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L-aspartate89-[ribosomal protein S12] + sulfur-(sulfur carrier) + 2 S-adenosyl-L-methionine + reduced acceptor = 3-(methylsulfanyl)-L-aspartate89-[ribosomal protein S12] + S-adenosyl-L-homocysteine + (sulfur carrier) + L-methionine + 5'-deoxyadenosine + oxidized acceptor
L-aspartate89-[ribosomal protein S12]-methanethiol + S-adenosyl-L-methionine + reduced acceptor = 3-(methylsulfanyl)-L-aspartate89-[ribosomal protein S12] + L-methionine + 5'-deoxyadenosine + oxidized acceptor
S-adenosyl-L-methionine + L-aspartate89-[ribosomal protein S12] + sulfur-(sulfur carrier) = S-adenosyl-L-homocysteine + L-aspartate89-[ribosomal protein S12]-methanethiol + (sulfur carrier)
L-aspartate89-[ribosomal protein S12] + sulfur-(sulfur carrier) + 2 S-adenosyl-L-methionine + reduced acceptor = 3-(methylsulfanyl)-L-aspartate89-[ribosomal protein S12] + S-adenosyl-L-homocysteine + (sulfur carrier) + L-methionine + 5'-deoxyadenosine + oxidized acceptor
(overall reaction)
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L-aspartate89-[ribosomal protein S12] + sulfur-(sulfur carrier) + 2 S-adenosyl-L-methionine + reduced acceptor = 3-(methylsulfanyl)-L-aspartate89-[ribosomal protein S12] + S-adenosyl-L-homocysteine + (sulfur carrier) + L-methionine + 5'-deoxyadenosine + oxidized acceptor
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L-aspartate89-[ribosomal protein S12]-methanethiol + S-adenosyl-L-methionine + reduced acceptor = 3-(methylsulfanyl)-L-aspartate89-[ribosomal protein S12] + L-methionine + 5'-deoxyadenosine + oxidized acceptor
(1b)
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L-aspartate89-[ribosomal protein S12]-methanethiol + S-adenosyl-L-methionine + reduced acceptor = 3-(methylsulfanyl)-L-aspartate89-[ribosomal protein S12] + L-methionine + 5'-deoxyadenosine + oxidized acceptor
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S-adenosyl-L-methionine + L-aspartate89-[ribosomal protein S12] + sulfur-(sulfur carrier) = S-adenosyl-L-homocysteine + L-aspartate89-[ribosomal protein S12]-methanethiol + (sulfur carrier)
(1a)
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S-adenosyl-L-methionine + L-aspartate89-[ribosomal protein S12] + sulfur-(sulfur carrier) = S-adenosyl-L-homocysteine + L-aspartate89-[ribosomal protein S12]-methanethiol + (sulfur carrier)
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3-methylthioaspartate89-[ribosomal protein S12 20mer peptide] + sulfur-(sulfur carrier) + 2 S-adenosyl-L-methionine
3,3-bismethylthioaspartate89-[ribosomal protein S12 20mer peptide] + S-adenosyl-L-homocysteine + (sulfur carrier) + L-methionine + 5'-deoxyadenosine
Asp88-[ribosomal protein S12] + sulfur-(sulfur carrier) + 2 S-adenosyl-L-methionine
3-methylthioaspartate88-[ribosomal protein S12] + S-adenosyl-L-homocysteine + (sulfur carrier) + L-methionine + 5'-deoxyadenosine
Asp89-[ribosomal protein S12 20mer peptide] + sulfur-(sulfur carrier) + 2 S-adenosyl-L-methionine
3-methylthioaspartate89-[ribosomal protein S12 20mer peptide] + S-adenosyl-L-homocysteine + (sulfur carrier) + L-methionine + 5'-deoxyadenosine
Asp89-[ribosomal protein S12] + sulfur-(sulfur carrier) + 2 S-adenosyl-L-methionine
3-methylthioaspartate89-[ribosomal protein S12] + S-adenosyl-L-homocysteine + (sulfur carrier) + L-methionine + 5'-deoxyadenosine
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L-aspartate89-[ribosomal protein S12] + sulfur-(sulfur carrier) + 2 S-adenosyl-L-methionine + reduced acceptor
3-methylthio-L-aspartate89-[ribosomal protein S12] + S-adenosyl-L-homocysteine + (sulfur carrier) + L-methionine + 5'-deoxyadenosine + oxidized acceptor
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L-aspartate89-[ribosomal protein S12] + sulfur-(sulfur carrier) + S-adenosyl-L-methionine + reduced acceptor
3-methylthio-L-aspartate89-[ribosomal protein S12] + S-adenosyl-L-homocysteine + (sulfur carrier) + L-methionine + 5'-deoxyadenosine + oxidized acceptor
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N6-dimethylallyladenine37 in tRNA + sulfur-(sulfur carrier) + 2 S-adenosyl-L-methionine
2-methylthio-N6-dimethylallyladenine37 in tRNA + S-adenosyl-L-homocysteine + (sulfur carrier) + L-methionine + 5'-deoxyadenosine
additional information
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3-methylthioaspartate89-[ribosomal protein S12 20mer peptide] + sulfur-(sulfur carrier) + 2 S-adenosyl-L-methionine
3,3-bismethylthioaspartate89-[ribosomal protein S12 20mer peptide] + S-adenosyl-L-homocysteine + (sulfur carrier) + L-methionine + 5'-deoxyadenosine
