EC Number   |
Cofactor |
Reference |
|---|
    4.3.99.3 | 4Fe-4S-center |
- |
748568 |
| 4.3.99.3 | 4Fe-4S-center |
S-adenosyl-L-methionine binds to the unique iron atom of a site-differentiated [4Fe-4S] cluster and is reductively cleaved to generate a 5'-deoxyadenosyl radical, which initiates turnover |
748040 |
| 4.3.99.3 | 4Fe-4S-center |
the enzyme requires the one electron reduction of the [4Fe-4S]2+ cluster to the +1 oxidation state. This can be achieved by using a chemical reductant, such as dithionite, or a biological reducing system in which the reducing equivalents are derived from NADPH and transferred to the cluster via flavodoxin reductase and flavodoxin |
747084 |
| 4.3.99.3 | more |
to initiate radical chemistry, all AdoMet radical enzymes require the one-electron reduction of the [4Fe-4S] cluster. This electron is typically supplied by a flavodoxin. For the Burkholderia multivorans enzyme, more product is generated using the chemical reductant dithionite |
730439 |
| 4.3.99.3 | S-adenosyl-L-methionine |
dependent on. Members of the radical SAM superfamily contain a CX3CX2C-motif for binding a [4Fe-4S] cluster, which when reductively activated, cleaves SAM to 5?-deoxyadenosyl radical, which in turn initiates radical mediated transformations of the substrate |
717240 |
| 4.3.99.3 | S-adenosyl-L-methionine |
Km is 0.045 mM, the cofactor supports multiple turnovers, it is regenerated at the end of each catalytic cycle |
729229 |
| 4.3.99.3 | S-adenosyl-L-methionine |
S-adenosyl-L-methionine-dependent radical enzyme |
746578, 747084, 747574, 748040, 748568, 749244 |
| 4.3.99.3 | S-adenosyl-L-methionine |
the binding site is conserved despite modified enzyme fold |
730439 |
