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Information on EC 1.5.1.20 - methylenetetrahydrofolate reductase [NAD(P)H] and Organism(s) Escherichia coli and UniProt Accession P0AEZ1
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1.5.1.20 methylenetetrahydrofolate reductase [NAD(P)H]IUBMB Comments
A flavoprotein (FAD). The enzyme catalyses the reversible conversion of 5,10-methylenetetrahydrofolate to 5-methyltetrahydrofolate, playing an important role in folate metabolism by regulating the distribution of one-carbon moieties between cellular methylation reactions and nucleic acid synthesis. This enzyme, characterized from Protozoan parasites of the genus Leishmania, is unique among similar characterized eukaryotic enzymes in that it lacks the C-terminal allosteric regulatory domain (allowing it to catalyse a reversible reaction) and uses NADH and NADPH with equal efficiency under physiological conditions. cf. EC 1.5.1.53, methylenetetrahydrofolate reductase (NADPH); EC 1.5.1.54, methylenetetrahydrofolate reductase (NADH); and EC 1.5.7.1, methylenetetrahydrofolate reductase (ferredoxin).
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Word Map
- 1.5.1.20
- nitrite
- homocysteine
- medicine
- paracoccus
-
assimilatory
-
denitrification
- chlorate
- narghi
-
resde
- napc
-
molybdoenzyme
- pantotrophus
-
ammonification
- nutrition
- analysis
The taxonomic range for the selected organisms is: Escherichia coli
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
Synonyms
respiratory nitrate reductase, 10-methylenetetrahydrofolate reductase, napab, met13, n5,n10-methylenetetrahydrofolate reductase, n5,10-methylenetetrahydrofolate reductase, methylenetetrahydrofolate reductase (nadph), atmthfr-1, 5,10-methylenetetrahydrofolate reductase (nadph), methylenetetrahydrofolic acid reductase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
5,10-CH2-H4folate reductase
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5,10-methylenetetrahydrofolate reductase
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5,10-methylenetetrahydrofolate reductase (NADPH)
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5,10-methylenetetrahydrofolic acid reductase
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-
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5,10-methylenetetrahydropteroylglutamate reductase
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5-methyltetrahydrofolate:NAD oxidoreductase
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5-methyltetrahydrofolate:NAD+ oxidoreductase
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5-methyltetrahydrofolate:NADP+ oxidoreductase
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methylenetetrahydrofolate (reduced riboflavin adenine dinucleotide) reductase
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methylenetetrahydrofolate reductase
methylenetetrahydrofolate reductase (NADPH)
methylenetetrahydrofolic acid reductase
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MTHFR
MTHFR2
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-
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N5,10-methylenetetrahydrofolate reductase
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N5,N10-methylenetetrahydrofolate reductase
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reductase, methylenetetrahydrofolate (reduced nicotinamide adenine dinucleotide phosphate)
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reductase, methylenetetrahydrofolate (reduced riboflavin adenine dinucleotide)
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methylenetetrahydrofolate reductase
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methylenetetrahydrofolate reductase (NADPH)
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MTHFR
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
5-methyltetrahydrofolate + NAD(P)+ = 5,10-methylenetetrahydrofolate + NAD(P)H + H+
ping-pong bi-bi mechanism, in which NAD(P)+ release precedes the binding of methylenetetrahydrofolate
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5-methyltetrahydrofolate + NAD(P)+ = 5,10-methylenetetrahydrofolate + NAD(P)H + H+
substrate binding and catalyic mechanism involve Asp120, half-reaction mechanisms
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5-methyltetrahydrofolate + NAD(P)+ = 5,10-methylenetetrahydrofolate + NAD(P)H + H+
NADH adopts a hairpin conformation and is sandwiched between a conserved phenylalanine, F223, and the isoalloxazine ring of FAD, resulting in a complex competent for hydride transfer. The binding sites of the two substrates overlap. Pinog-pong reaction is facilitated by motions of loops L2, L3, L4
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
redox reaction
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oxidation
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-
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reduction
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PATHWAY SOURCE
PATHWAYS
BRENDA
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SYSTEMATIC NAME
IUBMB Comments
5-methyltetrahydrofolate:NAD(P)+ oxidoreductase
A flavoprotein (FAD). The enzyme catalyses the reversible conversion of 5,10-methylenetetrahydrofolate to 5-methyltetrahydrofolate, playing an important role in folate metabolism by regulating the distribution of one-carbon moieties between cellular methylation reactions and nucleic acid synthesis. This enzyme, characterized from Protozoan parasites of the genus Leishmania, is unique among similar characterized eukaryotic enzymes in that it lacks the C-terminal allosteric regulatory domain (allowing it to catalyse a reversible reaction) and uses NADH and NADPH with equal efficiency under physiological conditions. cf. EC 1.5.1.53, methylenetetrahydrofolate reductase (NADPH); EC 1.5.1.54, methylenetetrahydrofolate reductase (NADH); and EC 1.5.7.1, methylenetetrahydrofolate reductase (ferredoxin).
