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Information on EC 1.16.1.8 - [methionine synthase] reductase
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EC Tree
1.16.1.8 [methionine synthase] reductaseIUBMB Comments
In humans, the enzyme is a flavoprotein containing FAD and FMN. The substrate of the enzyme is the inactivated cobalt(II) form of EC 2.1.1.13, methionine synthase. Electrons are transferred from NADPH to FAD to FMN. Defects in this enzyme lead to hereditary hyperhomocysteinemia.
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Word Map
- 1.16.1.8
- mthfr
- folate
- methylenetetrahydrofolate
-
case-control
- gg
- hyperhomocysteinemia
-
one-carbon
- cystathionine
- tetrahydrofolate
-
folic
-
remethylation
- thymidylate
- beta-synthase
-
transcobalamin
-
methylmalonic
-
megaloblastic
-
folate-related
-
spina
- bifida
-
cobiialamin
- methyltetrahydrofolate
-
cobalamin-dependent
- homocystinuria
- gcpii
- diagnostics
-
t-hcys
- medicine
-
folate-metabolizing
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Reaction Schemes
2
+
2
+
=
2
+
+
+
2
2
[methionine synthase]-methylcob(III)alamin
+
2
+
=
2
+
+
+
2
Synonyms
methionine synthase reductase, nadph-dependent diflavin oxidoreductase, 
more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
EC 2.1.1.135
-
-
formerly
-
Methionine synthase cob(II)alamin reductase (methylating)
-
-
-
-
Methionine synthase reductase
MSR
MTRR
Reductase, methionine synthase
-
-
-
-
Methionine synthase reductase
-
-
-
-
MSR
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
2 [methionine synthase]-methylcob(III)alamin + 2 S-adenosyl-L-homocysteine + NADP+ = 2 [methionine synthase]-cob(II)alamin + NADPH + H+ + 2 S-adenosyl-L-methionine
2 [methionine synthase]-methylcob(III)alamin + 2 S-adenosyl-L-homocysteine + NADP+ = 2 [methionine synthase]-cob(II)alamin + NADPH + H+ + 2 S-adenosyl-L-methionine
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, causing 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
-
2 [methionine synthase]-methylcob(III)alamin + 2 S-adenosyl-L-homocysteine + NADP+ = 2 [methionine synthase]-cob(II)alamin + NADPH + H+ + 2 S-adenosyl-L-methionine
mechanism for the NADPH-catalyzed reduction of diflavin oxidoreductases, overview
2 [methionine synthase]-methylcob(III)alamin + 2 S-adenosyl-L-homocysteine + NADP+ = 2 [methionine synthase]-cob(II)alamin + NADPH + H+ + 2 S-adenosyl-L-methionine
hydride transfer and interflavin electron transfer are two catalytic steps represented by two distinct kinetic phases leading to transient formation of the FAD hydroquinone
2 [methionine synthase]-methylcob(III)alamin + 2 S-adenosyl-L-homocysteine + NADP+ = 2 [methionine synthase]-cob(II)alamin + NADPH + H+ + 2 S-adenosyl-L-methionine
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-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
methyl group transfer
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
-
-
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SYSTEMATIC NAME
IUBMB Comments
[methionine synthase]-methylcob(III)alamin,S-adenosyl-L-homocysteine:NADP+ oxidoreductase
In humans, the enzyme is a flavoprotein containing FAD and FMN. The substrate of the enzyme is the inactivated cobalt(II) form of EC 2.1.1.13, methionine synthase. Electrons are transferred from NADPH to FAD to FMN. Defects in this enzyme lead to hereditary hyperhomocysteinemia.
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CAS REGISTRY NUMBER
COMMENTARY
207004-87-3
-
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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
2 [methionine synthase]-cob(II)alamin + NADPH + H+ + 2 S-adenosyl-L-methionine
2 [methionine synthase]-methylcob(I)alamin + 2 S-adenosylhomocysteine + NADP+
-
-
-
?
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+
-
-
-
-
?
[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
-
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
-
-
?
[methionine synthase]-cob(II)alamin + S-adenosyl-L-methionine + 2,6-dichlorophenolindophenol
[methionine synthase]methylcob(I)alamin + S-adenosylhomocysteine + ?
-
-
-
?
