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Literature summary extracted from

  • 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 (2007), Biochemistry, 46, 11833-11844.
    View publication on PubMed

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.16.1.8 MSR NADP(H)/FAD domain complex, sitting drop vapor diffusion method, 4°C, 10 mg/ml protein in 10 mM Tris/HCl, pH 8.0, 0.5 mM DTT, 1 mM EDTA, and 0.05% NaN3, reservoir solution comprising 0.1 M Tris/HCl, pH 7.5, 0.2 M KBr, and 15% PEG 4000, crystal soaking in saturated NADP+ solution, X-ray diffraction structure determination and analysis at 1.9 A resolution Homo sapiens

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.16.1.8 2',5'-ADP inhibition of MSR-catalyzed reduction of cytochrome c3+ Homo sapiens
1.16.1.8 NADP+ inhibition of MSR-catalyzed reduction of cytochrome c3+ Homo sapiens

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.16.1.8 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 Homo sapiens
1.16.1.8 0.00289
-
 NADPH pH 7.5, 25°C Homo sapiens

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.16.1.8 78000
-
 x * 78000, SDS-PAGE Homo sapiens

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.16.1.8 additional information Homo sapiens biological implications of an attenuated mechanism of MS reactivation by MSR on methionine and folate metabolism, overview ?
-
 ?
1.16.1.8 [methionine synthase]-methylcob(I)alamin + S-adenosylhomocysteine + NADP+ Homo sapiens
-
 [methionine synthase]-cob(II)alamin + NADPH + S-adenosyl-L-methionine
-
 r

Organism

EC Number Organism UniProt Comment Textmining
1.16.1.8 Homo sapiens
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.16.1.8 additional information biological implications of an attenuated mechanism of MS reactivation by MSR on methionine and folate metabolism, overview Homo sapiens ?
-
 ?
1.16.1.8 additional information the enzyme catalyzes also the inhibition of reduction of cytochrome c3+ Homo sapiens ?
-
 ?
1.16.1.8 [methionine synthase]-methylcob(I)alamin + S-adenosylhomocysteine + NADP+
-
 Homo sapiens [methionine synthase]-cob(II)alamin + NADPH + S-adenosyl-L-methionine
-
 r
1.16.1.8 [methionine synthase]-methylcob(I)alamin + S-adenosylhomocysteine + NADP+ MSR is a flavoprotein that regenerates the active form of cobalamin-dependent methionine synthase Homo sapiens [methionine synthase]-cob(II)alamin + NADPH + S-adenosyl-L-methionine
-
 r

Subunits

EC Number Subunits Comment Organism
1.16.1.8 ? x * 78000, SDS-PAGE Homo sapiens
1.16.1.8 More 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 Homo sapiens

Synonyms

EC Number Synonyms Comment Organism
1.16.1.8 Methionine synthase reductase
-
 Homo sapiens
1.16.1.8 MSR
-
 Homo sapiens

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.16.1.8 25
-
 assay at Homo sapiens

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.16.1.8 3.92
-
 NADPH pH 7.5, 25°C Homo sapiens

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.16.1.8 7.5
-
 assay at Homo sapiens

Cofactor

EC Number Cofactor Comment Organism Structure
1.16.1.8 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 Homo sapiens
1.16.1.8 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 Homo sapiens
1.16.1.8 additional information NAD(H) is a poor cofactor Homo sapiens
1.16.1.8 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 Homo sapiens
1.16.1.8 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 Homo sapiens

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
1.16.1.8 additional information
-
 additional information steady-state inhibition studies Homo sapiens
1.16.1.8 0.0014
-
 2',5'-ADP inhibition of reduction of cytochrome c3+ Homo sapiens
1.16.1.8 0.036
-
 NADP+ inhibition of reduction of cytochrome c3+ Homo sapiens