydrofolate (CH2-THF) in adult mammalian mitochondria. Enzyme MTHFD2L is bifunctional, possessing both methylenetetrahydrofolate dehydrogenase and methenyltetrahydrofolate cyclohydrolase activities, cf. EC 3.5.4.9
-
-
?
additional information
?
-
enzyme MTHFD2Luses the mono- and polyglutamylated forms of 5,10-methylenetetrahydrofolate with similar catalytic efficiencies
-
-
?
additional information
?
-
MTHFD2L catalyzes the oxidation of 5,10-methylenetetrahydrofolate in adult mammalian mitochondria. Enzyme MTHFD2L is bifunctional, possessing both methylenetetrahydrofolate dehydrogenase and methenyltetrahydrofolate cyclohydrolase activities, cf. EC 3.5.4.9
-
-
?
additional information
?
-
enzyme MTHFD2L uses the mono- and polyglutamylated forms of 5,10-methylenetetrahydrofolate with similar catalytic efficiencies
-
-
?
additional information
?
-
-
the presence of cytoplasmic and mitochondrial isoforms of a trifunctional dehydrogenase-cyclohydrolase-synthetase support a model wherin the mitochondria can produce fromate which can be used by the cytoplasmic enzymes for the synthesis of purins and for methylation reactions
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-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
5,10-methylene tetrahydrofolate + NAD+
5,10-methenyl tetrahydrofolate + NADH + H+
-
bifunctional enzyme exhibits dehydrogenase and cyclohydrogenase activities
-
-
r
5,10-methylene tetrahydrofolate + NADP+
5,10-methenyl tetrahydrofolate + NADPH
-
trifunctional enzyme exhibits synthetase, dehydrogenase and cyclohydrolase activities
-
-
r
5,10-methylene tetrahydrofolate + NADP+
5,10-methenyl tetrahydrofolate + NADPH + H+
5,10-methylene tetrahydrofolate + NADP+
5,10-methenyltetrahydrofolate + NADPH
dehydrogenase activity of MTHFD1
-
-
r
5,10-methylene-tetrahydrofolate + NAD+
5,10-methenyl-tetrahydrofolate + NADH
-
combined cofactors NAD+, Mg2+, and phosphate mimic the binding of NADP+ in NADP(+)-dependent dehydrogenase
50-60% channeled to the cyclohydrolase to form formyltetrahydrofolate
-
r
5,10-methylene-tetrahydrofolate + NADP+
5,10-methenyl-tetrahydrofolate + NADPH + H+
5,10-methylenetetrahydrofolate + NAD+
5,10-methenyltetrahydrofolate + NADH + H+
5,10-methylenetetrahydrofolate + NADP+
5,10-methenyltetrahydrofolate + NADPH + H+
additional information
?
-
5,10-methylene tetrahydrofolate + NADP+
5,10-methenyl tetrahydrofolate + NADPH + H+
-
trifunctional enzyme exhibits synthetase, dehydrogenase and cyclohydrogenase activities
-
-
r
5,10-methylene tetrahydrofolate + NADP+
5,10-methenyl tetrahydrofolate + NADPH + H+
-
DH activity
-
-
r
5,10-methylene-tetrahydrofolate + NADP+
5,10-methenyl-tetrahydrofolate + NADPH + H+
-
-
the cyclohydrolase forms formyltetrahydrofolate
-
r
5,10-methylene-tetrahydrofolate + NADP+
5,10-methenyl-tetrahydrofolate + NADPH + H+
-
-
10-formyl tetrahydrofolate (10-CHO-THF)is the product of subsequently active methenyltetrahydrofolate cyclohydrolase, ATP-dependent formate-tetrahydrofolate ligase catalyzes an alternative one step reaction from tetrahydrofolate + format to 10-formyl tetrahydrofolate
-
?
5,10-methylenetetrahydrofolate + NAD+
5,10-methenyltetrahydrofolate + NADH + H+
-
-
-
-
?
5,10-methylenetetrahydrofolate + NAD+
5,10-methenyltetrahydrofolate + NADH + H+
-
-
-
r
5,10-methylenetetrahydrofolate + NAD+
5,10-methenyltetrahydrofolate + NADH + H+
-
-
-
r
5,10-methylenetetrahydrofolate + NAD+
5,10-methenyltetrahydrofolate + NADH + H+
-
-
-
r
5,10-methylenetetrahydrofolate + NADP+
5,10-methenyltetrahydrofolate + NADPH + H+
-
-
-
-
?
5,10-methylenetetrahydrofolate + NADP+
5,10-methenyltetrahydrofolate + NADPH + H+
-
-
-
-
?
5,10-methylenetetrahydrofolate + NADP+
5,10-methenyltetrahydrofolate + NADPH + H+
-
-
-
r
5,10-methylenetetrahydrofolate + NADP+
5,10-methenyltetrahydrofolate + NADPH + H+
-
-
-
?
5,10-methylenetetrahydrofolate + NADP+
5,10-methenyltetrahydrofolate + NADPH + H+
-
-
-
?
5,10-methylenetetrahydrofolate + NADP+
5,10-methenyltetrahydrofolate + NADPH + H+
-
-
-
-
?
5,10-methylenetetrahydrofolate + NADP+
5,10-methenyltetrahydrofolate + NADPH + H+
-
-
-
?
5,10-methylenetetrahydrofolate + NADP+
5,10-methenyltetrahydrofolate + NADPH + H+
-
-
-
-
?
5,10-methylenetetrahydrofolate + NADP+
5,10-methenyltetrahydrofolate + NADPH + H+
the enzyme is involved in the folate recycling pathway
-
-
?
5,10-methylenetetrahydrofolate + NADP+
5,10-methenyltetrahydrofolate + NADPH + H+
-
-
-
-
?
