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
+
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
1.16.1.8 [methionine synthase] reductaseAdvanced search results
results (
results (Substrates Products
Substrates Products on EC 1.16.1.8 - [methionine synthase] reductase
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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
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-
?
[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
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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
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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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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
-
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
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-
?
additional information
?
-
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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
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?
additional information
?
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biological implications of an attenuated mechanism of MS reactivation by MSR on methionine and folate metabolism, overview
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?
additional information
?
-
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the enzyme catalyzes also the inhibition of reduction of cytochrome c3+
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-
?
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
?
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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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-
?