CAS REGISTRY NUMBER
COMMENTARY
71822-25-8
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9028-69-7
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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 + NADH
5-methyltetrahydrofolate + NAD+
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-
-
?
5,10-methylenetetrahydrofolate + reduced acceptor
5-methyltetrahydrofolate + oxidized acceptor
5-methyltetrahydrofolate + NAD+
5,10-methylenetetrahydrofolate + NADH
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-
-
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r
5-methyltetrahydrofolate + NADP+
5,10-methylenetetrahydrofolate + NADPH
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-
-
-
?
5,10-methylenetetrahydrofolate + FADH2
5-methyltetrahydrofolate + FAD
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-
-
-
?
5,10-methylenetetrahydrofolate + FADH2
5-methyltetrahydrofolate + FAD
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biosynthesis of 5-methyltetrahydrofolate, a donor of methyl groups of methionine
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-
?
5,10-methylenetetrahydrofolate + NADH
5-methyltetrahydrofolate + NAD+
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-
-
-
?
5,10-methylenetetrahydrofolate + NADH
5-methyltetrahydrofolate + NAD+
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physiological direction is the 5-methyltetrahydrofolate formation by transfer of reducing equivalents from NADH to the enzyme-bound FAD and from reduced FAD to methylenetetrahydrofolate
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-
?
5,10-methylenetetrahydrofolate + reduced acceptor
5-methyltetrahydrofolate + oxidized acceptor
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-
-
-
?
5,10-methylenetetrahydrofolate + reduced acceptor
5-methyltetrahydrofolate + oxidized acceptor
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under anaerobic conditions and in absence of electron acceptors, the equilibrium lies far to the 5-methyltetrahydrofolate formation, inclusion of menadione or oxygen promotes the oxidation of 5-methyltetrahydrofolate
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r
5,10-methylenetetrahydrofolate + reduced acceptor
5-methyltetrahydrofolate + oxidized acceptor
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forward reaction: reduced acceptor is FADH2
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r
5,10-methylenetetrahydrofolate + reduced acceptor
5-methyltetrahydrofolate + oxidized acceptor
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forward reaction: reduced acceptor is FADH2
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r
5,10-methylenetetrahydrofolate + reduced acceptor
5-methyltetrahydrofolate + oxidized acceptor
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reverse reaction: menadione as electron acceptor
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r
5,10-methylenetetrahydrofolate + reduced acceptor
5-methyltetrahydrofolate + oxidized acceptor
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reverse reaction: menadione as electron acceptor
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r
5,10-methylenetetrahydrofolate + reduced acceptor
5-methyltetrahydrofolate + oxidized acceptor
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reverse reaction: menadione as electron acceptor
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r
5,10-methylenetetrahydrofolate + reduced acceptor
5-methyltetrahydrofolate + oxidized acceptor
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prefers NADH as reductant
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r
5,10-methylenetetrahydrofolate + reduced acceptor
5-methyltetrahydrofolate + oxidized acceptor
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forward reaction: NADPH as reduced acceptor
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?
5,10-methylenetetrahydrofolate + reduced acceptor
5-methyltetrahydrofolate + oxidized acceptor
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forward reaction: NADH as reduced acceptor
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?
5,10-methylenetetrahydrofolate + reduced acceptor
5-methyltetrahydrofolate + oxidized acceptor
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forward reaction: NADH as reduced acceptor
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r
additional information
?
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no direct activity with pyridine nucleotides
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?
additional information
?
