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Enzyme Nomenclature
Information on EC 1.5.1.15 - methylenetetrahydrofolate dehydrogenase (NAD+)
for references in articles please use BRENDA:EC1.5.1.15
Word Map on EC 1.5.1.15
- 1.5.1.15
- homocysteine
-
odds
- women
-
case-control
- hyperhomocysteinemia
-
leiden
- thrombosis
- cardiovascular
- artery
-
prothrombin
-
folic
- thrombophilias
- children
-
meta-analysis
- venous
- pregnancy
-
homozygote
- coronary
- stroke
- thromboembolism
-
caucasian
-
smoking
-
ethnic
-
pcr-rflp
-
homozygosity
- methotrexate
-
anticoagulant
-
one-carbon
-
thermolabile
- cystathionine
-
prothrombotic
-
antithrombin
- thymidylate
-
pharmacogenetic
-
gene-gene
-
reaction-restriction
-
hypercoagulable
-
antiphospholipid
-
beta-synthase
- 5-methyltetrahydrofolate
-
remethylation
-
spina
- medicine
- bifida
-
fxiii
-
hypofibrinolysis
-
fortification
- homocystinuria
- hinfi
-
folate-dependent
-
anticardiolipin
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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
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EC NUMBER 
COMMENTARY 
1.5.1.15
-
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RECOMMENDED NAME
GeneOntology No.
methylenetetrahydrofolate dehydrogenase (NAD+)
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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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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
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SYSTEMATIC NAME
IUBMB Comments
5,10-methylenetetrahydrofolate:NAD+ oxidoreductase
-
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CAS REGISTRY NUMBER
COMMENTARY
82062-90-6
-
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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
-
-
black bellied hamster, cell line HA-Py(T), a polyoma virus-transformed hamster embryo fibroblast
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-
human; 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
-
-
bifunctional NAD-dependent methylenetetrahydrofolate dehydrogenase-methenyltetrahydrofolate cyclohydrolase
-
-
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; cell lines YAC, P815; DBA mice, mastocyma P815 (ATCC TIB 64); Ehrlich ascites line Swiss mice; mouse, Ehrlich ascites tumor cells
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-
mouse, Ehrlich ascites tumor cells
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-
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)
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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-methylenetetrahydrofolate + NADP+
5,10-methenyltetrahydrofolate + NADPH + H+
about 15% of the rate with NAD+
-
-
?
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
-
-
?
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+
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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-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
-
-
-
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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-
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NATURAL SUBSTRATES
NATURAL PRODUCTS
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
P18155
enzyme provides one-carbon units for purine synthesis during embryogenesis, metabolism overview
-
-
?
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
?
-
Q9WU20
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)
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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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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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 2’-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, 37°C, the Km-value for 5,10-methylenetetrahydrofolate in the presence of 2.7 mM NAD+ is below 0.005 mM
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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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, 37°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 45°C the enzyme begins to denature
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
enzyme is mainly expressed during embryogenesis for purine synthesis
additional information
expression pattern analysis, elevated enzyme expression in tumour cells due to different folate-mediated support of purine synthesis compared to normal cells
additional information
-
cell growth studies, wild-type and mutant cell lines, overview
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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PDB
SCOP
CATH
UNIPROT
ORGANISM
Saccharomyces cerevisiae (strain ATCC 204508 / S288c);
Q02046
Saccharomyces cerevisiae (strain ATCC 204508 / S288c);
Q02046
Saccharomyces cerevisiae (strain ATCC 204508 / S288c);
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
33000 - 38000
34000
34000
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2 * 34000, native bifunctional enzyme, associated with cyclohydrolase, SDS-PAGE
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
dimer
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2 * 34000, native bifunctional enzyme, associated with cyclohydrolase, SDS-PAGE
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Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
protein crystallized from 7% PEG 8000 in 50 mM Tris-HCl, pH 8.2 at 4°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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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
8
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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
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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
-80°C, enzyme is stable in 20-30% glycerol buffer and can be frozen for months without loss of activity
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4°C, can be stored dissolved in 0.1 M potassium maleate, pH 7.0 for at least 1 month without significant loss of activity
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4°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
DNA sequencing; isolation of cDNA and the gene encoding the murine cytoplasmic methylenetetrahydrofolate dehydrogenase-methenyltetrahydrofolate cyclohydrolase-formyltetrahydrofolate synthetase (DCS)
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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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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
C677T
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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
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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
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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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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
medicine
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enzyme distribution suggests it can be useful as an oncodevelopmental marker
medicine
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enzyme distribution suggests it can be useful as an oncodevelopmental marker
medicine
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NAD+ dependent isoenzyme is genuinely tumor-specific, it may provide a novel therapeutic target for cancer therapy and/or an important diagnostic tool
medicine
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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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LINKS TO OTHER DATABASES (specific for EC-Number 1.5.1.15)
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