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2 [methionine synthase]-cob(II)alamin + NADPH + H+ + 2 S-adenosyl-L-methionine
2 [methionine synthase]-methylcob(I)alamin + 2 S-adenosylhomocysteine + NADP+
Substrates: -
Products: -
?
2 [methionine synthase]-methylcob(I)alamin + 2 S-adenosylhomocysteine + NADP+
2 [methionine synthase]-cob(II)alamin + NADPH + H+ + 2 S-adenosyl-L-methionine
[methionine synthase]-cob(II)alamin + NADH + S-adenosyl-L-methionine
[methionine synthase]methylcob(I)alamin + S-adenosylhomocysteine + NAD+
-
Substrates: -
Products: -
?
[Methionine synthase]-cob(II)alamin + NADPH + S-adenosyl-L-methionine
?
[Methionine synthase]-cob(II)alamin + NADPH + S-adenosyl-L-methionine
[Methionine synthase]methylcob(I)alamin + S-adenosylhomocysteine + NADP+
[methionine synthase]-cob(II)alamin + NADPH + S-adenosylmethionine
[methionine synthase]-methylcob(I)alamin + NADPH + S-adenosylhomocysteine
-
Substrates: in presence of methionine synthase reductase, holoenzyme formation from apomethionine synthase and methylcobalamin is significantly enhanced due to stabilization of apomethionine synthase. In addition to reductase activity, methionine synthase reductase serves as a special chaperone for methionine synthase. It also has reductase activity for the reaction of aquacobalamin to cob(II)alamin
Products: -
?
[methionine synthase]-cob(II)alamin + S-adenosyl-L-methionine + 2,6-dichlorophenolindophenol
[methionine synthase]methylcob(I)alamin + S-adenosylhomocysteine + ?
Substrates: -
Products: -
?
[methionine synthase]-cob(II)alamin + S-adenosyl-L-methionine + 3-acetylpyridine adenine dinucleotide phosphate
[methionine synthase]methylcob(I)alamin + S-adenosylhomocysteine + ?
Substrates: -
Products: -
?
[methionine synthase]-cob(II)alamin + S-adenosyl-L-methionine + doxorubicin
[methionine synthase]methylcob(I)alamin + S-adenosylhomocysteine + ?
Substrates: -
Products: -
?
[methionine synthase]-cob(II)alamin + S-adenosyl-L-methionine + ferricyanide
[methionine synthase]methylcob(I)alamin + S-adenosylhomocysteine + ?
Substrates: -
Products: -
?
[methionine synthase]-cob(II)alamin + S-adenosyl-L-methionine + menadione
[methionine synthase]methylcob(I)alamin + S-adenosylhomocysteine + ?
Substrates: -
Products: -
?
[methionine synthase]-methylcob(I)alamin + S-adenosylhomocysteine + NADP+
[methionine synthase]-cob(II)alamin + NADPH + S-adenosyl-L-methionine
additional information
?
-
2 [methionine synthase]-methylcob(I)alamin + 2 S-adenosylhomocysteine + NADP+
2 [methionine synthase]-cob(II)alamin + NADPH + H+ + 2 S-adenosyl-L-methionine
Substrates: -
Products: -
?
2 [methionine synthase]-methylcob(I)alamin + 2 S-adenosylhomocysteine + NADP+
2 [methionine synthase]-cob(II)alamin + NADPH + H+ + 2 S-adenosyl-L-methionine
Substrates: the enzyme catalyzes the oxidation of NADPH and shuttles electrons via its FAD and FMN cofactors to inactive MScob(II)alamin
Products: -
?
2 [methionine synthase]-methylcob(I)alamin + 2 S-adenosylhomocysteine + NADP+
2 [methionine synthase]-cob(II)alamin + NADPH + H+ + 2 S-adenosyl-L-methionine
Substrates: the enzyme transfers reducing equivalents from NADPH via an FAD and FMN cofactor to a redox partner protein. hydride transfer from NADPH to FAD requires displacement of a conserved tryptophan that lies coplanar to the FAD isoalloxazine ring
Products: -
?
