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Literature summary for 1.16.1.8 extracted from

  • 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 (2007), Biochemistry, 46, 6696-6709.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expression of full-length enzyme and flavin-binding domain as GST-tagged proteins Homo sapiens

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information lack of control on the thermodynamics and kinetics of electron transfer in MSR, overview Homo sapiens

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
[methionine synthase]-methylcob(I)alamin + S-adenosylhomocysteine + NADP+ Homo sapiens 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 [methionine synthase]-cob(II)alamin + NADPH + S-adenosyl-L-methionine
-
r

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant GST-tagged full-length enzyme and flavin-binding domain by glutathione affinity and anion exchange chromatography, followed by ultrafiltration Homo sapiens

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
[methionine synthase]-methylcob(I)alamin + S-adenosylhomocysteine + NADP+ 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 Homo sapiens [methionine synthase]-cob(II)alamin + NADPH + S-adenosyl-L-methionine
-
r
[methionine synthase]-methylcob(I)alamin + S-adenosylhomocysteine + NADP+ 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 Homo sapiens [methionine synthase]-cob(II)alamin + NADPH + S-adenosyl-L-methionine
-
r

Synonyms

Synonyms Comment Organism
Methionine synthase reductase
-
Homo sapiens
MSR
-
Homo sapiens
NADPH-dependent diflavin oxidoreductase
-
Homo sapiens

Temperature Optimum [°C]

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

pH Optimum

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

Cofactor

Cofactor Comment Organism Structure
FAD midpoint reduction potential Homo sapiens
FMN midpoint reduction potential Homo sapiens
NADP+
-
Homo sapiens
NADPH
-
Homo sapiens