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Information on EC 1.5.1.15 - methylenetetrahydrofolate dehydrogenase (NAD+)
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1.5.1.15 methylenetetrahydrofolate dehydrogenase (NAD+)Specify your search results
Word Map
- 1.5.1.15
- homocysteine
-
case-control
- women
- hyperhomocysteinemia
- leiden
- thrombosis
- pregnancy
- cardiovascular
-
meta-analysis
-
folic
- prothrombin
- artery
- venous
- thrombophilias
- children
-
ethnic
- coronary
-
homozygote
- stroke
-
pcr-rflp
- thromboembolism
-
caucasian
-
homozygosity
-
smoking
-
pubmed
-
anticoagulant
- thymidylate
-
prothrombotic
-
one-carbon
- methotrexate
-
thermolabile
-
remethylation
- pai-1
- cystathionine
-
reaction-restriction
-
gene-gene
-
embase
- miscarriage
-
antiphospholipid
- beta-synthase
- antithrombin
-
pharmacogenetic
- 5-methyltetrahydrofolate
-
hypercoagulable
-
fxiii
-
folate-dependent
- homocystinuria
- medicine
-
anticardiolipin
- hinfi
-
hypofibrinolysis
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Reaction Schemes
Synonyms
5,10-CH2-THF dehydrogenase, 5,10-methylenetetrahydrofolate reductase, bifunctional N5,N10-methylene-H4F dehydrogenase/N5,N10-methenyltetrahydrofolate cyclohydrolase, FolD, methylenetetrahydrofolate dehydrogenase-cyclohydrolase, methylenetetrahydrofolate dehydrogenase-methenyltetrahydrofolate cyclohydrolase, methylenetetrahydrofolate dehydrogenase/cyclohydrolase, methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase, methylenetetrahydrofolate reductase, methyleneTHF dehydrogenase, 
more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
bifunctional N5,N10-methylene-H4F dehydrogenase/N5,N10-methenyltetrahydrofolate cyclohydrolase
FolD
methylenetetrahydrofolate dehydrogenase-cyclohydrolase
methylenetetrahydrofolate dehydrogenase-methenyltetrahydrofolate cyclohydrolase
methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase
-
MTHFR
NMDMC
bifunctional N5,N10-methylene-H4F dehydrogenase/N5,N10-methenyltetrahydrofolate cyclohydrolase
bifunctional enzyme EC 1.5.1.15/EC 3.5.4.9
bifunctional N5,N10-methylene-H4F dehydrogenase/N5,N10-methenyltetrahydrofolate cyclohydrolase
bifunctional enzyme EC 1.5.1.15/EC 3.5.4.9
-
methylenetetrahydrofolate dehydrogenase-methenyltetrahydrofolate cyclohydrolase
-
-
methylenetetrahydrofolate dehydrogenase-methenyltetrahydrofolate cyclohydrolase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
5,10-methylenetetrahydrofolate + NAD+ = 5,10-methenyltetrahydrofolate + NADH + H+
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-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
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-
-
-
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Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYSTEMATIC NAME
IUBMB Comments
5,10-methylenetetrahydrofolate:NAD+ oxidoreductase
-
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CAS REGISTRY NUMBER
COMMENTARY
82062-90-6
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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-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+
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 + 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+
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-
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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
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-
-
-
r
L-5,10-methenyl-tetrahydrofolate + NADH
L-5,10-methylenetetrahydrofolate + NAD+
-
-
-
-
r
L-5,10-methenyl-tetrahydrofolate + NADH
L-5,10-methylenetetrahydrofolate + NAD+
-
-
-
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r
L-5,10-methenyl-tetrahydrofolate + NADH
L-5,10-methylenetetrahydrofolate + NAD+
-
-
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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+
-
-
-
-
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+
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-
392075, 392076, 392077, 392078, 392079, 392080, 392081, 392082, 392084, 392085, 392086, 392087, 392088, 392090, 392091, 392092, 392093
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-
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
-
-
-
-
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
?
-
-
active only with L-5,10-methylenetetrahydrofolate, the L-isomer does not affect the reaction
-
-
?