[Methionine synthase]-cob(II)alamin + NADPH + S-adenosyl-L-methionine
?
-
Substrates: the enzyme is involved in reductive activation of methionine synthase:
Products: -
?
[Methionine synthase]-cob(II)alamin + NADPH + S-adenosyl-L-methionine
?
Substrates: the enzyme is involved in reductive activation of methionine synthase:
Products: -
?
[Methionine synthase]-cob(II)alamin + NADPH + S-adenosyl-L-methionine
?
Substrates: patients of the cblE complementation group of disorders of folate/cobalamin metabolism who are defective in reductive activation of methionine synthase exhibit megablastic anemia, developmental delay, hyperhomocysteinemia, and hypomethioninemia
Products: -
?
[Methionine synthase]-cob(II)alamin + NADPH + S-adenosyl-L-methionine
[Methionine synthase]methylcob(I)alamin + S-adenosylhomocysteine + NADP+
-
Substrates: -
Products: -
?
[Methionine synthase]-cob(II)alamin + NADPH + S-adenosyl-L-methionine
[Methionine synthase]methylcob(I)alamin + S-adenosylhomocysteine + NADP+
Substrates: -
Products: -
?
[methionine synthase]-methylcob(I)alamin + S-adenosylhomocysteine + NADP+
[methionine synthase]-cob(II)alamin + NADPH + S-adenosyl-L-methionine
-
Substrates: -
Products: -
r
[methionine synthase]-methylcob(I)alamin + S-adenosylhomocysteine + NADP+
[methionine synthase]-cob(II)alamin + NADPH + S-adenosyl-L-methionine
-
Substrates: MSR is a NADPH-dependent diflavin oxidoreductase required for the reductive regeneration of catalytically inert cob(II)alamin to cob(I)alamin, complex formation between the substrate's activation domain and MSR, and the substrate's activation domain and the isolated FMN-binding domain of MSR. Weshow that the MS activation domain interacts directly with the FMN-binding domain of MSR, overview
Products: -
r
[methionine synthase]-methylcob(I)alamin + S-adenosylhomocysteine + NADP+
[methionine synthase]-cob(II)alamin + NADPH + S-adenosyl-L-methionine
-
Substrates: interaction of the enzyme with the substrate enzyme methionine synthase via the C-terminal domain involves the residues K987 and K1071, interaction with substrate mutants K987T and K1071T is affected, structure-function relationship, overview
Products: -
r
[methionine synthase]-methylcob(I)alamin + S-adenosylhomocysteine + NADP+
[methionine synthase]-cob(II)alamin + NADPH + S-adenosyl-L-methionine
-
Substrates: MSR is a flavoprotein that regenerates the active form of cobalamin-dependent methionine synthase
Products: -
r
additional information
?
-
Substrates: difference in the relative efficiency of the very common polymorphic variant of the enzyme, I22M, suggests a molecular mechanism underlying the risk associated wiith the M22 allele for mild hyperhomocysteinemia
Products: -
?
additional information
?
-
-
Substrates: difference in the relative efficiency of the very common polymorphic variant of the enzyme, I22M, suggests a molecular mechanism underlying the risk associated wiith the M22 allele for mild hyperhomocysteinemia
Products: -
?
additional information
?
-
-
Substrates: biological implications of an attenuated mechanism of MS reactivation by MSR on methionine and folate metabolism, overview
Products: -
?
additional information
?
-
-
Substrates: the enzyme catalyzes also the inhibition of reduction of cytochrome c3+
Products: -
?
additional information
?
-
Substrates: the enzyme catalyzes the reduction of cytochrome c3+ with NADPH and NADH
Products: -
?
additional information
?
-
-
Substrates: the enzyme catalyzes the reduction of cytochrome c3+ with NADPH and NADH
Products: -
?
additional information
?
-
Substrates: the enzyme catalyzes the reduction of cytochrome c3+ with NADPH and NADH
Products: -
?
additional information
?