5,10-methylenetetrahydrofolate + NADP+
5,10-methenyltetrahydrofolate + NADPH + H+
the enzyme is involved in the folate recycling pathway
-
-
?
5,10-methylenetetrahydrofolate + NADP+
5,10-methenyltetrahydrofolate + NADPH + H+
-
-
-
-
?
5,10-methylenetetrahydrofolate + NADP+
5,10-methenyltetrahydrofolate + NADPH + H+
-
-
-
-
?
5,10-methylenetetrahydrofolate + NADP+
5,10-methenyltetrahydrofolate + NADPH + H+
-
-
-
-
r
5,10-methylenetetrahydrofolate + NADP+
5,10-methenyltetrahydrofolate + NADPH + H+
-
-
-
?
5,10-methylenetetrahydrofolate + NADP+
5,10-methenyltetrahydrofolate + NADPH + H+
-
-
-
?
5,10-methylenetetrahydrofolate + NADP+
5,10-methenyltetrahydrofolate + NADPH + H+
-
-
-
-
?
5,10-methylenetetrahydrofolate + NADP+
5,10-methenyltetrahydrofolate + NADPH + H+
-
-
-
-
?
5,10-methylenetetrahydrofolate + NADP+
5,10-methenyltetrahydrofolate + NADPH + H+
-
-
-
r
5,10-methylenetetrahydrofolate + NADP+
5,10-methenyltetrahydrofolate + NADPH + H+
-
-
-
r
5,10-methylenetetrahydrofolate + NADP+
5,10-methenyltetrahydrofolate + NADPH + H+
-
-
-
?
5,10-methylenetetrahydrofolate + NADP+
5,10-methenyltetrahydrofolate + NADPH + H+
-
-
-
-
?
5,10-methylenetetrahydrofolate + NADP+
5,10-methenyltetrahydrofolate + NADPH + H+
-
-
-
-
?
5,10-methylenetetrahydrofolate + NADP+
5,10-methenyltetrahydrofolate + NADPH + H+
-
-
-
r
5,10-methylenetetrahydrofolate + NADP+
5,10-methenyltetrahydrofolate + NADPH + H+
-
-
-
r
5,10-methylenetetrahydrofolate + NADP+
5,10-methenyltetrahydrofolate + NADPH + H+
-
-
-
-
?
5,10-methylenetetrahydrofolate + NADP+
5,10-methenyltetrahydrofolate + NADPH + H+
-
-
-
-
?
5,10-methylenetetrahydrofolate + NADP+
5,10-methenyltetrahydrofolate + NADPH + H+
-
-
-
-
?
5,10-methylenetetrahydrofolate + NADP+
5,10-methenyltetrahydrofolate + NADPH + H+
-
-
-
-
?
5,10-methylenetetrahydrofolate + NADP+
5,10-methenyltetrahydrofolate + NADPH + H+
-
-
-
r
5,10-methylenetetrahydrofolate + NADP+
5,10-methenyltetrahydrofolate + NADPH + H+
-
-
-
-
?
5,10-methylenetetrahydrofolate + NADP+
5,10-methenyltetrahydrofolate + NADPH + H+
-
-
-
?
5,10-methylenetetrahydrofolate + NADP+
5,10-methenyltetrahydrofolate + NADPH + H+
-
-
-
-
?
5,10-methylenetetrahydrofolate + NADP+
5,10-methenyltetrahydrofolate + NADPH + H+
-
-
-
-
?
5,10-methylenetetrahydrofolate + NADP+
5,10-methenyltetrahydrofolate + NADPH + H+
-
-
-
?
additional information
?
-
(MTHFD1) is a trifunctional enzyme that interconverts tetrahydrofolate derivatives for nucleotide synthesis
-
-
?
additional information
?
-
-
dehydrogenase and cyclohydrogenase activities are contained in the single bifunctional protein DHCH1
-
-
?
additional information
?
-
MTHFD2L catalyzes the oxidation of 5,10-methylenetetrahydrofolate (CH2-THF) in adult mammalian mitochondria. Enzyme MTHFD2L is bifunctional, possessing both methylenetetrahydrofolate dehydrogenase and methenyltetrahydrofolate cyclohydrolase activities, cf. EC 3.5.4.9
-
-
?
additional information
?
-
-
MTHFD2L catalyzes the oxidation of 5,10-methylenetetrahydrofolate (CH2-THF) in adult mammalian mitochondria. Enzyme MTHFD2L is bifunctional, possessing both methylenetetrahydrofolate dehydrogenase and methenyltetrahydrofolate cyclohydrolase activities, cf. EC 3.5.4.9
-
-
?
additional information
?
-
MTHFD2L catalyzes the oxidation of 5,10-methylenetetrahydrofolate (CH2-THF) in adult mammalian mitochondria. Enzyme MTHFD2L is bifunctional, possessing both methylenetetrahydrofolate dehydrogenase and methenyltetrahydrofolate cyclohydrolase activities, cf. EC 3.5.4.9
-
-
?
additional information
?
-
MTHFD2L catalyzes the oxidation of 5,10-methylenetetrahydrofolate in adult mammalian mitochondria. Enzyme MTHFD2L is bifunctional, possessing both methylenetetrahydrofolate dehydrogenase and methenyltetrahydrofolate cyclohydrolase activities, cf. EC 3.5.4.9
-
-
?
additional information
?
-
-
the presence of cytoplasmic and mitochondrial isoforms of a trifunctional dehydrogenase-cyclohydrolase-synthetase support a model wherin the mitochondria can produce fromate which can be used by the cytoplasmic enzymes for the synthesis of purins and for methylation reactions
-
-
?
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Acidosis
Increased activity of renal glycine-cleavage-enzyme complex in metabolic acidosis.
Anemia, Megaloblastic
Precision Molecular Diagnosis Defines Specific Therapy in Combined Immunodeficiency with Megaloblastic Anemia Secondary to MTHFD1 Deficiency.
