Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
5,10-methenyltetrahydrofolate + NADH + H+
5,10-methylenetetrahydrofolate + NAD+
5,10-methylenetetrahydrofolate + NAD+
5,10-methenyltetrahydrofolate + NADH
5,10-methylenetetrahydrofolate + NAD+
5,10-methenyltetrahydrofolate + NADH + H+
5,10-methylenetetrahydrofolate + NADP+
5,10-methenyltetrahydrofolate + NADPH + H+
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+
L-5,10-methenyl-tetrahydrofolate + NADH
L-5,10-methylenetetrahydrofolate + NAD+
L-5,10-methylenetetrahydrofolate + NAD+
5,10-methenyl-tetrahydrofolate + NADH
additional information
?
-
5,10-methenyltetrahydrofolate + NADH + H+
5,10-methylenetetrahydrofolate + NAD+
-
-
-
ir
5,10-methenyltetrahydrofolate + NADH + H+
5,10-methylenetetrahydrofolate + NAD+
-
-
-
ir
5,10-methylenetetrahydrofolate + NAD+
5,10-methenyltetrahydrofolate + NADH
-
-
-
?
5,10-methylenetetrahydrofolate + NAD+
5,10-methenyltetrahydrofolate + NADH
-
-
-
-
?
5,10-methylenetetrahydrofolate + NAD+
5,10-methenyltetrahydrofolate + NADH
-
-
-
?
5,10-methylenetetrahydrofolate + NAD+
5,10-methenyltetrahydrofolate + NADH
enzyme provides one-carbon units for purine synthesis during embryogenesis, metabolism overview
-
-
?
5,10-methylenetetrahydrofolate + NAD+
5,10-methenyltetrahydrofolate + NADH
N-terminal catalytic domain
-
-
?
5,10-methylenetetrahydrofolate + NAD+
5,10-methenyltetrahydrofolate + NADH + H+
-
-
-
-
r
5,10-methylenetetrahydrofolate + NAD+
5,10-methenyltetrahydrofolate + NADH + H+
-
enzyme binding structure analysis, overview
-
-
r
5,10-methylenetetrahydrofolate + NAD+
5,10-methenyltetrahydrofolate + NADH + H+
the bifunctional enzyme also shows N5,N10-methenyltetrahydrofolate cyclohydrolase activity EC 3.5.4.9. with NADP+ (1 mM), the enzyme shows less than 0.1% of the activity obtained with NAD+ (1 mM). The purified enzyme shows no activity with methylene-tetrahydromethanopterin or with 5,10-methylenetetrahydrosarcinapterin either in the presence of NAD+ or NADP+ or in the presence of F420
-
-
?
5,10-methylenetetrahydrofolate + NAD+
5,10-methenyltetrahydrofolate + NADH + H+
the bifunctional enzyme also shows N5,N10-methenyltetrahydrofolate cyclohydrolase activity EC 3.5.4.9. with NADP+ (1 mM), the enzyme shows less than 0.1% of the activity obtained with NAD+ (1 mM). The purified enzyme shows no activity with methylene-tetrahydromethanopterin or with 5,10-methylenetetrahydrosarcinapterin either in the presence of NAD+ or NADP+ or in the presence of F420
-
-
?
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+
about 15% of the rate with NAD+
-
-
?
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
-
-
?
L-5,10-methenyl-tetrahydrofolate + NADH
L-5,10-methylenetetrahydrofolate + NAD+
-
-
-
-
r
L-5,10-methenyl-tetrahydrofolate + NADH
L-5,10-methylenetetrahydrofolate + NAD+
-
physiological direction in most organisms is the forward rection, in the acetogens the reverse reaction is the physiologically important one
-
-
r
L-5,10-methenyl-tetrahydrofolate + NADH
L-5,10-methylenetetrahydrofolate + NAD+
Antheraea eucalypti
-
-
-
-
r
L-5,10-methenyl-tetrahydrofolate + NADH
L-5,10-methylenetetrahydrofolate + NAD+
-
-
-
-
r
L-5,10-methenyl-tetrahydrofolate + NADH
L-5,10-methylenetetrahydrofolate + NAD+
-
-
-
-
r
L-5,10-methenyl-tetrahydrofolate + NADH
L-5,10-methylenetetrahydrofolate + NAD+
-
-
-
-
r
L-5,10-methenyl-tetrahydrofolate + NADH
L-5,10-methylenetetrahydrofolate + NAD+
-
physiological direction in most organisms is the forward rection, in the acetogens the reverse reaction is the physiologically important one
-
-
r
L-5,10-methenyl-tetrahydrofolate + NADH
L-5,10-methylenetetrahydrofolate + NAD+
-
-
-
-
r
L-5,10-methenyl-tetrahydrofolate + NADH
L-5,10-methylenetetrahydrofolate + NAD+
-
-
-
-
r
L-5,10-methenyl-tetrahydrofolate + NADH
L-5,10-methylenetetrahydrofolate + NAD+
-
-
-
-
r
L-5,10-methenyl-tetrahydrofolate + NADH
L-5,10-methylenetetrahydrofolate + NAD+
-
-
-
-
r
L-5,10-methenyl-tetrahydrofolate + NADH
L-5,10-methylenetetrahydrofolate + NAD+
-
-
392077, 392079, 392083, 392084, 392085, 392086, 392087, 392088, 392090, 392091, 392093 -
-
r
L-5,10-methenyl-tetrahydrofolate + NADH
L-5,10-methylenetetrahydrofolate + NAD+
-
-
-
-
r
L-5,10-methenyl-tetrahydrofolate + NADH
L-5,10-methylenetetrahydrofolate + NAD+
-
-
-
-
r
L-5,10-methenyl-tetrahydrofolate + NADH
L-5,10-methylenetetrahydrofolate + NAD+
-
-
392075, 392076, 392077, 392078, 392079, 392080, 392081, 392082, 392084, 392085, 392086, 392087, 392088, 392090, 392091, 392092, 392093 -
-
r
L-5,10-methenyl-tetrahydrofolate + NADH
L-5,10-methylenetetrahydrofolate + NAD+
-
-
-
-
r
L-5,10-methenyl-tetrahydrofolate + NADH
L-5,10-methylenetetrahydrofolate + NAD+
-
-
-
-
r
L-5,10-methenyl-tetrahydrofolate + NADH
L-5,10-methylenetetrahydrofolate + NAD+
-
-
-
-
r
L-5,10-methenyl-tetrahydrofolate + NADH
L-5,10-methylenetetrahydrofolate + NAD+
-
-
-
-
r
L-5,10-methenyl-tetrahydrofolate + NADH
L-5,10-methylenetetrahydrofolate + NAD+
-
-
-
-
r
L-5,10-methylenetetrahydrofolate + NAD+
5,10-methenyl-tetrahydrofolate + NADH
-
-
-
-
r
