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 | 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 | UniProt | Comment | Textmining |
---|---|---|---|
Escherichia coli | - |
- |
- |
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 |
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 | 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 |