-
Substrates: fully reduced enzyme reaction with excess of cytochrome c, kinetics, overview. The NADPH-bound, fully reduced MSR completes most of its first turnover within the mixing dead time of the instrument, leaving only approximately 28% of the first turnover observable
Products: -
?
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2 [methionine synthase]-cob(II)alamin + NADPH + H+ + 2 S-adenosyl-L-methionine
2 [methionine synthase]-methylcob(I)alamin + 2 S-adenosylhomocysteine + NADP+
Substrates: -
Products: -
?
2 [methionine synthase]-methylcob(I)alamin + 2 S-adenosylhomocysteine + NADP+
2 [methionine synthase]-cob(II)alamin + NADPH + H+ + 2 S-adenosyl-L-methionine
Substrates: -
Products: -
?
[Methionine synthase]-cob(II)alamin + NADPH + S-adenosyl-L-methionine
?
[methionine synthase]-methylcob(I)alamin + S-adenosylhomocysteine + NADP+
[methionine synthase]-cob(II)alamin + NADPH + S-adenosyl-L-methionine
additional information
?
-
[Methionine synthase]-cob(II)alamin + NADPH + S-adenosyl-L-methionine
?
-
Substrates: the enzyme is involved in reductive activation of methionine synthase:
Products: -
?
[Methionine synthase]-cob(II)alamin + NADPH + S-adenosyl-L-methionine
?
Substrates: the enzyme is involved in reductive activation of methionine synthase:
Products: -
?
[Methionine synthase]-cob(II)alamin + NADPH + S-adenosyl-L-methionine
?
Substrates: patients of the cblE complementation group of disorders of folate/cobalamin metabolism who are defective in reductive activation of methionine synthase exhibit megablastic anemia, developmental delay, hyperhomocysteinemia, and hypomethioninemia
Products: -
?
[methionine synthase]-methylcob(I)alamin + S-adenosylhomocysteine + NADP+
[methionine synthase]-cob(II)alamin + NADPH + S-adenosyl-L-methionine
-
Substrates: -
Products: -
r
[methionine synthase]-methylcob(I)alamin + S-adenosylhomocysteine + NADP+
[methionine synthase]-cob(II)alamin + NADPH + S-adenosyl-L-methionine
-
Substrates: MSR is a NADPH-dependent diflavin oxidoreductase required for the reductive regeneration of catalytically inert cob(II)alamin to cob(I)alamin, complex formation between the substrate's activation domain and MSR, and the substrate's activation domain and the isolated FMN-binding domain of MSR. Weshow that the MS activation domain interacts directly with the FMN-binding domain of MSR, overview
Products: -
r
additional information
?
-
Substrates: difference in the relative efficiency of the very common polymorphic variant of the enzyme, I22M, suggests a molecular mechanism underlying the risk associated wiith the M22 allele for mild hyperhomocysteinemia
Products: -
?
additional information
?
-
-
Substrates: difference in the relative efficiency of the very common polymorphic variant of the enzyme, I22M, suggests a molecular mechanism underlying the risk associated wiith the M22 allele for mild hyperhomocysteinemia
Products: -
?
additional information
?
-
-
Substrates: biological implications of an attenuated mechanism of MS reactivation by MSR on methionine and folate metabolism, overview
Products: -
?
