EC Number   |
Cofactor |
Reference  |
|---|
    1.3.98.3 | 4Fe-4S-center |
HemN binds a 4Fe-4S cluster through three cysteine residues: Cys-62, Cys-66 and Cys-69, a juxtaposed S-adenosyl-L-methionine coordinates the fourth Fe ion through its amide nitrogen and carboxylate oxygen, detailed binding mode, cofactor geometry required for Radical SAM catalysis |
655340 |
| 1.3.98.3 | S-adenosyl-L-methionine |
HemN contains two S-adenosyl-L-methionine molecules as cofactors, detailed binding mode |
655340 |
| 1.3.98.3 | 4Fe-4S-center |
requirement, oxygen-sensitive Fe-S cluster, Cys-62, Cys-66 and Cys-69 are part of the conserved CXXXCXXC motif and essential for Fe-S cluster formation and enzyme function, Tyr-56 and His-58 are important for the Fe-S cluster integrity, His-58 may provide the fourth ligand besides the three cysteine residues |
656073 |
| 1.3.98.3 | NADH |
requires NAD(P)H, higher activity than with NADPH as cofactor |
656073 |
| 1.3.98.3 | NADPH |
requires NAD(P)H, lower activity than with NADH as cofactor |
656073 |
| 1.3.98.3 | S-adenosyl-L-methionine |
uses S-adenosyl-L-methionine as a cofactor |
656073 |
| 1.3.98.3 | 4Fe-4S-center |
structure, location and coordination of the cofactor, HemN requires the juxtaposition of the [4Fe-4S] cluster and the cosubstrate S-adenosyl-L-methionine |
658501 |
| 1.3.98.3 | NADH |
- |
672473 |
| 1.3.98.3 | S-adenosyl-L-methionine |
HemN binds two SAM molecules |
672473 |
| 1.3.98.3 | S-adenosyl-L-methionine |
cosubstrate of coproporphyrinogen-III |
674462 |
