This bacterial enzyme binds two [4Fe-4S] clusters as well as the transferred sulfur [3]. The enzyme is a member of the superfamily of?S-adenosyl-L-methionine-dependent radical (radical AdoMet) enzymes. The sulfur donor is believed to be one of the [4Fe-4S] clusters, which is sacrificed in the process, so that?in vitro?the reaction is a single turnover. The identity of the electron donor is not known.
Cofactor
iron-sulfur
History
Reactions
N(6)-dimethylallyladenine(37) in tRNA + sulfur-(sulfur carrier) + 2 S-adenosyl-L-methionine + reduced electron acceptor = 2-methylthio- N(6)-dimethylallyladenine(37) in tRNA + S-adenosyl-L-homocysteine + (sulfur carrier) + L-methionine + 5′-deoxyadenosine + electron acceptor.
