EC Number   |
Cofactor |
Reference |
|---|
    1.1.98.6 | iron-sulfur centre |
activation of enzyme involves generation of a specific amino acid free radical that is dependent on a reduced Fe-S cluster and S-adenosylmethionine |
740653 |
| 1.1.98.6 | S-adenosyl-L-methionine |
activation of enzyme involves generation of a specific amino acid free radical that is dependent on a reduced Fe-S cluster and S-adenosylmethionine |
740653 |
| 1.1.98.6 | S-adenosyl-L-methionine |
S-adenosyl-L-methionine is directly reduced by the Fe-S center of the small subunits during the activation of the enzyme, resulting in methionine and glycyl radical formation. S-adenosyl-L-methionine binds to the small subunits with a Kd of 10 microM and a 1:1 stoichiometry. Dithiothreitol triggers the cleavage of S-adenosyl-L-methionine, leading glycyl radical formation. 3 methionines are formed per mol of protein |
740660 |
| 1.1.98.6 | S-adenosyl-L-methionine |
S-adenosylmethionine together with a metal participates in the generation of the radical required for the reduction of carbon 2' of the ribosyl moiety of CTP |
741348 |
| 1.1.98.6 | [4Fe-4S]-center |
S-adenosyl-L-methionine is directly reduced by the Fe-S center of the small subunits during the activation of the enzyme |
740660 |
| 1.1.98.6 | [4Fe-4S]-center |
the 17.5-kDa subunit contains a 4Fe-4S cluster that joins two peptides in a 35-kDa small homodimer (beta2) |
740659 |
| 1.1.98.6 | [4Fe-4S]-center |
the [4Fe-4S]+ form is extremely sensitive to oxygen and converted to [4Fe-4S]2+, [3Fe-4S]+/0, and to the stable [2Fe-2S]2+ form. The oxidized protein retains full activity. The [2Fe-2S] form of the protein can be converted into a [3Fe-4S] form during chromatography on dATP-Sepharose |
740769 |