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FAD
-
-
FAD
-
contains both FAD and FMN. The values of the midpoint potentials are -236 mV FAD oxidized/semiquinone and -264 mV FAD semiquinone/hydroquinone, variant M22/S175
FAD
-
contains both FAD and FMN. The values of the midpoint potentials are -252 mV FAD oxidized/semiquinone and -285 mV FAD semiquinone/hydroquinone, variant I22/L175
FAD
-
dual flavoprotein with an equimolar concentration of FAD, 0.9 mol per mol of enzyme, and FMN, 1.1 mol per mol of enzyme
FAD
-
midpoint reduction potential
FAD
-
MSR contains one FAD and one FMN cofactor per polypeptide and functions in the sequential transfer of reducing equivalents from NADPH to MS via its flavin centers
FAD
the enzyme is a diflavin oxidoreductase, binding structure, overview
FAD
a dual-flavin reductase
FAD
the C-terminal domain of MTRR binds FAD
FAD
the proximal FAD histidine residue accelerates proton-coupled electron transfer from FADH2 to the higher potential FMN
FMN
-
FMN
-
contains both FAD and FMN. The values of the midpoint potentials are -103 mV FMN oxidized/semiquinone and -175 mV FMN semiquinone/hydroquinone, variant I22/L175
FMN
-
contains both FAD and FMN. The values of the midpoint potentials are -114 mV FMN oxidized/semiquinone and -212 mV FMN semiquinone/hydroquinone, variant M22/S175
FMN
-
dual flavoprotein with an equimolar concentration of FAD, 0.9 mol per mol of enzyme, and FMN, 1.1 mol per mol of enzyme
FMN
-
midpoint reduction potential
FMN
-
MSR contains one FAD and one FMN cofactor per polypeptide and functions in the sequential transfer of reducing equivalents from NADPH to MS via its flavin centers
FMN
the enzyme is a diflavin oxidoreductase, binding structure, overview
FMN
a dual-flavin reductase
FMN
the N-terminal domain of MTRR binds flavin mononucleotide
FMN
the proximal FAD histidine residue accelerates proton-coupled electron transfer from FADH2 to the higher potential FMN
NADH
-
under anaerobic growth conditions, oxidized ferredoxin (flavodoxin):NADP+ oxidoreductase accepts a hydride from NADPH and transfers the electron to flavodoxin, generating primarily flavodoxin semiquinone. Under anaerobic conditions the decarboxylation of pyruvate is coupled to reduction of flavodoxin, forming the flavodoxin hydroquinone. These reduced forms of flavodoxin bind to inactive cob(II)alamin enzyme, leading to a conformational change that is coupled with dissociation of His759 and protonation of the His759-Asp757-Ser810 triad. Although NADPH oxidation ultimately produces 2 equivalent of flavodoxin semiquinone, only one electron is transferred to methionine synthase during reductive methylation
NADH
-
can replace NADPH but only at significantly higher and nonphysiological concentrations
NADP+
-
-
NADP+
binding structure, overview
NADP+
-
dependent on, binding structure, overview, the NADP+-bound FNR-like module of MSR spans the NADP(H)-binding domain, the FAD-binding domain, the connecting domain, and part of the extended hinge region
NADPH
-
-
NADPH
-
preferred electron donor
NADPH
-
dependent on, binding structure, overview, the NADP+-bound FNR-like module of MSR spans the NADP(H)-binding domain, the FAD-binding domain, the connecting domain, and part of the extended hinge region
additional information
-
NAD(H) is a poor cofactor
-
additional information
a riboflavin-dependent enzyme
-
additional information
mechanism of NADPH reduction of a diflavin enzyme, overview
-
additional information
-
mechanism of NADPH reduction of a diflavin enzyme, overview
-
additional information
structure-based analysis of the cofactor domain interfaces, overview
-
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0.0023 - 0.0038
2,6-dichlorophenolindophenol
0.0177 - 0.018
3-acetylpyridine adenine dinucleotide phosphate
0.0286 - 0.0366
doxorubicin
0.663 - 0.774
ferricyanide
additional information
additional information
-
0.0023
2,6-dichlorophenolindophenol
variant I22/S175
0.0038
2,6-dichlorophenolindophenol
variant I22/S175
0.0177
3-acetylpyridine adenine dinucleotide phosphate
variant I22/S175
0.018
3-acetylpyridine adenine dinucleotide phosphate
variant I22/S175
0.0286
doxorubicin
variant I22/S175
0.0366
doxorubicin
variant I22/S175
0.663
ferricyanide
variant I22/S175
0.774
ferricyanide
variant I22/S175
0.0177
menadione
variant I22/S175
0.018
menadione
variant I22/S175
0.0024
NADPH
pH 7.5, 25°C, recombinant wild-type enzyme
0.00289
NADPH
-
pH 7.5, 25°C
0.0062
NADPH
pH 7.5, 25°C, recombinant mutant A312Q
0.015
NADPH
pH 7.5, 25°C, recombinant mutant A312H
additional information
additional information
-
isothermal titration calorimetry reveals a binding constant of 0.037 and 0.002 mM for binding of NADP+ and 2',5'-ADP, respectively, for the ligand-protein complex formed with full-length MSR or the isolated FNR module
-
additional information
additional information
-
lack of control on the thermodynamics and kinetics of electron transfer in MSR, overview