[methionine synthase]-cob(II)alamin + S-adenosyl-L-methionine + 3-acetylpyridine adenine dinucleotide phosphate
[methionine synthase]methylcob(I)alamin + S-adenosylhomocysteine + ?
-
-
-
?
[methionine synthase]-cob(II)alamin + S-adenosyl-L-methionine + doxorubicin
[methionine synthase]methylcob(I)alamin + S-adenosylhomocysteine + ?
-
-
-
?
[methionine synthase]-cob(II)alamin + S-adenosyl-L-methionine + ferricyanide
[methionine synthase]methylcob(I)alamin + S-adenosylhomocysteine + ?
-
-
-
?
[methionine synthase]-cob(II)alamin + S-adenosyl-L-methionine + menadione
[methionine synthase]methylcob(I)alamin + S-adenosylhomocysteine + ?
-
-
-
?
[methionine synthase]-methylcob(I)alamin + S-adenosylhomocysteine + NADP+
[methionine synthase]-cob(II)alamin + NADPH + S-adenosyl-L-methionine
2 [methionine synthase]-methylcob(I)alamin + 2 S-adenosylhomocysteine + NADP+
2 [methionine synthase]-cob(II)alamin + NADPH + H+ + 2 S-adenosyl-L-methionine
-
-
-
?
2 [methionine synthase]-methylcob(I)alamin + 2 S-adenosylhomocysteine + NADP+
2 [methionine synthase]-cob(II)alamin + NADPH + H+ + 2 S-adenosyl-L-methionine
the enzyme catalyzes the oxidation of NADPH and shuttles electrons via its FAD and FMN cofactors to inactive MScob(II)alamin
-
-
?
2 [methionine synthase]-methylcob(I)alamin + 2 S-adenosylhomocysteine + NADP+
2 [methionine synthase]-cob(II)alamin + NADPH + H+ + 2 S-adenosyl-L-methionine
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
-
-
?
[Methionine synthase]-cob(II)alamin + NADPH + S-adenosyl-L-methionine
?
-
the enzyme is involved in reductive activation of methionine synthase:
-
-
?
[Methionine synthase]-cob(II)alamin + NADPH + S-adenosyl-L-methionine
?
the enzyme is involved in reductive activation of methionine synthase:
-
-
?
[Methionine synthase]-cob(II)alamin + NADPH + S-adenosyl-L-methionine
?
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
-
-
?
[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
[Methionine synthase]methylcob(I)alamin + S-adenosylhomocysteine + NADP+
-
-
?
[methionine synthase]-methylcob(I)alamin + S-adenosylhomocysteine + NADP+
[methionine synthase]-cob(II)alamin + NADPH + S-adenosyl-L-methionine
-
-
-
-
r
[methionine synthase]-methylcob(I)alamin + S-adenosylhomocysteine + NADP+
[methionine synthase]-cob(II)alamin + NADPH + S-adenosyl-L-methionine
-
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
-
-
r
[methionine synthase]-methylcob(I)alamin + S-adenosylhomocysteine + NADP+
[methionine synthase]-cob(II)alamin + NADPH + S-adenosyl-L-methionine
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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
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-
r
[methionine synthase]-methylcob(I)alamin + S-adenosylhomocysteine + NADP+
[methionine synthase]-cob(II)alamin + NADPH + S-adenosyl-L-methionine
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MSR is a flavoprotein that regenerates the active form of cobalamin-dependent methionine synthase
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-
r
additional information
?
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
biological implications of an attenuated mechanism of MS reactivation by MSR on methionine and folate metabolism, overview
-
-
?
additional information
?
-
-
the enzyme catalyzes also the inhibition of reduction of cytochrome c3+
-
-
?
additional information
?
-
the enzyme catalyzes the reduction of cytochrome c3+ with NADPH and NADH
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-
?
additional information
?
-
-
the enzyme catalyzes the reduction of cytochrome c3+ with NADPH and NADH
-
-
?
additional information
?
-
the enzyme catalyzes the reduction of cytochrome c3+ with NADPH and NADH
-
-
?
additional information
?
-
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
-
-
?
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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
2 [methionine synthase]-cob(II)alamin + NADPH + H+ + 2 S-adenosyl-L-methionine
2 [methionine synthase]-methylcob(I)alamin + 2 S-adenosylhomocysteine + NADP+
-
-
-
?