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
?
-
-
level of enzyme activity appears to be strain dependent with Swiss mice having the highest activity
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?
additional information
?
-
enzyme deficiency results in a number of diseases
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-
?
additional information
?
-
-
enzyme deficiency results in a number of diseases
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-
?
additional information
?
-
-
contains 2 enzymes, monofunctional NAD+ dependent dehydrogenase EC1.5.1.15 and trifunctional NADP+ dependent dehydrogenase, EC1.5.1.5
-
-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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 + 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+
-
-
-
-
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
-
-
-
-
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
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
FAD
required for enzyme stability, binding site comprises amino acid residues 95-228
NAD+
-
Ehrlich ascites tumor cells contains 2 enzymes, NAD+ dependent and NADP+ dependent dehydrogenase
NAD+
with NADP+ (1 mM), the enzyme shows less than 0.1% of the activity obtained with NAD+ (1 mM)
NAD+
the enzyme exhibits dual redox cofactor specificity, utilizing either NADP+ or NAD+. NAD+-dependent dehydrogenase activity of MTHFD2 with the substrate 5,10-methylenetetrahydropteroylglutamate is 8.5fold higher than its NADP+-dependent activity. While the NAD+-dependent activity of MTHFD2 slightly decreases, its maximal NADP+-dependent activity considerably increases with 5,10-methylenetetrahydropteroylpentaglutamate compared to 5,10-methylenetetrahydropteroylglutamate
NAD+
the enzyme exhibits dual redox cofactor specificity, utilizing either NADP+ or NAD+. NAD+-dependent dehydrogenase activity of MTHFD2L with the substrate 5,10-methylenetetrahydropteroylglutamat is 3.4fold higher than its NADP+-dependent activity under saturating substrate conditions. While the NAD+-dependent activity of MTHFD2 slightly decreases, its maximal NADP+-dependent activity considerably increases with 5,10-methylenetetrahydropteroylpentaglutamate compared to 5,10-methylenetetrahydropteroylglutamate
NADP+
the enzyme exhibits dual redox cofactor specificity, utilizing either NADP+ or NAD+. NAD+-dependent dehydrogenase activity of MTHFD2 with the substrate 5,10-methylenetetrahydropteroylglutamate is 8.5fold higher than its NADP+-dependent activity. While the NAD+-dependent activity of MTHFD2 slightly decreases, its maximal NADP+-dependent activity considerably increases with 5,10-methylenetetrahydropteroylpentaglutamate compared to 5,10-methylenetetrahydropteroylglutamate
NADP+
the enzyme exhibits dual redox cofactor specificity, utilizing either NADP+ or NAD+. NAD+-dependent dehydrogenase activity of MTHFD2L with the substrate 5,10-methylenetetrahydropteroylglutamate is 3.4fold higher than its NADP+-dependent activity under saturating substrate conditions. While the NAD+-dependent activity of MTHFD2 slightly decreases, its maximal NADP+-dependent activity considerably increases with 5,10-methylenetetrahydropteroylpentaglutamate compared to 5,10-methylenetetrahydropteroylglutamate
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
Mn2+
Mg2+
-
NAD+ dependent enzyme from Ehrlich ascites tumor cells requires Mg2+ or Mn2+ for activity
Mn2+
-
NAD+ dependent enzyme from Ehrlich ascites tumor cells requires Mg2+ or Mn2+ for activity
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(2S)-2-[[4-[(6aR)-3-amino-1,9-dioxo-5,6,6a,7-tetrahydro-4H-imidazo[1,5-f]pteridin-8-yl]benzoyl]amino]pentanedioic acid
i.e. LY345899
S-adenosyl-L-methionine
allosteric inhibitor, enzyme contains a binding site at the C-terminus
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