Anemia, Megaloblastic
Update and new concepts in vitamin responsive disorders of folate transport and metabolism.
Anencephaly
Neural tube defects and folate pathway genes: family-based association tests of gene-gene and gene-environment interactions.
Angina, Stable
Methylenetetrahydrofolate Dehydrogenase 1 Polymorphisms Modify the Associations of Plasma Glycine and Serine With Risk of Acute Myocardial Infarction in Patients With Stable Angina Pectoris in WENBIT (Western Norway B Vitamin Intervention Trial).
Atherosclerosis
[Features of allele polymorphism of genes involved in homocysteine and folate metabolism in patients with atherosclerosis of the lower extremity arteries]
Atypical Hemolytic Uremic Syndrome
Update and new concepts in vitamin responsive disorders of folate transport and metabolism.
Breast Neoplasms
Folate-mediated one-carbon metabolism: a targeting strategy in cancer therapy.
Breast Neoplasms
Increased MTHFD2 expression is associated with poor prognosis in breast cancer.
Carcinogenesis
Methylenetetrahydrofolate Dehydrogenase 1 Silencing Expedites the Apoptosis of Non-Small Cell Lung Cancer Cells via Modulating DNA Methylation.
Carcinoma
High Expression of Methylenetetrahydrofolate Dehydrogenase 2 (MTHFD2) in Esophageal Squamous Cell Carcinoma and its Clinical Prognostic Significance.
Carcinoma
Methylenetetrahydrofolate Dehydrogenase 1 (MTHFD1) is Underexpressed in Clear Cell Renal Cell Carcinoma Tissue and Transfection and Overexpression in Caki-1 Cells Inhibits Cell Proliferation and Increases Apoptosis.
Carcinoma
MTHFD2 Overexpression Predicts Poor Prognosis in Renal Cell Carcinoma and is Associated with Cell Proliferation and Vimentin-Modulated Migration and Invasion.
Carcinoma
The Prognostic Significance of Immune-Related Metabolic Enzyme MTHFD2 in Head and Neck Squamous Cell Carcinoma.
Carcinoma, Endometrioid
Origin of clear cell carcinoma: nature or nurture?
Carcinoma, Hepatocellular
Methylenetetrahydrofolate dehydrogenase 2 overexpression is associated with tumor aggressiveness and poor prognosis in hepatocellular carcinoma.
Carcinoma, Hepatocellular
[The preliminary study on the function of methylenetetrahydrofolate dehydrogenase 2 in hepatocellular carcinoma].
Carcinoma, Non-Small-Cell Lung
Methylenetetrahydrofolate Dehydrogenase 1 Silencing Expedites the Apoptosis of Non-Small Cell Lung Cancer Cells via Modulating DNA Methylation.
Carcinoma, Renal Cell
Methylenetetrahydrofolate Dehydrogenase 1 (MTHFD1) is Underexpressed in Clear Cell Renal Cell Carcinoma Tissue and Transfection and Overexpression in Caki-1 Cells Inhibits Cell Proliferation and Increases Apoptosis.
Carcinoma, Renal Cell
MTHFD2 Overexpression Predicts Poor Prognosis in Renal Cell Carcinoma and is Associated with Cell Proliferation and Vimentin-Modulated Migration and Invasion.
Carcinoma, Squamous Cell
The Prognostic Significance of Immune-Related Metabolic Enzyme MTHFD2 in Head and Neck Squamous Cell Carcinoma.
Colorectal Neoplasms
The importance of mitochondrial folate enzymes in human colorectal cancer.
Congenital Abnormalities
Low Dietary Folate Interacts with MTHFD1 Synthetase Deficiency in Mice, a Model for the R653Q Variant, to Increase Incidence of Developmental Delays and Defects.
Down Syndrome
Combined folate gene MTHFD and TC polymorphisms as maternal risk factors for Down syndrome in China.
Down Syndrome
Methylenetetrahydrofolate dehydrogenase (MTHFD) enzyme polymorphism as a maternal risk factor for trisomy 21: a clinical study.
Esophageal Squamous Cell Carcinoma
High Expression of Methylenetetrahydrofolate Dehydrogenase 2 (MTHFD2) in Esophageal Squamous Cell Carcinoma and its Clinical Prognostic Significance.
Glioma
Expression and Prognostic Value Identification of Methylenetetrahydrofolate Dehydrogenase 2 (MTHFD2) in Brain Low-Grade Glioma.
Heart Defects, Congenital
Relationship between polymorphism of methylenetetrahydrofolate dehydrogenase and congenital heart defect.
Heart Diseases
MTHFR c.1793G>A polymorphism is associated with congenital cardiac disease in a Chinese population.
Hernia, Umbilical
Folate-related genes and omphalocele.
Hypertension
Investigation of homocysteine-pathway-related variants in essential hypertension.
Hypertension
Significant Association of Methylenetetrahydrofolate dehydrogenase 1 Promoter Hypomethylation with Stroke in a Chinese Population with Primary Hypertension.
Laryngeal Neoplasms
Polymorphic variants of folate metabolism genes and the risk of laryngeal cancer.
Leukemia, Myeloid, Acute
miR-92a Inhibits Proliferation and Induces Apoptosis by Regulating Methylenetetrahydrofolate Dehydrogenase 2 (MTHFD2) Expression in Acute Myeloid Leukemia.
Lung Neoplasms
Methylenetetrahydrofolate Dehydrogenase 1 Silencing Expedites the Apoptosis of Non-Small Cell Lung Cancer Cells via Modulating DNA Methylation.
Lung Neoplasms
Modulating redox homeostasis and cellular reprogramming through inhibited methylenetetrahydrofolate dehydrogenase 2 enzymatic activities in lung cancer.
Lung Neoplasms
Prognostic significance of folate metabolism polymorphisms for lung cancer.