-
additional information
additional information
steady-state kinetics analysis of wild-type and mutant enzymes with cytochrome c3+ and NADPH as substrates, overview
-
additional information
additional information
-
steady-state kinetics analysis of wild-type and mutant enzymes with cytochrome c3+ and NADPH as substrates, overview
-
additional information
additional information
steady-state kinetics analysis of wild-type and mutant enzymes with cytochrome c3+ and NADPH as substrates, overview
-
additional information
additional information
stopped-flow and steady-state kinetic analysis
-
additional information
additional information
-
stopped-flow and steady-state kinetic analysis
-
additional information
additional information
stopped-flow spectroscopy, single turnover methods and a kinetic model relating electron flux through the enzyme to its conformational setpoint and its rates of conformational switching, kinetic model for electron flux through a dual-flavin enzyme, overview
-
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A312H
site-directed mutangenesis, mutation of the catalytic residue leads to the kinetic coupling of hydride and interflavin electron transfer, and eliminates the formation of the FAD hydroquinone intermediate, substitution of Ala312 for His in MSR weakens NADP(H) binding as the Km for NADPH and Ki for NADP+ increases 6 and 1.7fold, respectively. NADPH reduction of A312H resembles that of native cytochrome P450 reductase, in that it occurs in two discrete kinetic phases, without the transient formation of the E-FADH2-FMN intermediate
A312Q
site-directed mutangenesis, the catalytic site mutant shows a 2.5fold increased Km and a slightly decreased Ki for the coenzyme FAD
A66G
-
naturally occuring mutation, the MTRR polymorphism leads to a lower affinity for substrate methionine synthase compared to the wild-type enzyme
I22M
-
natural occuring polymorphism, no significant association with bone mineral density or serum osteocalcin level
S175L
-
natural occuring polymorphism, no significant association with bone mineral density or serum osteocalcin level
S698A
site-directed mutagenesis, the mutant shows reduced activity with cytochrome c3+ as substrate compared to the wild-type enzyme, the S698A mutant displays a 6fold reduction in kcat/Km for NADPH
W697F
site-directed mutagenesis, the mutant shows enhanced catalysis, noted by increases in kcat and kcat/Km(NADPH) for steady-state cytochrome c3+ reduction and a 10fold increase in the rate constant associated with hydride transfer, W697F shows a 2.4fold increase in kcat and a 4.8fold increase in catalytic efficiency for NADPH. The mutant displays modest decreases in cytochrome c3+ reduction, a 30fold decrease in the rate of FAD reduction, accumulation of a FADH2-NADP+ charge-transfer complex, and dramatically suppressed rates of interflavin electron transfer
W697H
site-directed mutagenesis, the mutant shows increased activity with cytochrome c3+ as substrate compared to the wild-type enzyme
W697S
site-directed mutagenesis, the mutant shows reduced activity with cytochrome c3+ as substrate compared to the wild-type enzyme
W697Y
site-directed mutagenesis, the mutant shows enhanced catalysis, noted by increases in kcat and kcat/Km(NADPH) for steady-state cytochrome c3+ reduction and a 10fold increase in the rate constant associated with hydride transfer. W697Y shows a 3.4fold increase in kcat and a 6.7fold increase in catalytic efficiency for NADPH. The mutant displays modest decreases in cytochrome c3+ reduction, a 3.5fold decrease in the rate of FAD reduction, accumulation of a FADH2-NADP+ charge-transfer complex, and dramatically suppressed rates of interflavin electron transfer
additional information
generation of truncation mutant S698DELTA, which shows increased activity with cytochrome c3+ as substrate compared to the wild-type enzyme
additional information
-
generation of truncation mutant S698DELTA, which shows increased activity with cytochrome c3+ as substrate compared to the wild-type enzyme
additional information
common naturally occuring polymorphisms are MTRR 66A>G or MTRR 524C>T, which affect the enzyme activity. Effects of the MTRR genotype on human status with respect to vitmain B6, plasma folate, homocysteine, and plasma cobalamine levels, modeling, detailed overview
additional information
-
construction of mouse model with a gene trap in the methionine synthase reductase gene. Mutant animals have increased plasma homocyst(e)ine, decreased plasma methionine, and increased tissue methyltetrahydrofolate levels. Mice do not show decreases in the S-adenosylmethionine/S-adenosylhomocysteine ratio in most tissues
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Leclerc, D.; Wilson, A.; Dumas, R.; Gafuik, C.; Song, D.; Watkins, D.; Heng, H.H.Q.; Rommens, J.M.; Scherer, S.W.; Rosenblatt, D.S.; Gravel, R.A.