phosphate
-
absolute requirement, phosphate can be replaced by its analog arsenate
phosphate
absolutely required, binds in close proximity to the 2Ć¢ĀĀ-hydroxyl of NAD through interactions with R166 and R198. Km-value of wild-type 0.412 mM
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
5,10-methylenetetrahydrofolate
pH 6.0, 37ĆĀ°C, the Km-value for 5,10-methylenetetrahydrofolate in the presence of 2.7 mM NAD+ is below 0.005 mM
0.123
5,10-methylenetetrahydropteroylglutamate
pH 8.0, 30ĆĀ°C, at saturating concentrations of NADP+ (6.0 mM)
0.133
5,10-methylenetetrahydropteroylglutamate
pH 8.0, 30ĆĀ°C, at saturating concentrations of NAD+ (1.0 mM)
0.302
5,10-methylenetetrahydropteroylpentaglutamate
pH 8.0, 30ĆĀ°C, at saturating concentrations of NADP+ (6.0 mM)
0.359
5,10-methylenetetrahydropteroylpentaglutamate
pH 8.0, 30ĆĀ°C, at saturating concentrations of NAD+ (1.0 mM)
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1.5
5,10-methylenetetrahydropteroylglutamate
pH 8.0, 30ĆĀ°C, at saturating concentrations of NADP+ (6.0 mM)
12.4
5,10-methylenetetrahydropteroylglutamate
pH 8.0, 30ĆĀ°C, at saturating concentrations of NAD+ (1.0 mM)
6.4
5,10-methylenetetrahydropteroylpentaglutamate
pH 8.0, 30ĆĀ°C, at saturating concentrations of NADP+ (6.0 mM)
15.4
5,10-methylenetetrahydropteroylpentaglutamate
pH 8.0, 30ĆĀ°C, at saturating concentrations of NAD+ (1.0 mM)
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
12
5,10-methylenetetrahydropteroylglutamate
pH 8.0, 30ĆĀ°C, at saturating concentrations of NADP+ (6.0 mM)
93
5,10-methylenetetrahydropteroylglutamate
pH 8.0, 30ĆĀ°C, at saturating concentrations of NAD+ (1.0 mM)
21
5,10-methylenetetrahydropteroylpentaglutamate
pH 8.0, 30ĆĀ°C, at saturating concentrations of NADP+ (6.0 mM)
43
5,10-methylenetetrahydropteroylpentaglutamate
pH 8.0, 30ĆĀ°C, at saturating concentrations of NAD+ (1.0 mM)
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.0002
0.0003
0.0004
0.0005
0.0012
0.0015
0.0039
0.0042
0.005
0.0055
0.0063
2.4
5
pH 6.0, 37ĆĀ°C, extract from Escherichia coli cells carrying the expression vector
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
8
-
enzyme activity decreases approximately 2fold at pH 7.0 or pH 9.0
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
45
-
activity increases to the optimum, above 45ĆĀ°C the enzyme begins to denature
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
spruce budworm, cell lines IPRI CF1, IPRI CF16T, IPRI CF124T, FPMI-CF-70, FPMI-CF-27 and FPMI-34
-
-
brenda
black bellied hamster, cell line HA-Py(T), a polyoma virus-transformed hamster embryo fibroblast
-
-
brenda
normal human fibroblasts MCH-39, EBV-transformed normal human lymphoblast lines TL3 and TL4, human tumor lines MNNG/HOS(TE85 clone F-5), MCF-7, CCRF-CEM, osteosarcoma MG-63(ATCC CRL 1427), human chronic myeolitic leukemia line K562, Burkitt lymphoma line Raji, human choriocarcinoma BeWo, human intestinal carcinoma HCT
-
-
brenda
bifunctional NAD-dependent methylenetetrahydrofolate dehydrogenase-methenyltetrahydrofolate cyclohydrolase
-
-
brenda
C57 black mice, murine ascites tumor lines, T-cell lymphoma EL4, Moloney virus-induced lymphoma YAC, mouse melanoma M4(original designation RPMI 7272), 3T3-SV40
-
-
brenda
mouse, Ehrlich ascites tumor cells
-
-
brenda
murine cell lines NIH 3T3, Balb/C 3T3, Balb/C 3T3-SV-T2(SV40-transformed), C3H 10T1/2, YAC(Moloney virus transformed), PSI-2(a murine ecotropic packaging cell line)
-
-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
both Mthfd2 and Mthfd2l are expressed during embryogenesis but differ in timing of expression. Mthfd2l expression is low in early developmental stages but begins to increase at embryonic day 10.5 and remains elevated through birth while Mthfd2 is expressed more abundantly during early developmental stages and begins to taper off, with little or no expression observed in most adult tissues
