EC Number   |
Natural Substrates |
|---|
   1.16.1.8 | 2 [methionine synthase]-cob(II)alamin + NADPH + H+ + 2 S-adenosyl-L-methionine |
- |
| 1.16.1.8 | 2 [methionine synthase]-methylcob(I)alamin + 2 S-adenosylhomocysteine + NADP+ |
- |
| 1.16.1.8 | more |
difference in the relative efficiency of the very common polymorphic variant of the enzyme, I22M, suggests a molecular mechanism underlying the risk associated wiith the M22 allele for mild hyperhomocysteinemia |
| 1.16.1.8 | more |
biological implications of an attenuated mechanism of MS reactivation by MSR on methionine and folate metabolism, overview |
| 1.16.1.8 | [Methionine synthase]-cob(II)alamin + NADPH + S-adenosyl-L-methionine |
the enzyme is involved in reductive activation of methionine synthase: |
| 1.16.1.8 | [Methionine synthase]-cob(II)alamin + NADPH + S-adenosyl-L-methionine |
patients of the cblE complementation group of disorders of folate/cobalamin metabolism who are defective in reductive activation of methionine synthase exhibit megablastic anemia, developmental delay, hyperhomocysteinemia, and hypomethioninemia |
| 1.16.1.8 | [methionine synthase]-methylcob(I)alamin + S-adenosylhomocysteine + NADP+ |
- |
| 1.16.1.8 | [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 |