Cloning and mapping of a cDNA for methionine synthase reductase, a flavoprotein defective in patients with homocystinuria
Proc. Natl. Acad. Sci. USA
95
3059-3064
1998
Homo sapiens (Q9UBK8), Homo sapiens
brenda
Jarrett, J.T.; Hoover, D.M.; Ludwig, M.L.; Matthews, R.G.
The mechanism of adenosylmethionine-dependent activation of methionine synthase: a rapid kinetic analysis of intermediates in reductive methylation of cob(II)alamin enzyme
Biochemistry
37
12649-12658
1998
Escherichia coli
brenda
Olteanu, H.; Munson, T.; Banerjee, R.
Differences in the efficiency of reductive activation of methionine synthase and exogenous electron acceptors between the common polymorphic variants of human methionine synthase reductase
Biochemistry
41
13378-13385
2002
Homo sapiens (Q9UBK8), Homo sapiens
brenda
Olteanu, H.; Wolthers, K.R.; Munro, A.W.; Scrutton, N.S.; Banerjee, R.
Kinetic and thermodynamic characterization of the common polymorphic variants of human methionine synthase reductase
Biochemistry
43
1988-1997
2004
Homo sapiens
brenda
Olteanu, H.; Banerjee, R.
Human methionine synthase reductase, a soluble P-450 reductase-like dual flavoprotein, is sufficient for NADPH-dependent methionine synthase activation
J. Biol. Chem.
276
35558-35563
2001
Homo sapiens
brenda
Wilson, A.; Platt, R.; Wu, Q.; Leclerc, D.; Christensen, B.; Yang, H.; Gravel, R.A.; Rozen, R.
A common variant in methionine synthase reductase combined with low cobalamin (vitamin B12) increases risk for spina bifida
Mol. Genet. Metab.
67
317-323
1999
Homo sapiens
brenda
Kim, D.J.; Park, B.L.; Koh, J.M.; Kim, G.S.; Kim, L.H.; Cheong, H.S.; Shin, H.D.; Hong, J.M.; Kim, T.H.; Shin, H.I.; Park, E.K.; Kim, S.Y.
Methionine synthase reductase polymorphisms are associated with serum osteocalcin levels in postmenopausal women
Exp. Mol. Med.
38
519-524
2006
Homo sapiens
brenda
Elmore, C.L.; Wu, X.; Leclerc, D.; Watson, E.D.; Bottiglieri, T.; Krupenko, N.I.; Krupenko, S.A.; Cross, J.C.; Rozen, R.; Gravel, R.A.; Matthews, R.G.
Metabolic derangement of methionine and folate metabolism in mice deficient in methionine synthase reductase
Mol. Genet. Metab.
91
85-97
2007
Mus musculus
brenda
Yamada, K.; Gravel, R.A.; Toraya, T.; Matthews, R.G.
Human methionine synthase reductase is a molecular chaperone for human methionine synthase
Proc. Natl. Acad. Sci. USA
103
9476-9481
2006
Homo sapiens
brenda
Wolthers, K.R.; Lou, X.; Toogood, H.S.; Leys, D.; Scrutton, N.S.