Meningomyelocele
Neural tube defects and folate pathway genes: family-based association tests of gene-gene and gene-environment interactions.
Myocardial Infarction
Methylenetetrahydrofolate Dehydrogenase 1 Polymorphisms Modify the Associations of Plasma Glycine and Serine With Risk of Acute Myocardial Infarction in Patients With Stable Angina Pectoris in WENBIT (Western Norway B Vitamin Intervention Trial).
Neoplasms
Association of methylenetetrahydrofolate dehydrogenase 1 polymorphisms with cancer: a meta-analysis.
Neoplasms
Detection and characterisation of novel alternative splicing variants of the mitochondrial folate enzyme MTHFD2.
Neoplasms
Drug discovery of anticancer drugs targeting methylenetetrahydrofolate dehydrogenase 2.
Neoplasms
Folate enzymes in Ehrlich ascites carcinoma-bearing mice.
Neoplasms
Folate-mediated one-carbon metabolism: a targeting strategy in cancer therapy.
Neoplasms
High Expression of Methylenetetrahydrofolate Dehydrogenase 2 (MTHFD2) in Esophageal Squamous Cell Carcinoma and its Clinical Prognostic Significance.
Neoplasms
KRAS mutation status is associated with enhanced dependency on folate metabolism pathways in Non Small Cell Lung Cancer cells.
Neoplasms
Methylenetetrahydrofolate dehydrogenase 2 overexpression is associated with tumor aggressiveness and poor prognosis in hepatocellular carcinoma.
Neoplasms
Mitochondrial Methylenetetrahydrofolate Dehydrogenase (MTHFD2) Overexpression Is Associated with Tumor Cell Proliferation and Is a Novel Target for Drug Development.
Neoplasms
Modulating redox homeostasis and cellular reprogramming through inhibited methylenetetrahydrofolate dehydrogenase 2 enzymatic activities in lung cancer.
Neoplasms
MTHFD2 promotes tumorigenesis and metastasis in lung adenocarcinoma by regulating AKT/GSK-3?/?-catenin signalling.
Neoplasms
mTORC1 induces purine synthesis through control of the mitochondrial tetrahydrofolate cycle.
Neoplasms
NAD- and NADPH-Contributing Enzymes as Therapeutic Targets in Cancer: An Overview.
Neoplasms
NAD-dependent methylenetetrahydrofolate dehydrogenase-methenyltetrahydrofolate cyclohydrolase from ascites tumor cells. Purification and properties.
Neoplasms
p53 deficiency induces MTHFD2 transcription to promote cell proliferation and restrain DNA damage.
Neoplasms
Structure-Based Design and Synthesis of an Isozyme-Selective MTHFD2 Inhibitor with a Tricyclic Coumarin Scaffold.
Neoplasms
The folate cycle enzyme MTHFD2 induces cancer immune evasion through PD-L1 up-regulation.
Neoplasms
The folate-coupled enzyme MTHFD2 is a nuclear protein and promotes cell proliferation.
Neural Tube Defects
Association between MTHFD1 G1958A polymorphism and neural tube defects susceptibility: a meta-analysis.
Neural Tube Defects
Deletion of the neural tube defect-associated gene
Neural Tube Defects
MTHFD1 polymorphism as maternal risk for neural tube defects: a meta-analysis.
Neural Tube Defects
Paternal transmission of MTHFD1 G1958A variant predisposes to neural tube defects in the offspring.
Neural Tube Defects
Polymorphisms in MTHFD1 Gene and Susceptibility to Neural Tube Defects: A Case-Control Study in a Chinese Han Population with Relatively Low Folate Levels.
Ovarian Neoplasms
Lack of association between MTHFD1 G401A polymorphism and ovarian cancer susceptibility.
Pregnancy Complications
Altered folate metabolism modifies cell proliferation and progesterone secretion in human placental choriocarcinoma JEG-3 cells.
Prostatic Neoplasms
Lack of association between methylenetetrahydrofolate dehydrogenase 1 G1958A polymorphism and prostate cancer risk: a meta-analysis.
Severe Combined Immunodeficiency
Precision Molecular Diagnosis Defines Specific Therapy in Combined Immunodeficiency with Megaloblastic Anemia Secondary to MTHFD1 Deficiency.
Severe Combined Immunodeficiency
Update and new concepts in vitamin responsive disorders of folate transport and metabolism.
Small Cell Lung Carcinoma
Prognostic significance of folate metabolism polymorphisms for lung cancer.
Spinal Dysraphism
The methylenetetrahydrofolate dehydrogenase (MTHFD1) 1958G>A variant is not associated with spina bifida risk in the Dutch population.
Squamous Cell Carcinoma of Head and Neck
The Prognostic Significance of Immune-Related Metabolic Enzyme MTHFD2 in Head and Neck Squamous Cell Carcinoma.
Stroke
A comprehensive association analysis between homocysteine metabolic pathway gene methylation and ischemic stroke in a Chinese hypertensive population.
Stroke
Significant Association of Methylenetetrahydrofolate dehydrogenase 1 Promoter Hypomethylation with Stroke in a Chinese Population with Primary Hypertension.
Urinary Bladder Neoplasms
Expression and Role of Methylenetetrahydrofolate Dehydrogenase 1 Like (MTHFD1L) in Bladder Cancer.
