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N6-dimethylallyladenine37 in tRNA + sulfur-(sulfur carrier) + 2 S-adenosyl-L-methionine + reduced electron acceptor = 2-(methylsulfanyl)-N6-dimethylallyladenine37 in tRNA + S-adenosyl-L-homocysteine + (sulfur carrier) + L-methionine + 5'-deoxyadenosine + electron acceptor
N6-dimethylallyladenine37 in tRNA + sulfur-(sulfur carrier) + S-adenosyl-L-methionine + reduced electron acceptor = 2-sulfanyl-N6-dimethylallyladenine37 in tRNA + (sulfur carrier) + L-methionine + 5'-deoxyadenosine + electron acceptor
S-adenosyl-L-methionine + 2-sulfanyl-N6-dimethylallyladenine37 in tRNA = S-adenosyl-L-homocysteine + 2-(methylsulfanyl)-N6-dimethylallyladenine37 in tRNA
N6-dimethylallyladenine37 in tRNA + sulfur-(sulfur carrier) + 2 S-adenosyl-L-methionine + reduced electron acceptor = 2-(methylsulfanyl)-N6-dimethylallyladenine37 in tRNA + S-adenosyl-L-homocysteine + (sulfur carrier) + L-methionine + 5'-deoxyadenosine + electron acceptor
(overall reaction)
N6-dimethylallyladenine37 in tRNA + sulfur-(sulfur carrier) + 2 S-adenosyl-L-methionine + reduced electron acceptor = 2-(methylsulfanyl)-N6-dimethylallyladenine37 in tRNA + S-adenosyl-L-homocysteine + (sulfur carrier) + L-methionine + 5'-deoxyadenosine + electron acceptor
(overall reaction)
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N6-dimethylallyladenine37 in tRNA + sulfur-(sulfur carrier) + 2 S-adenosyl-L-methionine + reduced electron acceptor = 2-(methylsulfanyl)-N6-dimethylallyladenine37 in tRNA + S-adenosyl-L-homocysteine + (sulfur carrier) + L-methionine + 5'-deoxyadenosine + electron acceptor
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N6-dimethylallyladenine37 in tRNA + sulfur-(sulfur carrier) + S-adenosyl-L-methionine + reduced electron acceptor = 2-sulfanyl-N6-dimethylallyladenine37 in tRNA + (sulfur carrier) + L-methionine + 5'-deoxyadenosine + electron acceptor
(1a)
N6-dimethylallyladenine37 in tRNA + sulfur-(sulfur carrier) + S-adenosyl-L-methionine + reduced electron acceptor = 2-sulfanyl-N6-dimethylallyladenine37 in tRNA + (sulfur carrier) + L-methionine + 5'-deoxyadenosine + electron acceptor
(1a)
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N6-dimethylallyladenine37 in tRNA + sulfur-(sulfur carrier) + S-adenosyl-L-methionine + reduced electron acceptor = 2-sulfanyl-N6-dimethylallyladenine37 in tRNA + (sulfur carrier) + L-methionine + 5'-deoxyadenosine + electron acceptor
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S-adenosyl-L-methionine + 2-sulfanyl-N6-dimethylallyladenine37 in tRNA = S-adenosyl-L-homocysteine + 2-(methylsulfanyl)-N6-dimethylallyladenine37 in tRNA
(1b)
S-adenosyl-L-methionine + 2-sulfanyl-N6-dimethylallyladenine37 in tRNA = S-adenosyl-L-homocysteine + 2-(methylsulfanyl)-N6-dimethylallyladenine37 in tRNA
(1b)
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S-adenosyl-L-methionine + 2-sulfanyl-N6-dimethylallyladenine37 in tRNA = S-adenosyl-L-homocysteine + 2-(methylsulfanyl)-N6-dimethylallyladenine37 in tRNA
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N6-dimethylallyladenine in tRNA + sulfur-(sulfur carrier) + 2 S-adenosyl-L-methionine
2-methylthio-N6-dimethylallyladenine in tRNA + S-adenosyl-L-homocysteine + (sulfur carrier) + L-methionine + 5'-deoxyadenosine
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
N6-dimethylallyladenine37 in tRNA + sulfur-(sulfur carrier) + S-adenosyl-L-methionine
2-thio-N6-dimethylallyladenine37 in tRNA + (sulfur carrier) + L-methionine + 5'-deoxyadenosine
S-adenosyl-L-methionine + 2-thio-N6-dimethylallyladenine37 in tRNA
S-adenosyl-L-homocysteine + 2-methylthio-N6-dimethylallyladenine37 in tRNA
additional information
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N6-dimethylallyladenine in tRNA + sulfur-(sulfur carrier) + 2 S-adenosyl-L-methionine
2-methylthio-N6-dimethylallyladenine in tRNA + S-adenosyl-L-homocysteine + (sulfur carrier) + L-methionine + 5'-deoxyadenosine
substrate is a synthetic N6-dimethylallyladenine-containing RNA corresponding to the anticodon stem loop of tRNAPhe
overall reaction
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N6-dimethylallyladenine in tRNA + sulfur-(sulfur carrier) + 2 S-adenosyl-L-methionine
2-methylthio-N6-dimethylallyladenine in tRNA + S-adenosyl-L-homocysteine + (sulfur carrier) + L-methionine + 5'-deoxyadenosine
substrate is a synthetic N6-dimethylallyladenine-containing RNA corresponding to the anticodon stem loop of tRNAPhe
overall reaction
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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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overall reaction
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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
methylthiolation of N-6-isopentenyl adenosine in tRNAs
overall reaction
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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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overall reaction
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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
methylthiolation of N-6-isopentenyl adenosine in tRNAs
overall reaction
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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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overall reaction
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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) + S-adenosyl-L-methionine
2-thio-N6-dimethylallyladenine37 in tRNA + (sulfur carrier) + L-methionine + 5'-deoxyadenosine