L-5,10-methylenetetrahydrofolate + NAD+
5,10-methenyl-tetrahydrofolate + NADH
Antheraea eucalypti
-
-
-
-
r
L-5,10-methylenetetrahydrofolate + NAD+
5,10-methenyl-tetrahydrofolate + NADH
-
-
-
-
r
L-5,10-methylenetetrahydrofolate + NAD+
5,10-methenyl-tetrahydrofolate + NADH
-
-
-
-
r
L-5,10-methylenetetrahydrofolate + NAD+
5,10-methenyl-tetrahydrofolate + NADH
-
-
-
-
r
L-5,10-methylenetetrahydrofolate + NAD+
5,10-methenyl-tetrahydrofolate + NADH
-
-
-
-
r
L-5,10-methylenetetrahydrofolate + NAD+
5,10-methenyl-tetrahydrofolate + NADH
-
-
-
-
r
L-5,10-methylenetetrahydrofolate + NAD+
5,10-methenyl-tetrahydrofolate + NADH
-
-
-
-
r
L-5,10-methylenetetrahydrofolate + NAD+
5,10-methenyl-tetrahydrofolate + NADH
-
-
-
-
r
L-5,10-methylenetetrahydrofolate + NAD+
5,10-methenyl-tetrahydrofolate + NADH
-
-
392077, 392079, 392083, 392084, 392085, 392086, 392087, 392088, 392090, 392091, 392093 -
-
r
L-5,10-methylenetetrahydrofolate + NAD+
5,10-methenyl-tetrahydrofolate + NADH
-
-
-
-
r
L-5,10-methylenetetrahydrofolate + NAD+
5,10-methenyl-tetrahydrofolate + NADH
-
-
-
-
r
L-5,10-methylenetetrahydrofolate + NAD+
5,10-methenyl-tetrahydrofolate + NADH
-
-
392075, 392076, 392077, 392078, 392079, 392080, 392081, 392082, 392084, 392085, 392086, 392087, 392088, 392090, 392091, 392092, 392093 -
-
r
L-5,10-methylenetetrahydrofolate + NAD+
5,10-methenyl-tetrahydrofolate + NADH
-
-
-
-
r
L-5,10-methylenetetrahydrofolate + NAD+
5,10-methenyl-tetrahydrofolate + NADH
-
-
-
-
r
L-5,10-methylenetetrahydrofolate + NAD+
5,10-methenyl-tetrahydrofolate + NADH
-
-
-
-
r
L-5,10-methylenetetrahydrofolate + NAD+
5,10-methenyl-tetrahydrofolate + NADH
-
-
-
-
r
L-5,10-methylenetetrahydrofolate + NAD+
5,10-methenyl-tetrahydrofolate + NADH
-
-
-
-
r
additional information
?
-
-
-
-
-
?
additional information
?
-
-
active only with L-5,10-methylenetetrahydrofolate, the L-isomer does not affect the reaction
-
-
?
additional information
?
-
-
the reaction catalyzed by Escherichia coli MTHFR can be divided into a reductive half-reaction and an oxidative half-reaction, respectively, in which the FAD cofactor acts as an intermediate electron acceptor and donor. For enzyme assay, menadione is used as an alternate electron acceptor, MTHFR oxidizes NADH to NAD+, and the reaction can be monitored at 343 nm by the decrease in NADH absorbance
-
-
-
additional information
?
-
-
-
-
-
?
additional information
?
-
-
-
-
-
?
additional information
?
-
-
bifunctional enzyme
-
-
?
additional information
?
-
-
key enzyme in folate metabolism playing a major role in provision of methyl groups for DNA methylation and in production of dTMP for DNA synthesis
-
-
?
additional information
?
-
-
-
-
-
?
additional information
?
-
-
-
-
-
?
additional information
?
-
-
-
-
-
?
additional information
?
-
-
level of enzyme activity appears to be strain dependent with Swiss mice having the highest activity
-
-
?
additional information
?
-
enzyme deficiency results in a number of diseases
-
-
?
additional information
?
-
-
enzyme deficiency results in a number of diseases
-
-
?
additional information
?
-
MTHFD2 interacts with mitochondrial ETC complex III in mitochondria, mechanism
-
-
-
additional information
?
-
-
MTHFD2 interacts with mitochondrial ETC complex III in mitochondria, mechanism
-
-
-
additional information
?
-
identification of the reaction product of MSMEG_6596 by LC-MS/MS
-
-
-
additional information
?
-
identification of the reaction product of MSMEG_6596 by LC-MS/MS
-
-
-
additional information
?
-
-
identification of the reaction product of MSMEG_6596 by LC-MS/MS
-
-
-
additional information
?
-
identification of the reaction product of MSMEG_6649 by LC-MS/MS
-
-
-
additional information
?
-
identification of the reaction product of MSMEG_6649 by LC-MS/MS
-
-
-
additional information
?
-
-
identification of the reaction product of MSMEG_6649 by LC-MS/MS
-
-
-
additional information
?
-
identification of the reaction product of MSMEG_6596 by LC-MS/MS
-
-
-
additional information
?
-
identification of the reaction product of MSMEG_6596 by LC-MS/MS
-
-
-
additional information
?
-
identification of the reaction product of MSMEG_6649 by LC-MS/MS
-
-
-
additional information
?
-
identification of the reaction product of MSMEG_6649 by LC-MS/MS
-
-
-
additional information
?
-
-
-
-
-
?
additional information
?
-
-
-
-
-
?
additional information
?
-
-
contains 2 enzymes, monofunctional NAD+ dependent dehydrogenase EC1.5.1.15 and trifunctional NADP+ dependent dehydrogenase, EC1.5.1.5
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
5,10-methenyltetrahydrofolate + NADH + H+
5,10-methylenetetrahydrofolate + NAD+
5,10-methylenetetrahydrofolate + NAD+
5,10-methenyltetrahydrofolate + NADH
5,10-methylenetetrahydrofolate + NAD+
5,10-methenyltetrahydrofolate + NADH + H+
5,10-methylenetetrahydrofolate + NADP+
5,10-methenyltetrahydrofolate + NADPH + H+
L-5,10-methenyl-tetrahydrofolate + NADH
L-5,10-methylenetetrahydrofolate + NAD+
L-5,10-methylenetetrahydrofolate + NAD+
5,10-methenyl-tetrahydrofolate + NADH
additional information
?
