EC Number   |
Cofactor |
Reference |
|---|
    2.1.1.13 | ATP |
required |
441172 |
| 2.1.1.13 | Cobalamin |
cobalamin serves as an intermediary in methyl transfer reactions, and it cycles between the methylcob(III)alamin and cob(I)alamin forms |
703638 |
| 2.1.1.13 | Cobalamin |
preparation of a synthetic conjugate between apomyoglobin and cobalt tetradehydrocorrin to replicate the coordination behavior of cob(I)alamin in methionine synthase. The tetracoordinated Co(I) species is formed through the cleavage of the axial Co-His93 ligation after the reduction of the penta-coordinated Co(II) cofactor in the heme pocket |
733648 |
| 2.1.1.13 | cobinamide |
more active than cyanocobalamin with rat liver enzyme, but inhibitory with E. coli enzyme |
441196 |
| 2.1.1.13 | FAD |
enzyme requires reduced FAD and S-adenosyl-L-methionine |
441173 |
| 2.1.1.13 | more |
absolute requirement for a reducing system |
441180, 441182, 441183, 441189 |
| 2.1.1.13 | more |
enzyme requires another protein fraction, ATP, Mg2+, FAD and a NADH-generating system |
441172, 441174 |
| 2.1.1.13 | S-adenosyl-L-methionine |
- |
441191 |
| 2.1.1.13 | S-adenosyl-L-methionine |
bacterial enzyme requires reduced FAD and S-adenosyl-L-methionine |
441173 |
| 2.1.1.13 | S-adenosyl-L-methionine |
partially stimulates |
441180 |