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3-methylthioaspartate89-[ribosomal protein S12 20mer peptide] + sulfur-(sulfur carrier) + 2 S-adenosyl-L-methionine
3,3-bismethylthioaspartate89-[ribosomal protein S12 20mer peptide] + S-adenosyl-L-homocysteine + (sulfur carrier) + L-methionine + 5'-deoxyadenosine
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Asp88-[ribosomal protein S12] + sulfur-(sulfur carrier) + 2 S-adenosyl-L-methionine
3-methylthioaspartate88-[ribosomal protein S12] + S-adenosyl-L-homocysteine + (sulfur carrier) + L-methionine + 5'-deoxyadenosine
substrate Escherichia coli S12 is modified at residue Asp88
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Asp88-[ribosomal protein S12] + sulfur-(sulfur carrier) + 2 S-adenosyl-L-methionine
3-methylthioaspartate88-[ribosomal protein S12] + S-adenosyl-L-homocysteine + (sulfur carrier) + L-methionine + 5'-deoxyadenosine
substrate Escherichia coli S12 is modified at residue Asp88
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Asp89-[ribosomal protein S12 20mer peptide] + sulfur-(sulfur carrier) + 2 S-adenosyl-L-methionine
3-methylthioaspartate89-[ribosomal protein S12 20mer peptide] + S-adenosyl-L-homocysteine + (sulfur carrier) + L-methionine + 5'-deoxyadenosine
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Asp89-[ribosomal protein S12 20mer peptide] + sulfur-(sulfur carrier) + 2 S-adenosyl-L-methionine
3-methylthioaspartate89-[ribosomal protein S12 20mer peptide] + S-adenosyl-L-homocysteine + (sulfur carrier) + L-methionine + 5'-deoxyadenosine
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N6-dimethylallyladenine37 in tRNA + sulfur-(sulfur carrier) + 2 S-adenosyl-L-methionine
2-methylthio-N6-dimethylallyladenine37 in tRNA + S-adenosyl-L-homocysteine + (sulfur carrier) + L-methionine + 5'-deoxyadenosine
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N6-dimethylallyladenine37 in tRNA + sulfur-(sulfur carrier) + 2 S-adenosyl-L-methionine
2-methylthio-N6-dimethylallyladenine37 in tRNA + S-adenosyl-L-homocysteine + (sulfur carrier) + L-methionine + 5'-deoxyadenosine
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additional information
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enzyme catalyzes methyl transfer from 2 S-adenosyl-L-methionine to an acid/base labile acceptor on the protein in the absence of their respective macromolecular substrates. Denaturation of the 2 S-adenosyl-L-methionine-treated protein with acid results in production of ethanethiol. When the enzyme is first incubated with 2 S-adenosyl-L-methionine in the absence of substrate and reductant and then incubated with excess S-adenosyl-L-[methyl-d3]methionine in the presence of substrate and reductant, production of the unlabeled product precedes production of the deuterated product, showing that the methylated species is chemically and kinetically competent to be an intermediate
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additional information
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holo-RimO can specifically methylthiolate the aspartate residue of a 20mer peptide derived from S12, yielding a mixture of mono- and bismethylthio derivatives
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additional information
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mechanism involves activation of an exogenous sulfur cosubstrate at an exchangeable coordination site on the second iron-sulfur cluster, which remains intact during the reaction. The enzyme has two distinct [4Fe-4S] clusters for binding and activation of two different cosubstrates. The radical-SAM cluster most likely activates SAM to form the canonical Ado· radical, as proposed for all radical-SAM enzymes, whereas the second cluster serves to activate sulfide or methylsulfide through a still-undefined mechanism
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additional information
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enzyme catalyzes methyl transfer from 2 S-adenosyl-L-methionine to an acid/base labile acceptor on the protein in the absence of their respective macromolecular substrates. Denaturation of the 2 S-adenosyl-L-methionine-treated protein with acid results in production of ethanethiol. When the enzyme is first incubated with 2 S-adenosyl-L-methionine in the absence of substrate and reductant and then incubated with excess S-adenosyl-L-[methyl-d3]methionine in the presence of substrate and reductant, production of the unlabeled product precedes production of the deuterated product, showing that the methylated species is chemically and kinetically competent to be an intermediate
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additional information
?