-
5,10-methenyltetrahydrofolate + NADH + H+
5,10-methylenetetrahydrofolate + NAD+
-
-
-
ir
5,10-methenyltetrahydrofolate + NADH + H+
5,10-methylenetetrahydrofolate + NAD+
-
-
-
ir
5,10-methylenetetrahydrofolate + NAD+
5,10-methenyltetrahydrofolate + NADH
-
-
-
-
?
5,10-methylenetetrahydrofolate + NAD+
5,10-methenyltetrahydrofolate + NADH
enzyme provides one-carbon units for purine synthesis during embryogenesis, metabolism overview
-
-
?
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+
-
?
-
-
L-5,10-methenyl-tetrahydrofolate + NADH
L-5,10-methylenetetrahydrofolate + NAD+
-
-
-
-
r
L-5,10-methenyl-tetrahydrofolate + NADH
L-5,10-methylenetetrahydrofolate + NAD+
-
physiological direction in most organisms is the forward rection, in the acetogens the reverse reaction is the physiologically important one
-
-
r
L-5,10-methenyl-tetrahydrofolate + NADH
L-5,10-methylenetetrahydrofolate + NAD+
Antheraea eucalypti
-
-
-
-
r
L-5,10-methenyl-tetrahydrofolate + NADH
L-5,10-methylenetetrahydrofolate + NAD+
-
-
-
-
r
L-5,10-methenyl-tetrahydrofolate + NADH
L-5,10-methylenetetrahydrofolate + NAD+
-
-
-
-
r
L-5,10-methenyl-tetrahydrofolate + NADH
L-5,10-methylenetetrahydrofolate + NAD+
-
-
-
-
r
L-5,10-methenyl-tetrahydrofolate + NADH
L-5,10-methylenetetrahydrofolate + NAD+
-
physiological direction in most organisms is the forward rection, in the acetogens the reverse reaction is the physiologically important one
-
-
r
L-5,10-methenyl-tetrahydrofolate + NADH
L-5,10-methylenetetrahydrofolate + NAD+
-
-
-
-
r
L-5,10-methenyl-tetrahydrofolate + NADH
L-5,10-methylenetetrahydrofolate + NAD+
-
-
-
-
r
L-5,10-methenyl-tetrahydrofolate + NADH
L-5,10-methylenetetrahydrofolate + NAD+
-
-
-
-
r
L-5,10-methenyl-tetrahydrofolate + NADH
L-5,10-methylenetetrahydrofolate + NAD+
-
-
-
-
r
L-5,10-methenyl-tetrahydrofolate + NADH
L-5,10-methylenetetrahydrofolate + NAD+
-
-
392077, 392079, 392083, 392084, 392085, 392086, 392087, 392088, 392090, 392091, 392093 -
-
r
L-5,10-methenyl-tetrahydrofolate + NADH
L-5,10-methylenetetrahydrofolate + NAD+
-
-
-
-
r
L-5,10-methenyl-tetrahydrofolate + NADH
L-5,10-methylenetetrahydrofolate + NAD+
-
-
-
-
r
L-5,10-methenyl-tetrahydrofolate + NADH
L-5,10-methylenetetrahydrofolate + NAD+
-
-
392075, 392076, 392077, 392078, 392079, 392080, 392081, 392082, 392084, 392085, 392086, 392087, 392088, 392090, 392091, 392092, 392093 -
-
r
L-5,10-methenyl-tetrahydrofolate + NADH
L-5,10-methylenetetrahydrofolate + NAD+
-
-
-
-
r
L-5,10-methenyl-tetrahydrofolate + NADH
L-5,10-methylenetetrahydrofolate + NAD+
-
-
-
-
r
L-5,10-methenyl-tetrahydrofolate + NADH
L-5,10-methylenetetrahydrofolate + NAD+
-
-
-
-
r
L-5,10-methenyl-tetrahydrofolate + NADH
L-5,10-methylenetetrahydrofolate + NAD+
-
-
-
-
r
L-5,10-methenyl-tetrahydrofolate + NADH
L-5,10-methylenetetrahydrofolate + NAD+
-
-
-
-
r
L-5,10-methylenetetrahydrofolate + NAD+
5,10-methenyl-tetrahydrofolate + NADH
-
-
-
-
r
L-5,10-methylenetetrahydrofolate + NAD+
5,10-methenyl-tetrahydrofolate + NADH
Antheraea eucalypti
-
-
-
-
r
L-5,10-methylenetetrahydrofolate + NAD+
5,10-methenyl-tetrahydrofolate + NADH
-
-
-
-
r
L-5,10-methylenetetrahydrofolate + NAD+
5,10-methenyl-tetrahydrofolate + NADH
-
-
-
-
r
L-5,10-methylenetetrahydrofolate + NAD+
5,10-methenyl-tetrahydrofolate + NADH
-
-
-
-
r
L-5,10-methylenetetrahydrofolate + NAD+
5,10-methenyl-tetrahydrofolate + NADH
-
-
-
-
r
L-5,10-methylenetetrahydrofolate + NAD+
5,10-methenyl-tetrahydrofolate + NADH
-
-
-
-
r
L-5,10-methylenetetrahydrofolate + NAD+
5,10-methenyl-tetrahydrofolate + NADH
-
-
-
-
r
L-5,10-methylenetetrahydrofolate + NAD+
5,10-methenyl-tetrahydrofolate + NADH
-
-
-
-
r
L-5,10-methylenetetrahydrofolate + NAD+
5,10-methenyl-tetrahydrofolate + NADH
-
-
392077, 392079, 392083, 392084, 392085, 392086, 392087, 392088, 392090, 392091, 392093 -
-
r
L-5,10-methylenetetrahydrofolate + NAD+
5,10-methenyl-tetrahydrofolate + NADH
-
-
-
-
r
L-5,10-methylenetetrahydrofolate + NAD+
5,10-methenyl-tetrahydrofolate + NADH
-
-
-
-
r
L-5,10-methylenetetrahydrofolate + NAD+
5,10-methenyl-tetrahydrofolate + NADH
-
-
392075, 392076, 392077, 392078, 392079, 392080, 392081, 392082, 392084, 392085, 392086, 392087, 392088, 392090, 392091, 392092, 392093 -
-
r
L-5,10-methylenetetrahydrofolate + NAD+
5,10-methenyl-tetrahydrofolate + NADH
-
-
-
-
r
L-5,10-methylenetetrahydrofolate + NAD+
5,10-methenyl-tetrahydrofolate + NADH
-
-
-
-
r
L-5,10-methylenetetrahydrofolate + NAD+
5,10-methenyl-tetrahydrofolate + NADH
-
-
-
-
r
L-5,10-methylenetetrahydrofolate + NAD+
5,10-methenyl-tetrahydrofolate + NADH
-
-
-
-
r
L-5,10-methylenetetrahydrofolate + NAD+
5,10-methenyl-tetrahydrofolate + NADH
-
-
-
-
r
additional information
?
