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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

Reaction

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

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 Oxidoreductases
         1.16 Oxidizing metal ions
             1.16.1 With NAD+ or NADP+ as acceptor
                1.16.1.8 [methionine synthase] reductase

Reference

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Reference on EC 1.16.1.8 - [methionine synthase] reductase

Please use the Reference Search for a specific query.
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team