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catalytic mechanism, Asp-120 and Glu-28 at the flavin active site are relevant to catalysis, Asp-120: located near the enzyme-bound FAD, role in catalysis of folate reduction and in stabilization of the folate intermediate 5-iminium cation, Glu-28: located near N10 of the folate, general acid catalyst to aid in 5-iminium cation formation
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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-methyltetrahydrofolate + NAD+
5,10-methylenetetrahydrofolate + NADH
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-
-
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r
5,10-methylenetetrahydrofolate + FADH2
5-methyltetrahydrofolate + FAD
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-
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?
5,10-methylenetetrahydrofolate + FADH2
5-methyltetrahydrofolate + FAD
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biosynthesis of 5-methyltetrahydrofolate, a donor of methyl groups of methionine
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-
?
5,10-methylenetetrahydrofolate + NADH
5-methyltetrahydrofolate + NAD+
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-
-
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?
5,10-methylenetetrahydrofolate + NADH
5-methyltetrahydrofolate + NAD+
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physiological direction is the 5-methyltetrahydrofolate formation by transfer of reducing equivalents from NADH to the enzyme-bound FAD and from reduced FAD to methylenetetrahydrofolate
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-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
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no direct activity with pyridine nucleotides: NADH, NADPH
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FAD
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FAD is essential for electron transfer between NADH and methylenetetrahydrofolate
FAD
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redox properties of enzyme-bound FAD are influenced by Asp120, which electrostatically stabilizes putative 5-iminium cation intermediate during catalysis
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
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vitamin B12 and methionine can repress enzyme biosynthesis
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
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redox potentials of wild-type and mutant enzymes, kinetic mechanism, and rapid-reaction kinetics for the half-reactions, steady-state kinetics
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0.02
NADH
cosubstrate 5,10-methylenetetrahydrofolate, wild-type, pH 7.2, 25°C
0.14
NADH
cosubstrate 5,10-methylenetetrahydrofolate, mutant F223A, pH 7.2, 25°C
0.236
NADH
cosubstrate 5,10-methylenetetrahydrofolate, mutant F223L, pH 7.2, 25°C
0.0004
methylenetetrahydrofolate
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recombinant wild-type enzyme, pH 7.2, 4°C
0.0035
NADH
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recombinant wild-type enzyme, pH 7.2, 4°C, the mutant enzymes all show a Km below 0.0035 mM
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
10.4
NADH
cosubstrate 5,10-methylenetetrahydrofolate, wild-type, pH 7.2, 25°C
14
NADH
cosubstrate 5,10-methylenetetrahydrofolate, mutant F223L, pH 7.2, 25°C
21.9
NADH
cosubstrate 5,10-methylenetetrahydrofolate, mutant F223A, pH 7.2, 25°C
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.014
NADH
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recombinant wild-type enzyme, pH 7.2, 4°C, the mutant enzymes all show a Km below 0.0035 mM
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
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alterations in the hydrophobic interactions by 1 M urea lead to dissociation of the native tetramer, resulting in stabilization of enzymatically active holoenzyme dimers, at 3 M urea followed by unfolding of the dimers to denatured monomers along with dissociation of FAD from the enzyme subunits, alterations of the electrostatic interactions by 1.2 M NaCl lead to dissociation of the enzyme into inactive, partially denatured dimers
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
ligand-free mutant F223L and mutant F223L/E28Q in complex with methylenetetrahydrofolate, to 1.65 and 1.7 A resolution, respectively. folate is bound in a catalytically competent conformation, and L223 undergoes a conformational change similar to that observed for F223 in the E28Q-methylenetetrahydrofolate structure
mutant A177V, free and in complex with 5,10-dideazafolate analogue LY309887
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
A177V
mutation does not affect Km or kcat values for NADH or 5,10-methylenetetrahydrofolate
F223A
mutation impairs both NADH and methylenetetrahydrofolate binding each 40fold and slows catalysis of both half-reactins less than 2fold
F223L