-
-
key enzyme in folate metabolism playing a major role in provision of methyl groups for DNA methylation and in production of dTMP for DNA synthesis
-
-
?
additional information
?
-
enzyme deficiency results in a number of diseases
-
-
?
additional information
?
-
-
enzyme deficiency results in a number of diseases
-
-
?
additional information
?
-
MTHFD2 interacts with mitochondrial ETC complex III in mitochondria, mechanism
-
-
-
additional information
?
-
-
MTHFD2 interacts with mitochondrial ETC complex III in mitochondria, mechanism
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.0632 - 1
5,10-methenyltetrahydrofolate
0.0004 - 0.29
5,10-methylenetetrahydrofolate
0.123 - 0.133
5,10-methylenetetrahydropteroylglutamate
0.302 - 0.359
5,10-methylenetetrahydropteroylpentaglutamate
0.0046 - 0.26
L-5,10-methylenetetrahydrofolate
0.03 - 0.096
methenyltetrahydrofolate
additional information
5,10-methylenetetrahydrofolate
0.0632
5,10-methenyltetrahydrofolate
pH 7.6, 22°C
0.145
5,10-methenyltetrahydrofolate
pH 7.6, 22°C
0.15
5,10-methenyltetrahydrofolate
-
-
0.155
5,10-methenyltetrahydrofolate
-
-
1
5,10-methenyltetrahydrofolate
-
-
0.0004
5,10-methylenetetrahydrofolate
-
pH 7.2, 25°C, recombinant wild-type, NADH-CH2-H4folate oxidoreductase assay
0.03
5,10-methylenetetrahydrofolate
-
pH 7.2, 25°C, recombinant wild-type, CH3-H4folate-menadione oxidoreductase assay
0.108
5,10-methylenetetrahydrofolate
-
pH 7.2, 25°C, recombinant mutant Q183E, NADH-CH2-H4folate oxidoreductase assay
0.115
5,10-methylenetetrahydrofolate
-
pH 7.2, 25°C, recombinant mutant Q183E, CH3-H4folate-menadione oxidoreductase assay
0.29
5,10-methylenetetrahydrofolate
-
pH 7.2, 25°C, recombinant mutant Q183A, NADH-CH2-H4folate oxidoreductase assay
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)
0.0046
L-5,10-methylenetetrahydrofolate
-
-
0.005
L-5,10-methylenetetrahydrofolate
-
-
0.019
L-5,10-methylenetetrahydrofolate
-
-
0.06
L-5,10-methylenetetrahydrofolate
-
-
0.066
L-5,10-methylenetetrahydrofolate
-
-
0.26
L-5,10-methylenetetrahydrofolate
-
-
0.03
methenyltetrahydrofolate
-
-
0.096
methenyltetrahydrofolate
-
-
0.171
Mg2+
-
-
0.013
NAD+
-
-
0.202
NAD+
wild-type, pH 7.3
0.918
NAD+
mutant R198K, pH 7.3
1.99
NAD+
mutant D133N, pH 7.3
2.17
NAD+
mutant D133S, pH 7.3
3.88
NAD+
mutant D190N, pH 7.3
0.0035
NADH
-
pH 7.2, 25°C, recombinant wild-type, NADH-CH2-H4folate oxidoreductase assay
0.0066
NADH
-
pH 7.2, 25°C, recombinant wild-type, NADH-CH2-H4folate oxidoreductase assay
0.01
NADH
-
pH 7.2, 25°C, recombinant mutant Q183E, NADH-CH2-H4folate oxidoreductase assay
0.0151
NADH
-
pH 7.2, 25°C, recombinant mutant Q183A, NADH-menadione oxidoreductase assay
0.0204
NADH
-
pH 7.2, 25°C, recombinant mutant Q183E, NADH-menadione oxidoreductase assay
0.025
NADH
-
pH 7.2, 25°C, recombinant wild-type, NADH-menadione oxidoreductase assay
0.29
NADH
-
pH 7.2, 25°C, recombinant wild-type, NADH-CH2-H4folate oxidoreductase assay
0.255
NADP+
mutant R198S, pH 7.3
0.352
NADP+
wild-type, pH 7.3
0.503
NADP+
mutant D133S, pH 7.3
0.58
NADP+
mutant D133N, pH 7.3
0.689
NADP+
mutant D190N, pH 7.3
2.12
NADP+
mutant R198K, pH 7.3
0.17
phosphate
-
-
additional information
5,10-methylenetetrahydrofolate
pH 6.0, 37°C, the Km-value for 5,10-methylenetetrahydrofolate in the presence of 2.7 mM NAD+ is below 0.005 mM
additional information
additional information
-
Michaelis-Menten steady-state kinetic analysis, comparisons of half-reaction kinetics of wild-type and mutant enzymes
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.688 - 4.063
5,10-methenyltetrahydrofolate
0.15 - 2.7
5,10-methylenetetrahydrofolate
1.5 - 12.4
5,10-methylenetetrahydropteroylglutamate
6.4 - 15.4
5,10-methylenetetrahydropteroylpentaglutamate
1.58
L-5,10-methenyltetrahydrofolate
-
-
1.63
L-5,10-methylenetetrahydrofolate
-
-
0.688
5,10-methenyltetrahydrofolate
pH 7.6, 22°C
4.063
5,10-methenyltetrahydrofolate
pH 7.6, 22°C
0.15
5,10-methylenetetrahydrofolate
-
pH 7.2, 25°C, recombinant wild-type, CH3-H4folate-menadione oxidoreductase assay
0.29
5,10-methylenetetrahydrofolate
-
pH 7.2, 25°C, recombinant mutant Q183A, NADH-CH2-H4folate oxidoreductase assay
0.47
5,10-methylenetetrahydrofolate
-
pH 7.2, 25°C, recombinant wild-type, CH3-H4folate-menadione oxidoreductase assay
2.2
5,10-methylenetetrahydrofolate
-
pH 7.2, 25°C, recombinant wild-type, NADH-CH2-H4folate oxidoreductase assay
2.7
5,10-methylenetetrahydrofolate
-
pH 7.2, 25°C, recombinant mutant Q183E, NADH-CH2-H4folate oxidoreductase assay
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)
0.29
NADH
-
pH 7.2, 25°C, recombinant wild-type, NADH-CH2-H4folate oxidoreductase assay
2.2
NADH
-
pH 7.2, 25°C, recombinant wild-type, NADH-CH2-H4folate oxidoreductase assay
2.7
NADH
-
pH 7.2, 25°C, recombinant mutant Q183E, NADH-CH2-H4folate oxidoreductase assay
14
NADH
-
pH 7.2, 25°C, recombinant mutant Q183E, NADH-menadione oxidoreductase assay
15.3
NADH
-
pH 7.2, 25°C, recombinant mutant Q183A, NADH-menadione oxidoreductase assay
18.2
NADH
-
pH 7.2, 25°C, recombinant wild-type, NADH-menadione oxidoreductase assay
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.0001
-
C-57/Bl, bone marrow and whole adrenal, CD-1, adrenal
