| Product Name |
[ribosomal protein S12] (aspartate89-C3)-methylthiotransferase |
| Example Structure |
![Example Structure of [ribosomal protein S12] (aspartate89-C3)-methylthiotransferase EC#: 2.8.4.4](/wp-content/uploads/enzyme-structure/2.8.4.4.jpg) |
| Synonyms |
ribosomal protein S12 methylthiotransferase, ribosome maturation factor RimO, RimO, S12 methylthiotransferase, yliG |
| EC Number |
2.8.4.4 |
| CAS Registry Number |
|
| Comments |
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. |
| Cofactor |
iron-sulfur |
| History |
|
| Reactions |
L-aspartate-[ribosomal protein S12] + sulfur-(sulfur carrier) + 2 S-adenosyl-L-methionine = 3-methylthio-L-aspartate-[ribosomal protein S12] + S-adenosyl-L-homocysteine + (sulfur carrier) + L-methionine + 5′-deoxyadenosine. |