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0.228
(6R,S)-5,10-methylenetetrahydrofolate
pH 7.6, temperature not specified in the publication
0.068 - 0.302
5,10-methenyltetrahydrofolate
0.12
5,10-methylene-tetrahydrofolate
0.0011 - 4.76
5,10-methylenetetrahydrofolate
1.6
5,10-Methylenetetrahydropteroate
-
-
0.123 - 0.133
5,10-methylenetetrahydropteroylglutamate
0.302 - 0.359
5,10-methylenetetrahydropteroylpentaglutamate
0.04 - 0.153
5,10-methylenetetrahydropteroylpoly-L-glutamate
0.0088
5,10-methylenetetrahydropteroyltriglutamate
-
-
0.21
DL-tetrahydrofolic acid
-
-
0.0077
tetrahydropteroylglutamic acid
-
-
0.021
tetrahydropteroylmonoglutamate
-
-
0.025
Tetrahydropteroylpentaglutamate
-
-
additional information
additional information
-
0.068
5,10-methenyltetrahydrofolate
pH 7.6, 30°C, mutant enzyme G122D
0.104
5,10-methenyltetrahydrofolate
pH 7.6, 30°C, mutant enzyme D121A
0.205
5,10-methenyltetrahydrofolate
pH 7.6, 30°C, mutant enzyme K54S
0.279
5,10-methenyltetrahydrofolate
pH 7.6, 30°C, wild-type enzyme
0.302
5,10-methenyltetrahydrofolate
pH 7.6, 30°C, mutant enzyme C58Y
0.12
5,10-methylene-tetrahydrofolate
-
25 mM MOPS pH 7.3, 2.5 mM formaldehyde, 1 mM NADP+, 30 mM 2-mercaptoethanol, 27°C
0.12
5,10-methylene-tetrahydrofolate
-
recombinant DHCH1
0.0011
5,10-methylenetetrahydrofolate
-
cofactor: NADP+
0.002
5,10-methylenetetrahydrofolate
-
-
0.008
5,10-methylenetetrahydrofolate
-
deuterated, NADP+-dependent bifunctional dehydrogenase-cyclohydrolase domain of the cytoplasmic trifunctional enzyme
0.009
5,10-methylenetetrahydrofolate
-
NADP+-dependent bifunctional dehydrogenase-cyclohydrolase domain of the cytoplasmic trifunctional enzyme
0.01
5,10-methylenetetrahydrofolate
-
bifunctional methylenetetrahydrofolate dehydrogenase-cyclohydrolase enzyme
0.012
5,10-methylenetetrahydrofolate
-
NAD+-M2+-phopsphate-dependent mitochondrial dehydrogenase-cyclohydrolase enzyme
0.015
5,10-methylenetetrahydrofolate
-
-
0.016
5,10-methylenetetrahydrofolate
-
cofactor: NAD+
0.022
5,10-methylenetetrahydrofolate
-
-
0.024
5,10-methylenetetrahydrofolate
-
bifunctional methylenetetrahydrofolate dehydrogenase-cyclohydrolase enzyme
0.026
5,10-methylenetetrahydrofolate
-
-
0.026
5,10-methylenetetrahydrofolate
-
-
0.03
5,10-methylenetetrahydrofolate
-
-
0.037
5,10-methylenetetrahydrofolate
-
-
0.038
5,10-methylenetetrahydrofolate
-
-
0.039
5,10-methylenetetrahydrofolate
-
-
0.045
5,10-methylenetetrahydrofolate
-
-
0.08
5,10-methylenetetrahydrofolate
-
-
0.17
5,10-methylenetetrahydrofolate
-
-
0.228
5,10-methylenetetrahydrofolate
pH 7.6, temperature not specified in the publication
4.76
5,10-methylenetetrahydrofolate
-
-
0.123
5,10-methylenetetrahydropteroylglutamate
pH 8.0, 30°C, at saturating concentrations of NADP+ (6.0 mM)
0.133
5,10-methylenetetrahydropteroylglutamate
pH 8.0, 30°C, at saturating concentrations of NAD+ (1.0 mM)
0.302
5,10-methylenetetrahydropteroylpentaglutamate
pH 8.0, 30°C, at saturating concentrations of NADP+ (6.0 mM)
0.359
5,10-methylenetetrahydropteroylpentaglutamate
pH 8.0, 30°C, at saturating concentrations of NAD+ (1.0 mM)
0.04
5,10-methylenetetrahydropteroylpoly-L-glutamate
pH 8.0, 30°C, monoglutamylated substrate, with NAD+
0.042
5,10-methylenetetrahydropteroylpoly-L-glutamate
pH 8.0, 30°C, monoglutamylated substrate, with NADP+
0.13
5,10-methylenetetrahydropteroylpoly-L-glutamate
pH 8.0, 30°C, polyglutamylated substrate, with NAD+
0.153
5,10-methylenetetrahydropteroylpoly-L-glutamate
pH 8.0, 30°C, polyglutamylated substrate, with NADP+
0.147
NAD+
pH 8.0, 30°C
0.507
NAD+
-
NAD+-M2+-phopsphate-dependent mitochondrial dehydrogenase-cyclohydrolase enzyme
0.0004
NADP+
-
-
0.022
NADP+
-
NADP+-dependent bifunctional dehydrogenase-cyclohydrolase domain of the cytoplasmic trifunctional enzyme
0.038
NADP+
-
bifunctional methylenetetrahydrofolate dehydrogenase-cyclohydrolase enzyme
0.038
NADP+
-
25 mM MOPS pH 7.3, 2.5 mM formaldehyde, 30 mM 2-mercaptoethanol, 27°C, with 250 microM 5,10-methylene-tetrahydrofolate
0.038
NADP+
-
recombinant DHCH1
0.085
NADP+
pH 7.6, temperature not specified in the publication
0.13
NADP+
-
bifunctional methylenetetrahydrofolate dehydrogenase-cyclohydrolase enzyme
0.187
NADP+
pH 7.6, 30°C, wild-type enzyme
0.233
NADP+
pH 7.6, 30°C, mutant enzyme K54S
0.302
NADP+
pH 7.6, 30°C, mutant enzyme C58Y
additional information
additional information
-
Michaelis-Menten kinetics
-
additional information
additional information
Michaelis-Menten kinetics
-
additional information
additional information
Michaelis-Menten kinetics
-
additional information
additional information
-
Michaelis-Menten kinetics
-
additional information
additional information
Michaelis-Menten kinetics
-
additional information
NADP+
-
mutation of Arg173 causes a 500fold increase in the Km value for NADP+, while mutation of Ser197 causes a 20fold increase
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0.01 - 19.9
5,10-methenyltetrahydrofolate
14
5,10-methylene tetrahydrofolate
-
recombinant DHCH1, 0.25 mM substrate
14
5,10-methylene-tetrahydrofolate
-
25 mM MOPS pH 7.3, 2.5 mM formaldehyde, 1 mM NADP+, 30 mM 2-mercaptoethanol, 27°C
3.2 - 9.4
5,10-methylenetetrahydrofolate
1.5 - 12.4
5,10-methylenetetrahydropteroylglutamate
6.4 - 15.4
5,10-methylenetetrahydropteroylpentaglutamate
1.3 - 8.8
5,10-methylenetetrahydropteroylpoly-L-glutamate
0.01
5,10-methenyltetrahydrofolate
pH 7.6, 30°C, mutant enzyme D121A
0.06