0.0006
-
RLE cells, virus 3611.MSV v-raf oncogene-transformed
0.00076
-
fibroblasts, syrian hamster embryo
0.0011
-
Swiss, bone marrow
0.0017
-
cell line B-16 solid tumor
0.002
-
RLE cells, virus pRNR16 v-Ha-ras oncogene-transformed
0.0021
-
RLE cells, virus J2 v-raf/v-myc oncogene-transformed
0.0024
-
cell line M4, human cutaneous melanoma
0.0027
-
cell line MCF-7, 100% confluent
0.003
-
cell line LR-73, chinese hamster ovary
0.0031
-
cell line K562, human chronic myeolcytic leukemia
0.0033
-
cell line TL3, EBV-transformed
0.0035
-
cell line MCF-7, 50% confluent
0.004
-
cell line CCRF-CEM
0.0046
-
cell line TL4, EBV-transformed
0.0047
-
cell line MG-63, human osteosarcoma
0.0049
-
cell line BeWo, human choriocarcinoma
0.0059
-
cell line P815, ascites in vivo
0.0066
-
cell line EL4, ascites in vivo
0.0068
-
L-cells, murine fibroblast
0.0069
-
cell line MCF-7, human breast carcinoma
0.0071
-
cell line P-388 leukemia ip
0.0078
-
cell line CCRF-CEM, human leukemia
0.0089
-
Ehrlich ascites, ascites in vivo
0.0094
-
cell line EL4, murine T-cell lymphoma
0.0097
-
cell line YAC, murine lymphoma (Moloney virus-induced)
0.0105
-
cell line 3T3-SV40, SV40 transformed
0.02
-
Ehrlich ascites, murine mastocytoma
0.024
mutant D190E, cosubstrate NAD+, pH 7.3
0.156
mutant R198A, cosubstrate NADP+, pH 7.3
0.16
mutant D133A, cosubstrate NADP+, pH 7.3
0.17
mutant R198A, cosubstrate NAD+, pH 7.3
0.207
mutant R198S, cosubstrate NAD+, pH 7.3
0.392
mutant D133A, cosubstrate NAD+, pH 7.3
1 - 2
pH 6.0, 37°C, purified enzyme, recombinant
1.01
mutant D133S, cosubstrate NADP+, pH 7.3
1.24
mutant R198K, cosubstrate NADP+, pH 7.3
1.54
mutant R198S, cosubstrate NADP+, pH 7.3
12.6
mutant R198K, cosubstrate NAD+, pH 7.3
12.9
-
embryonal carcinoma
2 - 2.5
wild-type, cosubstrate NAD+, pH 7.3
2.92
wild-type, cosubstrate NADP+, pH 7.3
3.64
mutant D190N, cosubstrate NAD+, pH 7.3
3.96
mutant D190N, cosubstrate NADP+, pH 7.3
3.99
mutant D133S, cosubstrate NAD+, pH 7.3
4.6
mutant D133N, cosubstrate NAD+, pH 7.3
5
pH 6.0, 37°C, extract from Escherichia coli cells carrying the expression vector
0.0002
-
adrenal cortex
0.0003
-
cell line MRC-5
0.0003
-
HEP-G2 tumor in nude mice
0.0003
-
RLE cells and RLE cells virus J5 v-myc oncogene-transformed
0.0004
-
spleen
0.0004
-
CD-1, bone marrow
0.0005
-
human liver tumor
0.0005
-
colon 38 solid tumor
0.0012
-
cell line Hl-60
0.0012
-
RLE cells, spontaneous oncogene transformed
0.0015
-
cell line HEP-2
0.0015
-
RLE cells, aflatoxin oncogene-transformed
0.0039
-
cell line 3T3, mouse embryo
0.0039
-
cell line P-388 in vitro
0.0042
-
hamster embryo fibroblast, Polyoma virus transformed
0.0042
-
cell line HCT-8R, human intestinal carcinoma
0.0042
-
L-cells, Reovirus infected
0.005
-
cell line TR-3, transformed
0.005
-
cell line Raji, Burkitt lymphoma
0.0055
-
cell line MNNG/HOS, human osteosarcoma
0.0055
-
cell line P815, murine mastocytoma
0.0063
-
cell line MOLT-4
0.0063
-
cell line B-16 in vitro
2.4
-
cutaneous melanoma
2.4
mutant D133N, cosubstrate NADP+, pH 7.3
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Q183A
-
site-directed mutagenesis, the Gln183Ala variant exhibits a 6-10fold lower rate of folate reduction and bound CH2-H4folate with 7-fold lower affinity compared to wild-type enzyme. The oxidative half-reaction of the Gln183Ala mutant is considered reversible, and the enzyme can catalyze either of two half reactions involving folate: reduction of CH2-H4folate as part of the physiological oxidoreductase reaction or oxidation of CH3-H4folate as part of the CH3-H4folate-menadione oxidoreductase reaction, comparisons of half-reaction kinetics of wild-type and mutant enzymes
Q183E
-
site-directed mutagenesis, comparisons of half-reaction kinetics of wild-type and mutant enzymes, the Gln183Glu mutant displays catalytic constants within 3fold of the wild-type enzyme enzyme
C677T
-
one of several polymorphisms, leads to increased risk of hepatocellular carcinoma in patients with alcoholic cirrhosis, determination of genotypes in liver transplant patients with cirrhosis with and without hepatocellular carcinoma and in healthy persons
D133A
cosubstrate NAD+, 1.7% of wild-type activity, cosubstrate NADP+, 5.5% of wild-type activity
D133E
no enzymic activity
D133N
cosubstrate NAD+, 20.4% of wild-type activity, cosubstrate NADP+, 82.2% of wild-type activity
D133S
cosubstrate NAD+, 17.8% of wild-type activity, cosubstrate NADP+, 34.5% of wild-type activity
D190A
no enzymic activity
D190E
cosubstrate NAD+, 1% of wild-type activity
D190N
cosubstrate NAD+, 16% of wild-type activity
D190S
no enzymic activity
R166A
no enzymic activity
R166K
no enzymic activity
R166S
no enzymic activity
R198A
cosubstrate NAD+, 0.7% of wild-type activity, cosubstrate NADP+, 5.3% of wild-type activity
R198K
cosubstrate NAD+, 56% of wild-type activity, cosubstrate NADP+, 42% of wild-type activity
R198S
cosubstrate NAD+, 0.9% of wild-type activity, cosubstrate NADP+, 53% of wild-type activity
K56Q
-
inactivation of methenyltetrahydrofolate cyclohydrolase activity of bifunctional enzyme. Transfection with mutant enzyme rescues auxotrophy of enzyme-deficient fibroblasts, but only poorly. Rescued cells demonstrate a decrease in the ratio of incorporation of exogenous formate to serine
