|Superclasses:||Reactions Classified By Conversion Type → Simple Reactions → Chemical Reactions → Protein-Modification Reactions|
|Reactions Classified By Conversion Type → Simple Reactions → Chemical Reactions|
|Reactions Classified By Substrate → Macromolecule Reactions → Protein-Reactions → Protein-Modification Reactions|
EC Number: 220.127.116.11
The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the direction in which it was curated.
Most BioCyc compounds have been protonated to a reference pH value of 7.3, and some reactions have been computationally balanced for hydrogen by adding free protons. Please see the PGDB Concepts Guide for more information.
Mass balance status: Balanced.
Enzyme Commission Primary Name: [ribosomal protein S12] (aspartate89-C3)-methylthiotransferase
Enzyme Commission Synonyms: RimO
Enzyme Commission Summary:
This bacterial enzyme binds two [4Fe-4S] clusters [Lee09, Arragain10]. A bridge of five sulfur atoms is formed between the free Fe atoms of the two [4Fe-4S] clusters [Forouhar13]. In the first reaction the enzyme transfers a methyl group from SAM to the external sulfur ion of the sulfur bridge. In the second reaction the enzyme catalyses the reductive fragmentation of a second molecule of SAM, yielding a 5'-deoxyadenosyl radical, which then attacks the methylated sulfur atom of the polysulfide bridge, resulting in the transfer of a methylthiol group to aspartate89 [Landgraf13, Forouhar13]. The enzyme is a member of the superfamily of S-adenosyl-L-methionine-dependent radical (radical AdoMet) enzymes.
Anton08: Anton BP, Saleh L, Benner JS, Raleigh EA, Kasif S, Roberts RJ (2008). "RimO, a MiaB-like enzyme, methylthiolates the universally conserved Asp88 residue of ribosomal protein S12 in Escherichia coli." Proc Natl Acad Sci U S A 105(6);1826-31. PMID: 18252828
Arragain10: Arragain S, Garcia-Serres R, Blondin G, Douki T, Clemancey M, Latour JM, Forouhar F, Neely H, Montelione GT, Hunt JF, Mulliez E, Fontecave M, Atta M (2010). "Post-translational modification of ribosomal proteins: structural and functional characterization of RimO from Thermotoga maritima, a radical S-adenosylmethionine methylthiotransferase." J Biol Chem 285(8);5792-801. PMID: 20007320
Forouhar13: Forouhar F, Arragain S, Atta M, Gambarelli S, Mouesca JM, Hussain M, Xiao R, Kieffer-Jaquinod S, Seetharaman J, Acton TB, Montelione GT, Mulliez E, Hunt JF, Fontecave M (2013). "Two Fe-S clusters catalyze sulfur insertion by radical-SAM methylthiotransferases." Nat Chem Biol 9(5);333-8. PMID: 23542644
Landgraf13: Landgraf BJ, Arcinas AJ, Lee KH, Booker SJ (2013). "Identification of an intermediate methyl carrier in the radical S-adenosylmethionine methylthiotransferases RimO and MiaB." J Am Chem Soc 135(41);15404-16. PMID: 23991893
Lee09: Lee KH, Saleh L, Anton BP, Madinger CL, Benner JS, Iwig DF, Roberts RJ, Krebs C, Booker SJ (2009). "Characterization of RimO, a new member of the methylthiotransferase subclass of the radical SAM superfamily." Biochemistry 48(42);10162-74. PMID: 19736993
Strader11: Strader MB, Costantino N, Elkins CA, Chen CY, Patel I, Makusky AJ, Choy JS, Court DL, Markey SP, Kowalak JA (2011). "A proteomic and transcriptomic approach reveals new insight into beta-methylthiolation of Escherichia coli ribosomal protein S12." Mol Cell Proteomics 10(3);M110.005199. PMID: 21169565
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