brenda
-
enzyme is expressed during embryogenesis and in all immortilized cells
brenda
enzyme is mainly expressed during embryogenesis for purine synthesis
brenda
additional information
upregulation and overexpression in cancer cells
brenda
additional information
-
cell growth studies, wild-type and mutant cell lines, overview
brenda
additional information
expression pattern analysis, elevated enzyme expression in tumour cells due to different folate-mediated support of purine synthesis compared to normal cells
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
-
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
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 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
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). MTD1_DICDI
313
0
35069
Swiss-Prot
other Location (Reliability: 1)
MTD1_SCHPO
Schizosaccharomyces pombe (strain 972 / ATCC 24843)
320
0
35814
Swiss-Prot
other Location (Reliability: 3)
MTD1_YEAST
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
320
0
36240
Swiss-Prot
other Location (Reliability: 2)
MTD2L_CALJA
347
0
37342
Swiss-Prot
Mitochondrion (Reliability: 1)
MTD2L_HUMAN
347
0
37315
Swiss-Prot
Mitochondrion (Reliability: 1)
MTD2L_MOUSE
338
0
36438
Swiss-Prot
Mitochondrion (Reliability: 2)
MTD2L_RAT
338
0
36426
Swiss-Prot
Mitochondrion (Reliability: 2)
MTDC_BOVIN
350
0
37767
Swiss-Prot
Mitochondrion (Reliability: 1)
MTDC_CHICK
337
0
36411
Swiss-Prot
Mitochondrion (Reliability: 1)
MTDC_DROME
309
0
33551
Swiss-Prot
other Location (Reliability: 2)
MTDC_HUMAN
350
0
37895
Swiss-Prot
Mitochondrion (Reliability: 2)
MTDC_MOUSE
350
0
37863
Swiss-Prot
Mitochondrion (Reliability: 2)
A0A0F8B4W0_CERFI
333
0
37114
TrEMBL
other Location (Reliability: 2)
Q8KEH0_CHLTE
Chlorobaculum tepidum (strain ATCC 49652 / DSM 12025 / NBRC 103806 / TLS)
296
0
33244
TrEMBL
-
M5BLC9_THACB
Thanatephorus cucumeris (strain AG1-IB / isolate 7/3/14)
363
0
39362
TrEMBL
other Location (Reliability: 2)
A2R8J8_ASPNC
Aspergillus niger (strain CBS 513.88 / FGSC A1513)
334
0
36984
TrEMBL
other Location (Reliability: 2)
A0A3G2RZP1_9BASI
393
0
43096
TrEMBL
other Location (Reliability: 2)
A0A0B7FU61_THACB
Thanatephorus cucumeris (strain AG1-IB / isolate 7/3/14)
363
0
39334
TrEMBL
other Location (Reliability: 2)
A0A1S7UI93_ROSNE
329
0
36531
TrEMBL
other Location (Reliability: 2)
K0KLD5_WICCF
Wickerhamomyces ciferrii (strain F-60-10 / ATCC 14091 / CBS 111 / JCM 3599 / NBRC 0793 / NRRL Y-1031)
310
0
34393
TrEMBL
other Location (Reliability: 2)
A0A0F4YN84_TALEM
336
0
37489
TrEMBL
other Location (Reliability: 2)
A1Z9B4_DROME
122
1
13353
TrEMBL
Secretory Pathway (Reliability: 1)
A0A1Z5K4A0_FISSO
364
1
40689
TrEMBL
other Location (Reliability: 2)
A0A1H6PI72_YARLL
325
0
36208
TrEMBL
other Location (Reliability: 2)
W1QBS2_OGAPD
Ogataea parapolymorpha (strain ATCC 26012 / BCRC 20466 / JCM 22074 / NRRL Y-7560 / DL-1)
305
0
34102
TrEMBL
other Location (Reliability: 4)
C5P087_COCP7
Coccidioides posadasii (strain C735)
345
0
38401
TrEMBL
other Location (Reliability: 2)
A0A084FY34_PSEDA
329
0
36390
TrEMBL
other Location (Reliability: 2)
B8BT80_THAPS
266
0
29926
TrEMBL
other Location (Reliability: 1)
Q7JRN6_DROME
223
1
24828
TrEMBL
Secretory Pathway (Reliability: 1)
B8Y659_LEIDO
475
0
50730
TrEMBL
Mitochondrion (Reliability: 3)
Q4WC87_ASPFU
Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100)
298
0
33064
TrEMBL
other Location (Reliability: 2)
A0A1Z5JE80_FISSO
364
0
40578
TrEMBL
other Location (Reliability: 2)
C1LFF7_SCHJA
333
0
35994
TrEMBL
other Location (Reliability: 4)
FOLD_METBF
Methanosarcina barkeri (strain Fusaro / DSM 804)
287
0
31051
Swiss-Prot
-
MTHR_MOUSE
654
0
74580
Swiss-Prot
other Location (Reliability: 3)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
33000 - 38000
34000
34000
-