additional information
construction of a gene deletion mutant cell line, the cells can survive in liver and other tissues because the null defect is rescued by metabolites supplied by surrounding normal cells
additional information
-
primary fibroblasts from embryo of knock-out mice, spontaneous immortalization, the mutant cells require methionine and glycine for growth, glycine auxotrophy, replacement of mehtionine by homocysteine results in much lower enzyme activity, metabolism overview
additional information
-
enzyme deletion mutant, auxotroph for glycine
additional information
short hairpin RNAs (shRNAs) suppression of expression of Mthfd2 gene in E14 mouse embryonic stem cells (mESCs). Mthfd2 knockdown (KD) results in loss of typical stem cell morphology, with reduced alkaline phosphatase (AP) staining. The expression of pluripotency marker genes is downregulated and that of lineage marker genes upregulated, showing that Mthfd2 depletion results in differentiation of mESCs. Knockdown of Mthfd2 in another G4 mESC line shows results consistent with those in Mthfd2 KD E14 mESCs. Additionally, homozygous Mthfd2 knockout (KO) mESCs are characterized by the loss of typical mESC morphology, abnormal expression of marker genes, and compromised cell proliferation. Forced expression of Mthfd2 rescues the Mthfd2 KO-induced differentiation and compromised cell proliferation. In addition, MTHFD2 protein expression is gradually silenced during the differentiation of mESCs into embryoid bodies (EBs). Expression of Mthfd2 facilitates mouse induced pluripotent stem cells (iPSCs)induction, Mthfd2 promotes complete reprogramming of iPSCs and improves the quality of iPSCs. All iPSCs induced with Mthfd2 (OSKM2 iPSCs) show typical mESC-like morphology and express Oct4-driven GFP. Analysis of changes in the transcriptome due to suppression of Mthfd2. Mthfd2 depletion hinders DNA repair in mESCs
additional information
-
short hairpin RNAs (shRNAs) suppression of expression of Mthfd2 gene in E14 mouse embryonic stem cells (mESCs). Mthfd2 knockdown (KD) results in loss of typical stem cell morphology, with reduced alkaline phosphatase (AP) staining. The expression of pluripotency marker genes is downregulated and that of lineage marker genes upregulated, showing that Mthfd2 depletion results in differentiation of mESCs. Knockdown of Mthfd2 in another G4 mESC line shows results consistent with those in Mthfd2 KD E14 mESCs. Additionally, homozygous Mthfd2 knockout (KO) mESCs are characterized by the loss of typical mESC morphology, abnormal expression of marker genes, and compromised cell proliferation. Forced expression of Mthfd2 rescues the Mthfd2 KO-induced differentiation and compromised cell proliferation. In addition, MTHFD2 protein expression is gradually silenced during the differentiation of mESCs into embryoid bodies (EBs). Expression of Mthfd2 facilitates mouse induced pluripotent stem cells (iPSCs)induction, Mthfd2 promotes complete reprogramming of iPSCs and improves the quality of iPSCs. All iPSCs induced with Mthfd2 (OSKM2 iPSCs) show typical mESC-like morphology and express Oct4-driven GFP. Analysis of changes in the transcriptome due to suppression of Mthfd2. Mthfd2 depletion hinders DNA repair in mESCs
additional information
construction of the Mycobacterium smegmatis DELTAmsmeg_6596 strain. The mutant is partially auxotrophic for methionine and grows only poorly without methionine or without being complemented with a functional copy of MTHFR1 or MTHFR2. Furthermore, the DELTAmsmeg_6596 strain is more sensitive to folate pathway inhibitors (sulfachloropyridazine, p-aminosalicylic acid, sulfamethoxazole, and trimethoprim)
additional information
construction of the Mycobacterium smegmatis DELTAmsmeg_6596 strain. The mutant is partially auxotrophic for methionine and grows only poorly without methionine or without being complemented with a functional copy of MTHFR1 or MTHFR2. Furthermore, the DELTAmsmeg_6596 strain is more sensitive to folate pathway inhibitors (sulfachloropyridazine, p-aminosalicylic acid, sulfamethoxazole, and trimethoprim)
additional information
-
construction of the Mycobacterium smegmatis DELTAmsmeg_6596 strain. The mutant is partially auxotrophic for methionine and grows only poorly without methionine or without being complemented with a functional copy of MTHFR1 or MTHFR2. Furthermore, the DELTAmsmeg_6596 strain is more sensitive to folate pathway inhibitors (sulfachloropyridazine, p-aminosalicylic acid, sulfamethoxazole, and trimethoprim)
additional information
-
construction of the Mycobacterium smegmatis DELTAmsmeg_6596 strain. The mutant is partially auxotrophic for methionine and grows only poorly without methionine or without being complemented with a functional copy of MTHFR1 or MTHFR2. Furthermore, the DELTAmsmeg_6596 strain is more sensitive to folate pathway inhibitors (sulfachloropyridazine, p-aminosalicylic acid, sulfamethoxazole, and trimethoprim)
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Moore, M.R.; O'Brien, W.E.; Ljungdahl, L.G.