Mechanism of coenzyme binding to human methionine synthase reductase revealed through the crystal structure of the FNR-like module and isothermal titration calorimetry
Biochemistry
46
11833-11844
2007
Homo sapiens
brenda
Wolthers, K.R.; Scrutton, N.S.
Protein interactions in the human methionine synthase-methionine synthase reductase complex and implications for the mechanism of enzyme reactivation
Biochemistry
46
6696-6709
2007
Homo sapiens
brenda
Rigby, S.; Lou, X.; Toogood, H.; Wolthers, K.; Scrutton, N.
ELDOR spectroscopy reveals that energy landscapes in human methionine synthase reductase are extensively remodelled following ligand and partner protein binding
ChemBioChem
12
863-867
2011
Homo sapiens
brenda
Han, D.; Shen, C.; Meng, X.; Bai, J.; Chen, F.; Yu, Y.; Jin, Y.; Fu, S.
Methionine synthase reductase A66G polymorphism contributes to tumor susceptibility: evidence from 35 case-control studies
Mol. Biol. Rep.
39
805-816
2012
Homo sapiens
brenda
Meints, C.E.; Gustafsson, F.S.; Scrutton, N.S.; Wolthers, K.R.
Tryptophan 697 modulates hydride and interflavin electron transfer in human methionine synthase reductase
Biochemistry
50
11131-11142
2011
Homo sapiens (Q9UBK8), Homo sapiens
brenda
Zhao, J.; Yang, X.; Gong, X.; Gu, Z.; Duan, W.; Wang, J.; Ye, Z.; Shen, H.; Shi, K.; Hou, J.; Huang, G.; Jin, L.; Qiao, B.; Wang, H.
A functional variant in MTRR intron-1 significantly increases the risk of congenital heart disease in han Chinese population
Circulation
125
482-490
2012
Homo sapiens
brenda
Meints, C.E.; Simtchouk, S.; Wolthers, K.R.
Aromatic substitution of the FAD-shielding tryptophan reveals its differential role in regulating electron flux in methionine synthase reductase and cytochrome P450 reductase
FEBS J.
280
1460-1474
2013
Homo sapiens (Q9UBK8)
brenda
Meints, C.E.; Parke, S.M.; Wolthers, K.R.
Proximal FAD histidine residue influences interflavin electron transfer in cytochrome P450 reductase and methionine synthase reductase
Arch. Biochem. Biophys.
547
18-26
2014
Homo sapiens (Q9UBK8), Homo sapiens
brenda
Haque, M.M.; Bayachou, M.; Tejero, J.; Kenney, C.T.; Pearl, N.M.; Im, S.C.; Waskell, L.; Stuehr, D.J.
Distinct conformational behaviors of four mammalian dual-flavin reductases (cytochrome P450 reductase, methionine synthase reductase, neuronal nitric oxide synthase, endothelial nitric oxide synthase) determine their unique catalytic profiles
FEBS J.
281
5325-5340
2014
Homo sapiens (Q9UBK8)
brenda
Garcia-Minguillan, C.J.; Fernandez-Ballart, J.D.; Ceruelo, S.; Rios, L.; Bueno, O.; Berrocal-Zaragoza, M.I.; Molloy, A.M.; Ueland, P.M.; Meyer, K.; Murphy, M.M.
Riboflavin status modifies the effects of methylenetetrahydrofolate reductase (MTHFR) and methionine synthase reductase (MTRR) polymorphisms on homocysteine
Genes Nutr.
9
435
2014
Homo sapiens (Q9UBK8)
brenda
Cheng, H.; Li, H.; Bu, Z.; Zhang, Q.; Bai, B.; Zhao, H.; Li, R.K.; Zhang, T.; Xie, J.
Functional variant in methionine synthase reductase intron-1 is associated with pleiotropic congenital malformations
Mol. Cell. Biochem.
407
51-56
2015
Homo sapiens (Q9UBK8)
brenda