Transferases;
Transferring sulfur-containing groups;
Transferring alkylthio groups
BRITE hierarchy

[ribosomal protein uS12]-L-aspartate89:sulfur-(sulfur carrier),S-adenosyl-L-methionine C3-(methylsulfanyl)transferase

L-aspartate89-[ribosomal protein uS12] + sulfur-(sulfur carrier) + 2 S-adenosyl-L-methionine + reduced acceptor = 3-(methylsulfanyl)-L-aspartate89-[ribosomal protein uS12] + S-adenosyl-L-homocysteine + (sulfur carrier) + L-methionine + 5'-deoxyadenosine + oxidized acceptor (overall reaction) [RN:R10652];
(1a) S-adenosyl-L-methionine + L-aspartate89-[ribosomal protein uS12] + sulfur-(sulfur carrier) = S-adenosyl-L-homocysteine + L-aspartate89-[ribosomal protein uS12]-methanethiol + (sulfur carrier);
(1b) L-aspartate89-[ribosomal protein uS12]-methanethiol + S-adenosyl-L-methionine + reduced acceptor = 3-(methylsulfanyl)-L-aspartate89-[ribosomal protein uS12] + L-methionine + 5'-deoxyadenosine + oxidized acceptor

R10652
Reaction

L-aspartate89-[ribosomal protein uS12];
sulfur-(sulfur carrier);
S-adenosyl-L-methionine [CPD:C00019];
reduced acceptor [CPD:C00030];
L-aspartate89-[ribosomal protein uS12]-methanethiol

This bacterial enzyme binds two [4Fe-4S] clusters [2,3]. A bridge of five sulfur atoms is formed between the free Fe atoms of the two [4Fe-4S] clusters [6]. In the first reaction the enzyme transfers a methyl group from AdoMet to the external sulfur ion of the sulfur bridge. In the second reaction the enzyme catalyses the reductive fragmentation of a second molecule of AdoMet, yielding a 5'-deoxyadenosine radical, which then attacks the methylated sulfur atom of the polysulfide bridge, resulting in the transfer of a methylsulfanyl group to aspartate89 [5,6]. The enzyme is a member of the superfamily of S-adenosyl-L-methionine-dependent radical (radical AdoMet) enzymes.

EC 2.8.4.4 created 2014, modified 2014, modified 2023