Purification and characterisation of nicotinamide adenine dinucleotide-dependent methylenetetrahydrofolate dehydrogenase from Clostridium formicoaceticum
J. Biol. Chem.
249
5250-5253
1974
Saccharomyces cerevisiae, Gottschalkia acidurici, Clostridium formicaceticum, Mus musculus
brenda
Ragsdale, S.W.; Ljungdahl, L.G.
Purification and properties of NAD-dependent 5,10-methylenetetrahydrofolate dehydrogenase from Acetobacterium woodii
J. Biol. Chem.
259
3499-3503
1984
Acetobacterium woodii, Saccharomyces cerevisiae, Clostridium formicaceticum, Mus musculus
brenda
Mejia, N.; Mackenzie, R.E.
NAD-dependent methylenetetrahydrofolate dehydrogenase is expressed by immortal cells
J. Biol. Chem.
260
14616-14620
1985
Cricetulus griseus, Cricetus cricetus, Homo sapiens, Mesocricetus auratus, Mus musculus, Rattus norvegicus
brenda
Mejia, N.; Rios-Orlandi, E.M.; Mackenzie, R.E.
NAD-dependent methylenetetrahydrofolate dehydrogenase-methenyltetrahydrofolate cyclohydrolase from ascites tumor cells. Purification and properties
J. Biol. Chem.
261
9509-9513
1986
Acetobacterium woodii, Clostridium formicaceticum, Mus musculus
brenda
Mackenzie, R.E.; Mejia, N.; Yang, X.M.
Methylenetetrahydrofolate dehydrogenases in normal and transformed mammalian cells
Adv. Enzyme Regul.
27
31-39
1988
Saccharomyces cerevisiae, Homo sapiens, Mus musculus
brenda
Mejia, N.; Mackenzie, R.E.
NAD-dependent methylenetetrahydrofolate dehydrogenase-methenyltetrahydrofolate cyclohydrolase in transformed cells is a mitochondrial enzyme
Biochem. Biophys. Res. Commun.
155
1-6
1988
Mus musculus
brenda
Rios-Orlandi, E.M.; Mackenzie, R.E.
The activities of the NAD-dependent methylenetetrahydrofolate dehydrogenase-methenyltetrahydrofolate cyclohydrolase from ascites tumor cells are kinetically independent
J. Biol. Chem.
263
4662-4667
1988
Mus musculus
brenda
Belanger, C.; Mackenzie, R.E.
Isolation and characterization of cDNA clones encoding the murine NAD-dependent methylenetetrahydrofolate dehydrogenase-methenyltetrahydrofolate cyclohydrolase
J. Biol. Chem.
264
4837-4843
1989
Mus musculus
brenda
Barlowe, C.K.; Appling, D.R.
Isolation and characterization of a novel eukaryotic monofunctional NAD+-dependent 5,10-methylenetetrahydrofolate dehydrogenase
Biochemistry
29
7089-7094
1990
Acetobacterium woodii, Saccharomyces cerevisiae, Clostridium formicaceticum, Homo sapiens, Rattus norvegicus, Saccharomyces cerevisiae KSY8
brenda
Smith, G.K.; Banks, S.D.; Monaco, T.J.; Rigual, R.; Duch, D.S.; Mullin, R.J.; Huber, B.E.
Activity of an NAD-dependent 5,10-methylenetetrahydrofolate dehydrogenase in normal tissue, neoplastic cells, and oncogene-transformed cells
Arch. Biochem. Biophys.
283
367-371
1990
Bos taurus, Homo sapiens, Mus musculus, Rattus norvegicus, Rattus norvegicus Fischer
brenda
Peri, K.G.; Mackenzie, R.E.
NAD(+)-dependent methylenetetrahydrofolate dehydrogenase-cyclohydrolase: detection of the mRNA in normal murine tissues and transcriptional regulation of the gene in cell lines
Biochim. Biophys. Acta
1171
281-287
1993
Homo sapiens, Mus musculus, Rattus norvegicus
brenda
Price, B.D.; Laughon, A.
The isolation and characterization of a Drosophila gene encoding a putative NAD-dependent methylenetetrahydrofolate dehydrogenase-methenyltetrahydrofolate cyclohydrolase
Biochim. Biophys. Acta
1173
94-98
1993
Drosophila melanogaster, Homo sapiens, Mus musculus
brenda
Yang, X.M.; Mackenzie, R.E.
NAD-dependent methylenetetrahydrofolate dehydrogenase-methenyltetrahydrofolate cyclohydrolase is the mammalian homolog of the mitochondrial enzyme encoded by the yeast MIS1 gene
Biochemistry
32
11118-11123
1993
Saccharomyces cerevisiae, Homo sapiens, Mus musculus
brenda
Tremblay, G.B.; Sohi, S.S.; Retnakaran, A.; Mackenzie, R.E.
NAD-dependent methylenetetrahydrofolate dehydrogenase-methenyltetrahydrofolate cyclohydrolase is targeted to the cytoplasm in insect cell lines
FEBS Lett.
368
177-182
1995
Antheraea eucalypti, Choristoneura fumiferana, Drosophila melanogaster, Homo sapiens, Malacosoma disstria, Mus musculus, Spodoptera frugiperda
brenda
Monzingo, A.F.; West, M.G.; Schelp, E.; Appling, D.R.; Robertus, J.D.
Crystallization of the NAD-dependent 5,10-methylenetetrahydrofolate dehydrogenase from Saccharomyces cerevisiae
Proteins
26
481-482
1996
Acetobacterium woodii, Saccharomyces cerevisiae
brenda
Appling, D.R.; West, M.G.
Monofunctional NAD-dependent 5,10-methylenetetrahydrofolate dehydrogenase from Saccharomyces cerevisiae
Methods Enzymol.
281
178-188
1997
Acetobacterium woodii, Saccharomyces cerevisiae, Clostridium formicaceticum, Drosophila melanogaster, Homo sapiens, Mus musculus
brenda
Mackenzie, R.E.
Mitochondrial NAD-dependent methylenetetrahydrofolate dehydrogenase-methenyltetrahydrofolate cyclohydrolase
Methods Enzymol.
281
171-177
1997
Drosophila melanogaster, Homo sapiens, Mus musculus, Saccharomyces cerevisiae, Spodoptera frugiperda
brenda
Di Pietro, E.; Sirois, J.; Trenblay, M.L.; Mackenzie, R.E.