2 * 34000, native bifunctional enzyme, associated with cyclohydrolase, SDS-PAGE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
dimer
-
2 * 34000, native bifunctional enzyme, associated with cyclohydrolase, SDS-PAGE
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystal structure of the enzyme (MTHFD2) in complex with a substrate-based inhibitor and the enzyme cofactors NAD+ and inorganic phosphate
protein crystallized from 7% PEG 8000 in 50 mM Tris-HCl, pH 8.2 at 4ĆĀ°C in both hanging and sitting drop conditions, space group P4212 with cell constants a/b/c 75.9/75,9/160.0 A, crystals diffract to 2.9 A resolution, crystals form as tetragonal bipyramids and may grow as large as 0.45 mm on a side
-
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
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
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
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
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
8
-
enzyme activity decreases approximately 2fold at pH 7.0 or pH 9.0
392083
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
50
-
stable for 30 min at temperatures below, loses 25% of its activity during incubation
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
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OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-80ĆĀ°C, enzyme is stable in 20-30% glycerol buffer and can be frozen for months without loss of activity
-
4ĆĀ°C, can be stored dissolved in 0.1 M potassium maleate, pH 7.0 for at least 1 month without significant loss of activity
-
4ĆĀ°C, enzyme activity is stable for several weeks after storage in the final elution buffer
-
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
native enzyme from yeast as well as recombinant yest enzyme expressed in Escherichia coli
-
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
heterologously overproduced in Escherichia coli with a C-terminal His6-tag
isolation of cDNA and the gene encoding the murine cytoplasmic methylenetetrahydrofolate dehydrogenase-methenyltetrahydrofolate cyclohydrolase-formyltetrahydrofolate synthetase (DCS)
-
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
medicine
-
enzyme distribution suggests it can be useful as an oncodevelopmental marker
medicine
-
enzyme distribution suggests it can be useful as an oncodevelopmental marker
medicine
-
NAD+ dependent isoenzyme is genuinely tumor-specific, it may provide a novel therapeutic target for cancer therapy and/or an important diagnostic tool
medicine
-
NAD+ dependent isoenzyme is genuinely tumor-specific, it may provide a novel therapeutic target for cancer therapy and/or an important diagnostic tool
-
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
Homo sapiens, Mus musculus, Saccharomyces cerevisiae
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
Homo sapiens, Mus musculus, Saccharomyces cerevisiae
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
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Mackenzie, R.E.
Mitochondrial NAD-dependent methylenetetrahydrofolate dehydrogenase-methenyltetrahydrofolate cyclohydrolase
Methods Enzymol.
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171-177
1997
Saccharomyces cerevisiae, Drosophila melanogaster, Homo sapiens, Mus musculus, 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
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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.
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11
2017
Homo sapiens (P13995), Homo sapiens (Q9H903)
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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)
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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)
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