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N6-dimethylallyladenine37 in tRNA + sulfur-(sulfur carrier) + S-adenosyl-L-methionine
2-thio-N6-dimethylallyladenine37 in tRNA + (sulfur carrier) + L-methionine + 5'-deoxyadenosine
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S-adenosyl-L-methionine + 2-thio-N6-dimethylallyladenine37 in tRNA
S-adenosyl-L-homocysteine + 2-methylthio-N6-dimethylallyladenine37 in tRNA
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S-adenosyl-L-methionine + 2-thio-N6-dimethylallyladenine37 in tRNA
S-adenosyl-L-homocysteine + 2-methylthio-N6-dimethylallyladenine37 in tRNA
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additional information
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enzyme catalyzes methyl transfer from S-adenosyl-L-methionine to an acid/base labile acceptor on the protein in the absence of their respective macromolecular substrates. Denaturation of the S-adenosyl-L-methionine-treated protein with acid results in production of ethanethiol. When the enzyme is first incubated with 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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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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MiaB protein is a bifunctional system, involved in both thiolation and methylation of N6-dimethylallyladenine. In this process, one molecule of S-adenosyl-L-methionine is converted to 5'-deoxyadenosine, probably through reductive cleavage and intermediate formation of a 5'-deoxyadenosyl radical as observed in other radical-S-adenosyl-L-methionine enzymes, and a second molecule of S-adenosyl-L-methionine is used as a methyl donor
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additional information
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enzyme catalyzes methyl transfer from S-adenosyl-L-methionine to an acid/base labile acceptor on the protein in the absence of their respective macromolecular substrates. Denaturation of the S-adenosyl-L-methionine-treated protein with acid results in production of ethanethiol. When the enzyme is first incubated with 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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MiaB protein is a bifunctional system, involved in both thiolation and methylation of N6-dimethylallyladenine. In this process, one molecule of S-adenosyl-L-methionine is converted to 5'-deoxyadenosine, probably through reductive cleavage and intermediate formation of a 5'-deoxyadenosyl radical as observed in other radical-S-adenosyl-L-methionine enzymes, and a second molecule of S-adenosyl-L-methionine is used as a methyl donor
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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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S-adenosyl-L-methionine
the enzyme is a member of the superfamily of S-adenosyl-L-methionine-dependent radical (radical AdoMet) enzymes
[4Fe-4S]-center
enzyme MiaB contains both iron and sulfide and an apoprotein form can chelate as much as 2.5-3 iron and 3-3.5 sulfur atoms per polypeptide chain. Under reducing and anaerobic conditions, a [4Fe-4S] cluster is present, whereas [2Fe-2S] and [3Fe-4S] forms are generated under aerobic conditions. Residues Cys157, Cys161, and Cys164 are involved in iron chelation, and the cluster is essential for activity
[4Fe-4S]-center
presence of two distinct [4Fe-4S]2+,1+ clusters in the protein. One is coordinated by residues Cys150, Cys154, and Cys157 in the radical-AdoMet motif, and the other is proposed to be coordinated by the three N-terminal conserved cysteines Cys10, Cys46, and Cys79. The two [4Fe-4S]2+ clusters have similar UV-visible absorption, resonance Raman, and Moessbauer properties but differ in terms of redox properties and the EPR properties of the reduced [4Fe-4S]1+ clusters
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Pierrel, F.; Hernandez, H.L.; Johnson, M.K.; Fontecave, M.; Atta, M.
MiaB protein from Thermotoga maritima. Characterization of an extremely thermophilic tRNA-methylthiotransferase
J. Biol. Chem.
278
29515-29524
2003
Thermotoga maritima (Q9WZC1), Thermotoga maritima DSM 3109 (Q9WZC1)
brenda
Hernandez, H.L.; Pierrel, F.; Elleingand, E.; Garcia-Serres, R.; Huynh, B.H.; Johnson, M.K.; Fontecave, M.; Atta, M.
MiaB, a bifunctional radical-S-adenosylmethionine enzyme involved in the thiolation and methylation of tRNA, contains two essential [4Fe-4S] clusters
Biochemistry
46
5140-5147
2007
Thermotoga maritima (Q9WZC1), Thermotoga maritima DSM 3109 (Q9WZC1)
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 (Q9WZC1), Thermotoga maritima DSM 3109 (Q9WZC1)
brenda
Pierrel, F.; Bjoerk, G.R.; Fontecave, M.; Atta, M.
Enzymatic modification of tRNAs: MiaB is an iron-sulfur protein
J. Biol. Chem.
277
13367-13370
2002
Escherichia coli (P0AEI1)
brenda
Pierrel, F.; Douki, T.; Fontecave, M.; Atta, M.
MiaB protein is a bifunctional radical-S-adenosylmethionine enzyme involved in thiolation and methylation of tRNA
J. Biol. Chem.
279
47555-47563
2004
Thermotoga maritima (Q9WZC1), Thermotoga maritima DSM 3109 (Q9WZC1)
brenda
Boutigny, S.; Saini, A.; Baidoo, E.E.; Yeung, N.; Keasling, J.D.; Butland, G.
Physical and functional interactions of a monothiol glutaredoxin and an iron sulfur cluster carrier protein with the sulfur-donating radical S-adenosyl-L-methionine enzyme MiaB
J. Biol. Chem.
288
14200-14211
2013
Escherichia coli (P0AEI1)
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 (Q9WZC1), Thermotoga maritima DSM 3109 (Q9WZC1)
brenda