Mitochondrial NAD-dependent methylenetetrahydrofolate dehydrogenase-methenyltetrahydrofolate cyclohydrolase is essential for embryonic development
Mol. Cell. Biol.
22
4158-4166
2002
Saccharomyces cerevisiae, Cricetulus griseus, Mus musculus
brenda
Patel, H.; Christensen, K.E.; Mejia, N.; Mackenzie, R.E.
Mammalian mitochondrial methylenetetrahydrofolate dehydrogenase-cyclohydrolase
Arch. Biochem. Biophys.
403
145-148
2002
Drosophila melanogaster, Homo sapiens, Mus musculus
brenda
Takeya, C.; Esumi, M.; Shiroishi, T.; Hishida, R.; Yamamoto, T.
Multiple single-nucleotide polymorphisms in the methylenetetrahydrofolate reductase and its truncated pseudogene of 23 inbred strains of mice
Biochem. Biophys. Res. Commun.
312
480-486
2003
Mus musculus (Q9WU20), Mus musculus
brenda
Di Pietro, E.; Wang, X.L.; MacKenzie, R.E.
The expression of mitochondrial methylenetetrahydrofolate dehydrogenase-cyclohydrolase supports a role in rapid cell growth
Biochim. Biophys. Acta
1674
78-84
2004
Mus musculus (P18155)
brenda
Saffroy, R.; Pham, P.; Chiappini, F.; Gross-Goupil, M.; Castera, L.; Azoulay, D.; Barrier, A.; Samuel, D.; Debuire, B.; Lemoine, A.
The MTHFR 677C > T polymorphism is associated with an increased risk of hepatocellular carcinoma in patients with alcoholic cirrhosis
Carcinogenesis
25
1443-1448
2004
Homo sapiens
brenda
Patel, H.; Pietro, E.D.; MacKenzie, R.E.
Mammalian fibroblasts lacking mitochondrial NAD+-dependent methylenetetrahydrofolate dehydrogenase-cyclohydrolase are glycine auxotrophs
J. Biol. Chem.
278
19436-19441
2003
Mus musculus
brenda
Patel, H.; Di Pietro, E.; Mejia, N.; MacKenzie, R.E.
NAD- and NADP-dependent mitochondrially targeted methylenetetrahydrofolate dehydrogenase-cyclohydrolases can rescue mthfd2 null fibroblasts
Arch. Biochem. Biophys.
442
133-139
2005
Mus musculus
brenda
Christensen, K.E.; Mirza, I.A.; Berghuis, A.M.; Mackenzie, R.E.
Magnesium and phosphate ions enable NAD binding to methylenetetrahydrofolate dehydrogenase-methenyltetrahydrofolate cyclohydrolase
J. Biol. Chem.
280
34316-34323
2005
Homo sapiens (P13995), Homo sapiens
brenda
Buchenau, B.; Thauer, R.K.
Tetrahydrofolate-specific enzymes in Methanosarcina barkeri and growth dependence of this methanogenic archaeon on folic acid or p-aminobenzoic acid
Arch. Microbiol.
182
313-325
2004
Methanosarcina barkeri (Q46A53), Methanosarcina barkeri DSM 804 (Q46A53)
brenda
Shin, M.; Momb, J.; Appling, D.R.
Human mitochondrial MTHFD2 is a dual redox cofactor-specific methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase
Cancer Metab.
5
11
2017
Homo sapiens (P13995), Homo sapiens (Q9H903)
brenda
Gustafsson, R.; Jemth, A.S.; Gustafsson, N.M.; Faernegardh, K.; Loseva, O.; Wiita, E.; Bonagas, N.; Dahllund, L.; Llona-Minguez, S.; Haeggblad, M.; Henriksson, M.; Andersson, Y.; Homan, E.; Helleday, T.; Stenmark, P.
Crystal structure of the emerging cancer target MTHFD2 in complex with a substrate-based inhibitor
Cancer Res.
77
937-948
2017
Homo sapiens (P13995)
brenda
Hitzel, J.; Lee, E.; Zhang, Y.; Bibli, S.I.; Li, X.; Zukunft, S.; Pflueger, B.; Hu, J.; Schuermann, C.; Vasconez, A.E.; Oo, J.A.; Kratzer, A.; Kumar, S.; Rezende, F.; Josipovic, I.; Thomas, D.; Giral, H.; Schreiber, Y.; Geisslinger, G.; Fork, C.; Yang, X.; Sigala, F.; Romanoski, C.E.; Kroll, J.; Jo, H.; Lan, L.a.n.d.
Oxidized phospholipids regulate amino acid metabolism through MTHFD2 to facilitate nucleotide release in endothelial cells
Nat. Commun.
9
2292
2018
Homo sapiens (P13995)
brenda
Zuo, C.; Jolly, A.L.; Nikolova, A.P.; Satzer, D.I.; Cao, S.; Sanchez, J.S.; Ballou, D.P.; Trimmer, E.E.
A role for glutamine 183 in the folate oxidative half-reaction of methylenetetrahydrofolate reductase from Escherichia coli
Arch. Biochem. Biophys.
642
63-74
2018
Escherichia coli
brenda
Sah, S.; Lahry, K.; Talwar, C.; Singh, S.; Varshney, U.
Monomeric NADH-oxidizing methylenetetrahydrofolate reductases from Mycobacterium smegmatis lack flavin coenzyme
J. Bacteriol.
202
e00709-19
2020
no activity by Mycobacterium smegmatis MSMEG_6664, no activity by Mycobacterium smegmatis MSMEI_6484, Mycolicibacterium smegmatis (A0R6M0), Mycolicibacterium smegmatis (A0R6S0), Mycolicibacterium smegmatis, Mycolicibacterium smegmatis ATCC 700084 (A0R6M0), Mycolicibacterium smegmatis ATCC 700084 (A0R6S0)
brenda
Yue, L.; Pei, Y.; Zhong, L.; Yang, H.; Wang, Y.; Zhang, W.; Chen, N.; Zhu, Q.; Gao, J.; Zhi, M.; Wen, B.; Zhang, S.; Xiang, J.; Wei, Q.; Liang, H.; Cao, S.; Lou, H.; Chen, Z.; Han, J.
Mthfd2 modulates mitochondrial function and DNA repair to maintain the pluripotency of mouse stem cells
Stem Cell Reports
15
529-545
2020
Mus musculus (P18155), Mus musculus
brenda