5,10-methenyltetrahydrofolate
pH 7.6, 30°C, mutant enzyme G122D
2.6
5,10-methenyltetrahydrofolate
pH 7.6, 30°C, mutant enzyme C58Y
14.3
5,10-methenyltetrahydrofolate
pH 7.6, 30°C, mutant enzyme K54S
19.9
5,10-methenyltetrahydrofolate
pH 7.6, 30°C, wild-type enzyme
3.2
5,10-methylenetetrahydrofolate
-
deuterated, NADP+-dependent bifunctional dehydrogenase-cyclohydrolase domain of the cytoplasmic trifunctional enzyme
9.4
5,10-methylenetetrahydrofolate
-
NADP+-dependent bifunctional dehydrogenase-cyclohydrolase domain of the cytoplasmic trifunctional enzyme
1.5
5,10-methylenetetrahydropteroylglutamate
pH 8.0, 30°C, at saturating concentrations of NADP+ (6.0 mM)
12.4
5,10-methylenetetrahydropteroylglutamate
pH 8.0, 30°C, at saturating concentrations of NAD+ (1.0 mM)
6.4
5,10-methylenetetrahydropteroylpentaglutamate
pH 8.0, 30°C, at saturating concentrations of NADP+ (6.0 mM)
15.4
5,10-methylenetetrahydropteroylpentaglutamate
pH 8.0, 30°C, at saturating concentrations of NAD+ (1.0 mM)
1.3
5,10-methylenetetrahydropteroylpoly-L-glutamate
pH 8.0, 30°C, monoglutamylated substrate, with NADP+
2.7
5,10-methylenetetrahydropteroylpoly-L-glutamate
pH 8.0, 30°C, monoglutamylated substrate, with NAD+
7.2
5,10-methylenetetrahydropteroylpoly-L-glutamate
pH 8.0, 30°C, polyglutamylated substrate, with NADP+
8.8
5,10-methylenetetrahydropteroylpoly-L-glutamate
pH 8.0, 30°C, polyglutamylated substrate, with NAD+
3.6
NAD+
pH 8.0, 30°C
1.1
NADP+
pH 8.0, 30°C
2.8
NADP+
pH 7.6, 30°C, mutant enzyme C58Y
3.8
NADP+
-
substrate constant: methylenetetrahydrofolate, deuterated, NADP+-dependent bifunctional dehydrogenase-cyclohydrolase domain of the cytoplasmic trifunctional enzyme
10
NADP+
-
NADP+-dependent bifunctional dehydrogenase-cyclohydrolase domain of the cytoplasmic trifunctional enzyme
10
NADP+
-
25 mM MOPS pH 7.3, 2.5 mM formaldehyde, 30 mM 2-mercaptoethanol, 27°C
10
NADP+
-
recombinant DHCH1, 1 mM NADP+
12.3
NADP+
pH 7.6, 30°C, mutant enzyme K54S
17.08
NADP+
pH 7.6, 30°C, wild-type enzyme
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0.0011 - 0.0051
(2S)-2-[[4-[(6aR)-3-amino-1,9-dioxo-5,6,6a,7-tetrahydro-4H-imidazol[3,4-f]pteridin-8-yl]benzoyl]amino]pentanedioic acid
0.0011 - 0.0051
(2S)-2-[[4-[(6aR)-3-amino-1,9-dioxo-5,6,6a,7-tetrahydro-4H-imidazo[3,4-f]pteridin-8-yl]benzoyl]amino]pentanedioic acid
0.00068 - 0.00076
2,4-diamino-6-(3,4-dichlorophenoxy)-quinazoline
0.0004 - 0.00044
2,4-diamino-6-benzyl-5-(3-phenylpropyl)-pyrimidine
0.000036 - 0.000041
methotrexate
0.0011
(2S)-2-[[4-[(6aR)-3-amino-1,9-dioxo-5,6,6a,7-tetrahydro-4H-imidazol[3,4-f]pteridin-8-yl]benzoyl]amino]pentanedioic acid
Leishmania major
-
wild type enzyme
0.0045
(2S)-2-[[4-[(6aR)-3-amino-1,9-dioxo-5,6,6a,7-tetrahydro-4H-imidazol[3,4-f]pteridin-8-yl]benzoyl]amino]pentanedioic acid
Leishmania major
-
dhch1-/pXNG4-DHCH1 mutant, FV1 line
0.0051
(2S)-2-[[4-[(6aR)-3-amino-1,9-dioxo-5,6,6a,7-tetrahydro-4H-imidazol[3,4-f]pteridin-8-yl]benzoyl]amino]pentanedioic acid
Leishmania major
-
WT/pXNG4-DHCH mutant, FV1 line
0.0011
(2S)-2-[[4-[(6aR)-3-amino-1,9-dioxo-5,6,6a,7-tetrahydro-4H-imidazo[3,4-f]pteridin-8-yl]benzoyl]amino]pentanedioic acid
Leishmania major
-
50% growth inhibition of wild-type cell line
0.0033
(2S)-2-[[4-[(6aR)-3-amino-1,9-dioxo-5,6,6a,7-tetrahydro-4H-imidazo[3,4-f]pteridin-8-yl]benzoyl]amino]pentanedioic acid
Leishmania major
-
50% growth inhibition of null mutant with plasmid expressing formate-tetrahydrofolate ligase
0.0037
(2S)-2-[[4-[(6aR)-3-amino-1,9-dioxo-5,6,6a,7-tetrahydro-4H-imidazo[3,4-f]pteridin-8-yl]benzoyl]amino]pentanedioic acid
Leishmania major
-
50% growth inhibition of wild-type with plasmid expressing formate-tetrahydrofolate ligase
0.0045
(2S)-2-[[4-[(6aR)-3-amino-1,9-dioxo-5,6,6a,7-tetrahydro-4H-imidazo[3,4-f]pteridin-8-yl]benzoyl]amino]pentanedioic acid
Leishmania major
-
50% growth inhibition of null mutant with plasmid expressing the enzyme
0.0051
(2S)-2-[[4-[(6aR)-3-amino-1,9-dioxo-5,6,6a,7-tetrahydro-4H-imidazo[3,4-f]pteridin-8-yl]benzoyl]amino]pentanedioic acid
Leishmania major
-
50% growth inhibition of wild-type with plasmid expressing the enzyme (overexpressing it as a result)
0.00068
2,4-diamino-6-(3,4-dichlorophenoxy)-quinazoline
Leishmania major
-
wild type enzyme
0.00076
2,4-diamino-6-(3,4-dichlorophenoxy)-quinazoline
Leishmania major
-
dhch1-/pXNG4-DHCH1 mutant, FV1 line
0.0004
2,4-diamino-6-benzyl-5-(3-phenylpropyl)-pyrimidine
Leishmania major
-
dhch1-/pXNG4-DHCH1 mutant, FV1 line
0.00044
2,4-diamino-6-benzyl-5-(3-phenylpropyl)-pyrimidine
Leishmania major
-
wild type enzyme
0.000036
methotrexate
Leishmania major
-
wild type enzyme
0.000041
methotrexate
Leishmania major
-
dhch1-/pXNG4-DHCH1 mutant, FV1 line
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evolution
the redox cofactor requirements of the isozymes from Mus musculus and Rattus norvegicus are quite similar, both exhibit lower Km values for NAD+ than for NADP+, their NAD+-dependent activities require phosphate and Mg2+, and their NADP+-dependent activities are inhibited by phosphate
evolution
the redox cofactor requirements of the isozymes from Mus musculus and Rattus norvegicus are quite similar, both exhibit lower Km values for NAD+ than for NADP+, their NAD+-dependent activities require phosphate and Mg2+, and their NADP+-dependent activities are inhibited by phosphate
evolution