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holo-RimO can specifically methylthiolate the aspartate residue of a 20mer peptide derived from S12, yielding a mixture of mono- and bismethylthio derivatives
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?
additional information
?
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mechanism involves activation of an exogenous sulfur cosubstrate at an exchangeable coordination site on the second iron-sulfur cluster, which remains intact during the reaction. The enzyme has two distinct [4Fe-4S] clusters for binding and activation of two different cosubstrates. The radical-SAM cluster most likely activates SAM to form the canonical Ado· radical, as proposed for all radical-SAM enzymes, whereas the second cluster serves to activate sulfide or methylsulfide through a still-undefined mechanism
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Lee, K.H.; Saleh, L.; Anton, B.P.; Madinger, C.L.; Benner, J.S.; Iwig, D.F.; Roberts, R.J.; Krebs, C.; Booker, S.J.
Characterization of RimO, a new member of the methylthiotransferase subclass of the radical SAM superfamily
Biochemistry
48
10162-10174
2009
Escherichia coli
brenda
Landgraf, B.J.; Arcinas, A.J.; Lee, K.H.; Booker, S.J.
Identification of an intermediate methyl carrier in the radical S-adenosylmethionine methylthiotransferases RimO and MiaB
J. Am. Chem. Soc.
135
15404-15416
2013
Thermotoga maritima (Q9X2H6), Thermotoga maritima DSM 3109 (Q9X2H6)
brenda
Arragain, S.; Garcia-Serres, R.; Blondin, G.; Douki, T.; Clemancey, M.; Latour, J.M.; Forouhar, F.; Neely, H.; Montelione, G.T.; Hunt, J.F.; Mulliez, E.; Fontecave, M.; Atta, M.
Post-translational modification of ribosomal proteins: structural and functional characterization of RimO from Thermotoga maritima, a radical S-adenosylmethionine methylthiotransferase
J. Biol. Chem.
285
5792-5801
2010
Thermotoga maritima (Q9X2H6), Thermotoga maritima DSM 3109 (Q9X2H6)
brenda
Strader, M.; Costantino, N.; Elkins, C.; Chen, C.; Patel, I.; Makusky, A.; Choy, J.; Court, D.; Markey, S.; Kowalak, J.
A proteomic and transcriptomic approach reveals new insight into beta-methylthiolation of Escherichia coli ribosomal protein
Mol. Cell. Proteomics
10
M110.005199
2011
Escherichia coli (P0AEI4), Escherichia coli W3110 / ATCC 27325 (P0AEI4)
brenda
Forouhar, F.; Arragain, S.; Atta, M.; Gambarelli, S.; Mouesca, J.M.; Hussain, M.; Xiao, R.; Kieffer-Jaquinod, S.; Seetharaman, J.; Acton, T.B.; Montelione, G.T.; Mulliez, E.; Hunt, J.F.; Fontecave, M.
Two Fe-S clusters catalyze sulfur insertion by radical-SAM methylthiotransferases
Nat. Chem. Biol.
9
333-338
2013
Thermotoga maritima (Q9X2H6), Thermotoga maritima DSM 3109 (Q9X2H6)
brenda
Anton, B.P.; Saleh, L.; Benner, J.S.; Raleigh, E.A.; Kasif, S.; Roberts, R.J.
RimO, a MiaB-like enzyme, methylthiolates the universally conserved Asp88 residue of ribosomal protein S12 in Escherichia coli
Proc. Natl. Acad. Sci. USA
105
1826-1831
2008
Escherichia coli (P0AEI4)
brenda
Molle, T.; Moreau, Y.; Clemancey, M.; Forouhar, F.; Ravanat, J.L.; Duraffourg, N.; Fourmond, V.; Latour, J.M.; Gambarelli, S.; Mulliez, E.; Atta, M.
Redox behavior of the S-adenosylmethionine (SAM)-binding Fe-S cluster in methylthiotransferase RimO, toward understanding dual SAM activity
Biochemistry
55
5798-5808
2016
Thermotoga maritima (Q9X2H6)
brenda
Landgraf, B.J.; Booker, S.J.
Stereochemical course of the reaction catalyzed by RimO, a radical SAM methylthiotransferase
J. Am. Chem. Soc.
138
2889-2892
2016
Bacteroides thetaiotaomicron
brenda
2.8.4.4 [ribosomal protein S12] (aspartate89-C3)-methylthiotransferase
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