4.3.1.30	4Fe-4S-center	a radical S-adenosyl-L-methionine-dependent enzyme. Dependence on a [4Fe-4S] cluster and S-adenosyl-L-methionine for DesII activity	715304	
4.3.1.30	4Fe-4S-center	[4Fe-4S]1+ is the catalytically active form of all radical S-adenosyl-L-methionine-dependent enzymes. Dependence on a [4Fe-4S] cluster and S-adenosyl-L-methionine for DesII activity	715254, 715276	
4.3.1.30	additional information	in the experiment, the [4Fe-4S]2+ of DesII is reduced to [4Fe-4S]1+ by stepwise electron transfer from NADPH through flavodoxin and flavodoxin reductase. Accordingly, a system consisting of flavodoxin/flavodoxin reductase-NADPH or its equivalent from the cellular pool may serve as the in vivo reducing system for the DesII-catalyzed reaction	715254	
4.3.1.30	S-adenosyl-L-methionine	a radical S-adenosyl-L-methionine-dependent enzyme. Dependence on a [4Fe-4S] cluster and S-adenosyl-L-methionine for DesII activity	715254, 715304	
4.3.1.30	S-adenosyl-L-methionine	a radical S-adenosyl-L-methionine-dependent enzyme. Dependence on a [4Fe-4S] cluster and S-adenosyl-L-methionine for DesII activity. Radical S-adenosyl-L-methionine enzymes are an important class of biological catalysts involved in radical mediated transformations in both primary and secondary metabolic pathways. All of these enzymes contain a [4Fe-4S] cluster in the active-site and are S-adenosyl-L-methionine dependent. The reactions are initiated by a single electron transfer from the reduced [4Fe-4S]1+ cluster to SAM to induce the homolytic cleavage of the C5'-S bond in -adenosyl-L-methionine, which yields a reactive 5'-deoxyadenosyl radical along with L-methionine. The 5'-deoxyadenosyl radical is used to generate a substrate radical intermediate that is subsequently converted to product	715276