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the redox cofactor requirements of the isozymes from Mus musculus and Rattus norvegicus are quite similar, both exhibit lower Km values for NAD+ than for NADP+, their NAD+-dependent activities require phosphate and Mg2+, and their NADP+-dependent activities are inhibited by phosphate
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metabolism
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cytosolic protein with role in cytosolic purine synthesis, ubiquitously expressed in all mammalian cells
metabolism
-
mitochondrial protein with role in cytosolic purine synthesis (main switch for format production in mitochondria) during embryonic development and in cells undergoing rapid growth, not expressed in differentiated cells
metabolism
-
product of the bifuncional enzyme, 10-formyl tetrahydrofolate, is not essential for de novo purine synthesis in Leishmania and other parasitic protozoans contrary to other organisms, it is utilized for methionyl-tRNA formulation in mitochondria, the bifunctional enzyme product is essential for Leishmania major and may even reveal novel pathways
metabolism
the dehydrogenase activity of FolD catalyses NADP+-dependent oxidation of 5,10-methylenetetrahydrofolate to 5,10-methenyltetrahydrofolate. The 5,10-methenyltetrahydrofolate cyclohydrolase activity in Clostridium perfringens is provided by another protein, the 5,10-methylenetetrahydrofolate cyclohydrolase FchA, whose cyclohydrolase activity is 10 times more efficient than that of Eco FolD. Both Clostridium perfringens FolD and FchA are required to substitute for the single bifunctional FolD in Escherichia coli. The simultaneous presence of Clostridium perfringens FolD and FchA is also necessary to rescue an Escherichia coli K16 folD deletion strain for its formate and glycine auxotrophies, and to alleviate its susceptibility to trimethoprim (an antifolate drug) or UV light
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
metabolism
the enzyme is involved in the folate recycling pathway
metabolism
the enzyme plays a central role in folate homeostasis and serve as targets for antibacterials
metabolism
the mitochondrial methylenetetrahydrofolate dehydrogenase/cyclohydrolase(MTHFD2)-controlled cluster redirects metabolism to glycine synthesis to replenish purine nucleotides. Since endothelial cells secrete purines in response to oxPAPC, the MTHFD2-controlled response maintains endothelial ATP. Accordingly, MTHFD2-dependent glycine synthesis is a prerequisite for angiogenesis. It is proposed that endothelial cells undergo MTHFD2-mediated reprogramming toward serine-glycine and mitochondrial one-carbon metabolism to compensate for the loss of ATP in response to oxidized phospholipids during atherosclerosis
metabolism
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the enzyme is involved in the folate recycling pathway
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physiological function
MTHFD2L uses both NAD+ and NADP+ and is expressed in embryonic tissues during neural tube closure. The cofactor specificity allows for rapid response to changing metabolic conditions. MTHFD2 uses Mg2+ and phosphate to convert an NADP+ binding site into an NAD+ binding site. Phosphate binds in close proximity to the 2'-hydroxyl of NAD+ and competes with NADP+ binding. Mg2 plays a role in positioning phosphatei and NAD+
physiological function
MTHFD2L uses both NAD+ and NADP+ and is expressed in embryonic tissues during neural tube closure. The cofactor specificity allows for rapid response to changing metabolic conditions. MTHFD2 uses Mg2+ and phosphate to convert an NADP+ binding site into an NAD+ binding site. Phosphate binds in close proximity to the 2'-hydroxyl of NAD+ and competes with NADP+ binding. Mg2 plays a role in positioning phosphatei and NAD+
physiological function
unlike the bifunctional enzyme FolD of Escherichia coli, and contrary to its annotated bifunctional nature, Clostridium perfringens FolD is a monofunctional 5,10-CH2-THF dehydrogenase. The dehydrogenase activity of Clostridium perfringens FolD is about five times more efficient than that of Escherichia coli FolD. FolD plays an important role in maintaining the NADP+/NADPH ratio
physiological function
-
MTHFD2L uses both NAD+ and NADP+ and is expressed in embryonic tissues during neural tube closure. The cofactor specificity allows for rapid response to changing metabolic conditions. MTHFD2 uses Mg2+ and phosphate to convert an NADP+ binding site into an NAD+ binding site. Phosphate binds in close proximity to the 2'-hydroxyl of NAD+ and competes with NADP+ binding. Mg2 plays a role in positioning phosphatei and NAD+
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additional information
MTFHD2 isozyme has been named NAD+-dependent methylenetetrahydrofolate dehydrogenase-methenyltetrahydrofolate cyclohydrolase but in fact exhibits dehydrogenase activity with NADP+, albeit with a much higher Km and lower Vmax
additional information
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MTFHD2 isozyme has been named NAD+-dependent methylenetetrahydrofolate dehydrogenase-methenyltetrahydrofolate cyclohydrolase but in fact exhibits dehydrogenase activity with NADP+, albeit with a much higher Km and lower Vmax
additional information
MTFHD2 isozyme has been named NAD+-dependent methylenetetrahydrofolate dehydrogenase-methenyltetrahydrofolate cyclohydrolase but in fact exhibits dehydrogenase activity with NADP+, albeit with a much higher Km and lower Vmax