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]-methylcob(I)alamin + S-adenosylhomocysteine + NADP+
[methionine synthase]-cob(II)alamin + NADPH + S-adenosyl-L-methionine
[Methionine synthase]-cob(II)alamin + NADPH + S-adenosyl-L-methionine
?
-
the enzyme is involved in reductive activation of methionine synthase:
-
-
?
[Methionine synthase]-cob(II)alamin + NADPH + S-adenosyl-L-methionine
?
the enzyme is involved in reductive activation of methionine synthase:
-
-
?
[Methionine synthase]-cob(II)alamin + NADPH + S-adenosyl-L-methionine
?
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
-
-
?
[methionine synthase]-methylcob(I)alamin + S-adenosylhomocysteine + NADP+
[methionine synthase]-cob(II)alamin + NADPH + S-adenosyl-L-methionine
-
-
-
-
r
[methionine synthase]-methylcob(I)alamin + S-adenosylhomocysteine + NADP+
[methionine synthase]-cob(II)alamin + NADPH + S-adenosyl-L-methionine
-
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
-
-
r
additional information
?
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
biological implications of an attenuated mechanism of MS reactivation by MSR on methionine and folate metabolism, overview
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
-
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 proximal FAD histidine residue accelerates proton-coupled electron transfer from FADH2 to the higher potential 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
-
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 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+
-
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
-
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
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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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
NADP+
competitive inhibition in the reaction with NADPH and cytochrome c3+ as substrates, overview
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
reduced flavodoxin
-
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
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
steady-state inhibition studies
-
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.5
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
postmenopausal women, certain genetic polymorphisms of enzyme leading to a reduced activity may cause hyperhomocysteinemia and affect bone metabolism
-
-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
in vivo quantitative real-time PCR analysis of MTRR mRNA in cardiac tissue samples from congenital heart disease patients, overview
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
metabolism
physiological function
additional information
malfunction
-
the c.56+781 A>C (rs326119) variant of intron-1 of MTRR significantly increases the risk of congenital heart disease in the Han Chinese population and is highly related to septation defects. The c.56+781 C allele profoundly decreases MTRR transcription. Phenotype, overview
malfunction
analysis of correlations of single nucleotide polymorphisms and various malformation anomalies, overview
metabolism
-
the MTRR gene is involved in tumorigenesis by regulating DNA methylation through activation of methionine synthase
physiological function
-
methionine synthase reductase is essential for the adequate remethylation of homocysteine, which is the dominant pathway for homocysteine removal during early embryonic development
physiological function
methionine synthase reductase, a diflavin oxidoreductase, plays a vital role in methionine and folate metabolism by sustaining methionine synthase activity
physiological function
roles of methionine synthase, MS, and methylenetetrahydrofolate reductase, MTHFR, and methionine synthase reductase, MTRR, in the folate cycle and homocysteine remethylation, overview
additional information
-
genotyping for the A66G polymorphism and analysis of the association with cancer risk reveals that the G allele and GG variant genotypes are associated with a significantly increased cancer risk
additional information
effects of the MTRR genotype on human status with respect to vitmain B6, plasma folate, homocysteine, and plasma cobalamine levels, modeling, detailed overview
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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). MTRR_BOVIN
695
0
77163
Swiss-Prot
Mitochondrion (Reliability: 5)
MTRR_CAEEL
682
0
76834
Swiss-Prot
other Location (Reliability: 2)
MTRR_HUMAN
698
0
77674
Swiss-Prot
other Location (Reliability: 4)
MTRR_MOUSE
696
0
77518
Swiss-Prot
Mitochondrion (Reliability: 5)
MTRR_RAT
700
0
78025
Swiss-Prot
Mitochondrion (Reliability: 4)
Q9VEV2_DROME
454
0
51288
TrEMBL
other Location (Reliability: 1)
M2Y299_GALSU
515
0
59498
TrEMBL
other Location (Reliability: 2)
A8IS63_CHLRE
628
0
68197
TrEMBL
other Location (Reliability: 3)
A0A088S4N9_9TRYP
1891
0
206190
TrEMBL
other Location (Reliability: 1)
A0A0D2N4U9_9CHLO
1561
0
161589
TrEMBL
Mitochondrion (Reliability: 4)
A0A1S7UL41_ROSNE
618
0
68935
TrEMBL
other Location (Reliability: 4)