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Literature summary for 1.16.1.8 extracted from

  • 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 (1998), Biochemistry, 37, 12649-12658.
    View publication on PubMed
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Activating Compound

Activating Compound Comment Organism Structure
reduced flavodoxin under anaerobic growth conditions, oxidized ferredoxin (flavodoxin):NADP+ oxidoreductase accepts a hydride from NADPH and transfers the electron to flavodoxin, generating primarily flavodoxin semiquinone. Under anaerobic conditions the decarboxylation of pyruvate is coupled to reduction of flavodoxin, forming the flavodoxin hydroquinone. These reduced forms of flavodoxin bind to inactive cob(II)alamin enzyme, leading to a conformational change that is coupled with dissociation of His759 and protonation of the His759-Asp757-Ser810 triad. Although NADPH oxidation ultimately produces 2 equivalent of flavodoxin semiquinone, only one electron is transferred to methionine synthase during reductive methylation Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
[Methionine synthase]-cob(II)alamin + NADPH + S-adenosyl-L-methionine Escherichia coli the enzyme is involved in reductive activation of methionine synthase: ?
-
 ?

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Reaction

Reaction Comment Organism Reaction ID
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 under anaerobic growth conditions, oxidized ferredoxin (flavodoxin):NADP+ oxidoreductase accepts a hydride from NADPH and transfers the electron to flavodoxin, generating primarily flavodoxin semiquinone. Under anaerobic conditions the decarboxylation of pyruvate is coupled to reduction of flavodoxin, forming the flavodoxin hydroquinone. These reduced forms of flavodoxin bind to inactive cob(II)alamin enzyme, causing a conformational change that is coupled with dissociation of His759 and protonation of the His759-Asp757-Ser810 triad. Although NADPH oxidation ultimately produces 2 equivalent of flavodoxin semiquinone, only one electron is transferred to methionine synthase during reductive methylation Escherichia coli
a

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
[Methionine synthase]-cob(II)alamin + NADPH + S-adenosyl-L-methionine the enzyme is involved in reductive activation of methionine synthase: Escherichia coli ?
-
 ?

Cofactor

Cofactor Comment Organism Structure
NADH under anaerobic growth conditions, oxidized ferredoxin (flavodoxin):NADP+ oxidoreductase accepts a hydride from NADPH and transfers the electron to flavodoxin, generating primarily flavodoxin semiquinone. Under anaerobic conditions the decarboxylation of pyruvate is coupled to reduction of flavodoxin, forming the flavodoxin hydroquinone. These reduced forms of flavodoxin bind to inactive cob(II)alamin enzyme, leading to a conformational change that is coupled with dissociation of His759 and protonation of the His759-Asp757-Ser810 triad. Although NADPH oxidation ultimately produces 2 equivalent of flavodoxin semiquinone, only one electron is transferred to methionine synthase during reductive methylation Escherichia coli