additional information
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the amino acid residue Tyr49 contributes to its catalytic activity
additional information
-
MTFHD2 isozyme has been named NAD+-dependent methylenetetrahydrofolate dehydrogenase-methenyltetrahydrofolate cyclohydrolase but in fact exhibits dehydrogenase activity with NADP+, albeit with a much higher Km and lower Vmax
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Saccharomyces cerevisiae, Ovis aries, Sus scrofa
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Pisum sativum
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Oryctolagus cuniculus
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Sus scrofa
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Homo sapiens, Mus musculus
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Escherichia coli, Escherichia coli B / ATCC 11303
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Moorella thermoacetica
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Moorella thermoacetica
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Salmonella enterica subsp. enterica serovar Typhimurium
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1962
Saccharomyces cerevisiae
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1977
Saccharomyces cerevisiae
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Homo sapiens
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Bos taurus
brenda
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Sus scrofa
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1973
Sus scrofa
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1984
Sus scrofa
brenda
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The NADP-dependent trifunctional methylenetetrahydrofolate dehydrogenase purified from mouse liver is immunologically distinct from the mouse NAD-dependent [corrected] bifunctional enzyme [published erratum appears in Biochem Cell Biol 1988 May;66(5):459]
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1988
Mus musculus
brenda
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Formyl-methyl-methylenetetrahydrofolate synthetase-(combined). An ovine protein with multiple catalytic activities
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251
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1976
Ovis aries
brenda
Cossins, E.A.; Wong, K.F.; Roos, A.J.
Plant N5,N10-methylenetetrahydrofolate dehydrogenase: partial purification and some general properties of the enzyme from germinating pea seedlings
Phytochemistry
9
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1970
Pisum sativum
-
brenda
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Comparative study on major pathways of glycine and serine catabolism in vertebrate livers
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1503-1516
1972
Bos taurus, Elaphe quadrivirgata, Gallus gallus bankiva, Ovis aries
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1995
Homo sapiens
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Methenyltetrahydrofolate cyclohydrolase is rate limiting for the enzymatic conversion of 10-formyltetrahydrofolate to 5,10-methylenetetrahydrofolate in bifunctional dehydrogenase-cyclohydrolase enzymes
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1998
Homo sapiens, Photobacterium phosphoreum
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Hyphomicrobium zavarzinii, no activity in Methylobacterium extorquens, Hyphomicrobium zavarzinii ZV580
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Arthrobacter globiformis
-
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Thermoplasma acidophilum
brenda
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Homo sapiens (P11586)
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Leishmania major
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Saccharomyces cerevisiae, Homo sapiens
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406
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Thermoplasma acidophilum (Q05213)
brenda
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brenda
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Homo sapiens, Rattus norvegicus
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Clostridium perfringens, Clostridium perfringens (Q0TPD4)
brenda
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Escherichia coli (P24186), Escherichia coli K12 (P24186)
brenda
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75
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Homo sapiens (P11586)
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5
11
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Homo sapiens (P13995), Homo sapiens (Q9H903)
brenda
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164
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Escherichia coli (P24186), Escherichia coli K12 (P24186)
brenda
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9
2292
2018
Homo sapiens (P13995)
brenda
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10
689
2020
Homo sapiens (P11586)
brenda
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Molecular structure of a 5,10-methylenetetrahydrofolate dehydrogenase from the silkworm Bombyx mori
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9
618-628
2019
Bombyx mori
brenda