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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KM Value
KM Value on EC 1.16.1.8 - [methionine synthase] reductase
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additional information
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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
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additional information
additional information
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lack of control on the thermodynamics and kinetics of electron transfer in MSR, overview
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additional information
additional information
steady-state kinetics analysis of wild-type and mutant enzymes with cytochrome c3+ and NADPH as substrates, overview
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additional information
additional information
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steady-state kinetics analysis of wild-type and mutant enzymes with cytochrome c3+ and NADPH as substrates, overview
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additional information
additional information
steady-state kinetics analysis of wild-type and mutant enzymes with cytochrome c3+ and NADPH as substrates, overview
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additional information
additional information
stopped-flow and steady-state kinetic analysis
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additional information
additional information
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stopped-flow and steady-state kinetic analysis
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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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