1.16.1.8: [methionine synthase] reductase
This is an abbreviated version!
For detailed information about [methionine synthase] reductase, go to the full flat file.
Word Map on EC 1.16.1.8
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1.16.1.8
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mthfr
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folate
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methylenetetrahydrofolate
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case-control
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gg
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hyperhomocysteinemia
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one-carbon
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cystathionine
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tetrahydrofolate
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folic
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remethylation
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thymidylate
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beta-synthase
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transcobalamin
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methylmalonic
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megaloblastic
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folate-related
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spina
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bifida
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cobiialamin
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methyltetrahydrofolate
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cobalamin-dependent
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homocystinuria
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gcpii
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diagnostics
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t-hcys
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medicine
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folate-metabolizing
- 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
Reaction
2 [methionine synthase]-methylcob(III)alamin + 2 S-adenosyl-L-homocysteine + = 2 [methionine synthase]-cob(II)alamin + + + 2 S-adenosyl-L-methionine
Synonyms
EC 2.1.1.135, Methionine synthase cob(II)alamin reductase (methylating), Methionine synthase reductase, MSR, MTRR, NADPH-dependent diflavin oxidoreductase, Reductase, methionine synthase
ECTree
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Cofactor
Cofactor on EC 1.16.1.8 - [methionine synthase] reductase
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FAD
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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
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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
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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
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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
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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
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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
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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
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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
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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
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can replace NADPH but only at significantly higher and nonphysiological concentrations
NADP+
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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
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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
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additional information
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mechanism of NADPH reduction of a diflavin enzyme, overview
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additional information
structure-based analysis of the cofactor domain interfaces, overview
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