affinity for methylenetetrahydrofolate is unaffeacted. Mutant catalyzes the oxidative half-reaction 3fold faster than wild-type
A177V
D120A
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site-directed mutagenesis, decreased catalytic efficiency in the folate oxidative half-reaction, loss of negative charge near the flavin, small increasing effects on the NADH reductive half reaction
D120K
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site-directed mutagenesis, decreased catalytic efficiency in the folate oxidative half-reaction, loss of negative charge near the flavin, small increasing effects on the NADH reductive half reaction
D120N
D120S
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site-directed mutagenesis, decreased catalytic efficiency in the folate oxidative half-reaction, loss of negative charge near the flavin, small increasing effects on the NADH reductive half reaction
D120V
-
site-directed mutagenesis, decreased catalytic efficiency in the folate oxidative half-reaction, loss of negative charge near the flavin, small increasing effects on the NADH reductive half reaction
E28Q
D120N
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mutant with 150fold decreased activity in the physiological NADH-CH2-H4folate oxidoreductase reaction, enzyme is reduced by NADH 30% more rapidly than the wild-type enzyme, it binds methylenetetrahydrofolate in its ring-closed form, but no conversion to the 5-iminium cation, enzyme-bound FAD is more easily reduced and more difficult reoxidized than FAD of wild-type enzyme
D120N
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site-directed mutagenesis, decreased catalytic efficiency in the folate oxidative half-reaction, loss of negative charge near the flavin, small increasing effects on the NADH reductive half reaction
E28Q
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mutant enzyme is unable to catalyze reduction of methylenetetrahydrofolate and is inactive in the physiological NADH-CH2-H4folate oxidoreductase reaction, it binds methyltetrahydrofolate, but reduces not the FAD cofactor, 240fold decrease in NADH-menadione oxidoreductase activity
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
methyltetrahydrofolate and S-adenosylmethionine protects enzyme from the loss of FAD after dilution
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purification of wild-type and histidine-tagged D120N and E28Q mutant enzymes
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression of the D120N and E28Q mutant plasmids in Escherichia coli strain AB 1909
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expression of wild-type and mutant enzymes in Escherichia coli strain AB109 and AB1909-(DE3)7D
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RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
dissociated enzyme after treatment with 1 M urea, no refolding and renaturation is possible after treatment with 1.2 M NaCl
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Guenther, B.D.; Sheppard, C.A.; Tran, P.; Rozen, R.; Matthews, R.G.; Ludwig, M.L.
The structure and properties of methylenetetrahydrofolate reductase from Escherichia coli suggest how folate ameliorates human hyperhomocysteinemia
Nat. Struct. Biol.
6
359-365
1999
Escherichia coli (P0AEZ1)
Matthews, R.G.; Sheppard, C.; Goulding, C.
Methylenetetrahydrofolate reductase and methionine synthase: biochemistry and molecular biology
Eur. J. Pediatr.
157
54-59
1998
Escherichia coli, Homo sapiens, Sus scrofa
-
Buchanan, J.M.
Methionine biosynthesis (hog liver)
Methods Enzymol.
17B
371-378
1971
Escherichia coli, Sus scrofa, Escherichia coli 113-3
-
Katzen, H.M.; Buchanan, J.M.
Enzymatic synthesis of the methyl group of methionine. VIII. Repression derepression, purification, and properties of 5,10-methylene-tetrahydrofolate reductase from Escherichia coli
J. Biol. Chem.
240
825-835
1965
Escherichia coli, Escherichia coli 113-3
Roje, S.; Wang, H.; McNeil, S.D.; Raymond, R.K.; Appling, D.R.; Shachar-Hill, Y.; Bohnert, H.J.; Hanson, A.D.
Isolation, characterization, and functional expression of cDNAs encoding NADH-dependent methylenetetrahydrofolate reductase from higher plants
J. Biol. Chem.
274
36089-36096
1999
Arabidopsis sp., Escherichia coli, Zea mays (Q9SE94), Zea mays
Yamada, K.; Chen, Z.; Rozen, R.; Matthews, R.G.
Effects of common polymorphisms on the properties of recombinant human methylenetetrahydrofolate reductase
Proc. Natl. Acad. Sci. USA
98
14853-14858
2001
Escherichia coli, Homo sapiens
Trimmer, E.E.; Ballou, D.P.; Ludwig, M.L.; Matthews, R.G.
Folate activation and catalysis in methylenetetrahydrofolate reductase from Escherichia coli: Roles for aspartate 120 and glutamate 28
Biochemistry
40
6216-6226
2001
Escherichia coli
Misra, S.K.; Bhakuni, V.
Unique holoenzyme dimers of the tetrameric enzyme Escherichia coli methylenetetrahydrofolate reductase: characterization of structural features associated with modulation of the enzyme's function
Biochemistry
42
3921-3928
2003
Escherichia coli
Trimmer, E.E.; Ballou, D.P.; Galloway, L.J.; Scannell, S.A.; Brinker, D.R.; Casas, K.R.
