EC Number   |
Cofactor |
Reference |
|---|
  2.1.1.308 | Cobalamin |
- |
729108 |
| 2.1.1.308 | methylcobalamin |
a B12-derived cofactor. A conserved domain search of the Fom3 sequence shows that it has two conserved domains. The N-terminal domain is identified as a B12-like binding domain, whereas the C-terminal domain shows homology to the radical-SAM protein family, containing three conserved Cys residues that serve as ligands to a [4Fe-4S] cluster |
703183 |
| 2.1.1.308 | methylcobalamin |
proposed mechanism: a 5'-deoxyadenosine radical generated from reductive cleavage of S-adenosyl-L-methionine is used to abstract the hydrogen atom from the C-H bond of the substrate resulting in a substrate radical that reacts with methylcobalamin yielding (S)-2-hydroxypropylphosphonate and cob(II)alamin |
703345 |
| 2.1.1.308 | S-adenosyl-L-methionine |
a conserved domain search of the Fom3 sequence shows it has two conserved domains. The N-terminal domain is identified as a B12-like binding domain, whereas the C-terminal domain shows homology to the radical-SAM protein family, containing three conserved Cys residues that serve as ligands to a [4Fe-4S] cluster |
703183 |
| 2.1.1.308 | S-adenosyl-L-methionine |
proposed mechanism: a 5'-deoxyadenosine radical generated from reductive cleavage of S-adenosyl-L-methionine is used to abstract the hydrogen atom from the C-H bond of the substrate resulting in a substrate radical that reacts with methylcobalamin yielding (S)-2-hydroxypropylphosphonate and cob(II)alamin |
703345 |
