EC Number   |
Metals/Ions |
Reference |
|---|
    4.3.99.3 | Fe2+ |
the enzyme uses a bound [4Fe-4S]+ cluster to catalyze the reductive cleavage of S-adenosyl-L-methionine cofactor to generate methionine, a single [4Fe-4S] cluster per monomer |
729229 |
| 4.3.99.3 | Fe2+ |
the enzyme uses a bound [4Fe-4S]+ cluster to catalyze the reductive cleavage of S-adenosyl-L-methionine cofactor to generate methionine, a single [4Fe-4S] cluster per monomer. The cluster-binding motifs of each monomer are located at opposite ends of the dimer molecule, of the Fe atoms from the cluster are coordinated by three cysteine residues from the CX14CXPhiC motif. The remaining unique Fe binds the alpha-amino and alpha-carboxyl groups of S-adenosyl-L-methionine, which adopts an anti orientation about the glycosidic bond |
730439 |
| 4.3.99.3 | Mg2+ |
dependent on |
746578 |
| 4.3.99.3 | Mg2+ |
dependent on, Km is 0.21 mM |
729229 |
| 4.3.99.3 | Mg2+ |
dependent on, the ligand environment about Mg2+ is pseudo-octahedral, with three water ligands, the substrate C4 carbonyl and C6 carboxylate oxygens, and the hydroxyl of T51 |
730439 |
| 4.3.99.3 | Mg2+ |
Mg2+ provides key contacts with the substrate 6-carboxy-5,6,7,8-tetrahydropterin and the product 7-carboxy-7-carbaguanine, thus anchoring the molecules in the active site. The formation of either 6-carboxypterin product is not enhanced by the presence of Mg2+ |
748040 |
| 4.3.99.3 | Mg2+ |
the Mg2+ complexation not only brings the substrate into the reactive conformation but also, once a hydrogen atom is abstracted from the substrate, holds the resultant intermediate radical in a highly strained conformation |
747574 |