Aspartate 120 of Escherichia coli methylenetetrahydrofolate reductase: evidence for major role in folate binding and catalysis and a minor role in flavin reactivity
Biochemistry
44
6809-6822
2005
Escherichia coli
Pejchal, R.; Sargeant, R.; Ludwig, M.L.
Structures of NADH and CH3-H4folate complexes of Escherichia coli methylenetetrahydrofolate reductase reveal a spartan strategy for a ping-pong reaction
Biochemistry
44
11447-11457
2005
Escherichia coli
Pejchal, R.; Campbell, E.; Guenther, B.D.; Lennon, B.W.; Matthews, R.G.; Ludwig, M.L.
Structural perturbations in the Ala --> Val polymorphism of methylenetetrahydrofolate reductase: how binding of folates may protect against inactivation
Biochemistry
45
4808-4818
2006
Escherichia coli
Kasap, M.; Sazci, A.; Ergul, E.; Akpinar, G.
Molecular phylogenetic analysis of methylenetetrahydrofolate reductase family of proteins
Mol. Phylogenet. Evol.
42
838-846
2007
Agrobacterium tumefaciens (Q7CXU3), Aquifex aeolicus (O67422), Arabidopsis thaliana (O80585), Aspergillus nidulans (Q5B0P7), Aspergillus oryzae (Q2UEQ8), Bacteroides thetaiotaomicron (Q8A146), Bifidobacterium longum (Q8G652), Bordetella bronchiseptica (A0A0H3LLF9), Bordetella parapertussis, Bos taurus (Q5I598), Bradyrhizobium japonicum (Q89UJ7), Brucella suis (A0A0H3G3R1), Caenorhabditis elegans (Q17693), Candida albicans (Q5AEI0), Candidatus Blochmannia floridanus (Q7VRL4), Caulobacter vibrioides (Q9A6F4), Chromobacterium violaceum (Q7NZF6), Collimonas fungivorans (Q6J6A1), Corynebacterium diphtheriae (Q6NGB6), Corynebacterium glutamicum (Q8NNM2), Coxiella burnetii (Q83A63), Desulfovibrio vulgaris (Q72DD2), Dictyostelium discoideum (Q54X84), Escherichia coli, Fusarium graminearum, Gloeobacter violaceus (Q7NMH7), Homo sapiens (P42898), Leptospira interrogans (Q9L5C1), Macaca fascicularis (Q60HE5), Macaca mulatta, Mesorhizobium loti (Q98K87), Methanosarcina mazei (Q8PZQ4), Mus musculus (Q9WU20), Oryza sativa (Q10BJ7), Pasteurella multocida (Q9CP31), Photorhabdus luminescens (Q7MYD0), Prochlorococcus marinus (Q7VE38), Pseudomonas syringae (Q87V72), Pyricularia grisea, Ralstonia solanacearum (Q8Y389), Rattus norvegicus, Rhodopirellula baltica (Q7UNJ7), Rhodopseudomonas palustris (Q6N3J2), Saccharomyces cerevisiae (P53128), Schizosaccharomyces pombe (Q10258), Shigella flexneri (Q0SY49), Sinorhizobium meliloti (Q92NK1), Streptococcus pneumoniae (Q8DQT1), Tetraodon nigroviridis (Q4T956), Thermus thermophilus (Q72H39), Vibrio cholerae (Q9KNP6), Vibrio parahaemolyticus (Q87L52), Vibrio vulnificus (Q7MH66), Wolinella succinogenes (Q7M8S8), Xenopus laevis (Q7ZWU2), Xylella fastidiosa (Q9PEA7), Zea mays (Q9SE94), [Candida] glabrata (Q6FU20)
Lee, M.N.; Takawira, D.; Nikolova, A.P.; Ballou, D.P.; Furtado, V.C.; Phung, N.L.; Still, B.R.; Thorstad, M.K.; Tanner, J.J.; Trimmer, E.E.
Functional role for the conformationally mobile phenylalanine 223 in the reaction of methylenetetrahydrofolate reductase from Escherichia coli
Biochemistry
48
7673-7685
2009
Escherichia coli (P0AEZ1)
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