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Literature summary extracted from

  • 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 (2013), Nat. Chem. Biol., 9, 333-338.
    View publication on PubMedView publication on EuropePMC

Organism

EC Number Organism UniProt Comment Textmining
2.8.4.3 Thermotoga maritima Q9WZC1
-
-
2.8.4.3 Thermotoga maritima DSM 3109 Q9WZC1
-
-
2.8.4.4 Thermotoga maritima Q9X2H6
-
-
2.8.4.4 Thermotoga maritima DSM 3109 Q9X2H6
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.8.4.3 additional information 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 Thermotoga maritima ?
-
 ?
2.8.4.3 additional information 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 Thermotoga maritima DSM 3109 ?
-
 ?
2.8.4.3 N6-dimethylallyladenine37 in tRNA + sulfur-(sulfur carrier) + 2 S-adenosyl-L-methionine
-
 Thermotoga maritima 2-methylthio-N6-dimethylallyladenine37 in tRNA + S-adenosyl-L-homocysteine + (sulfur carrier) + L-methionine + 5'-deoxyadenosine
-
 ?
2.8.4.3 N6-dimethylallyladenine37 in tRNA + sulfur-(sulfur carrier) + 2 S-adenosyl-L-methionine
-
 Thermotoga maritima DSM 3109 2-methylthio-N6-dimethylallyladenine37 in tRNA + S-adenosyl-L-homocysteine + (sulfur carrier) + L-methionine + 5'-deoxyadenosine
-
 ?
2.8.4.4 additional information 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 Thermotoga maritima ?
-
 ?
2.8.4.4 additional information 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 Thermotoga maritima DSM 3109 ?
-
 ?
2.8.4.4 N6-dimethylallyladenine37 in tRNA + sulfur-(sulfur carrier) + 2 S-adenosyl-L-methionine
-
 Thermotoga maritima 2-methylthio-N6-dimethylallyladenine37 in tRNA + S-adenosyl-L-homocysteine + (sulfur carrier) + L-methionine + 5'-deoxyadenosine
-
 ?
2.8.4.4 N6-dimethylallyladenine37 in tRNA + sulfur-(sulfur carrier) + 2 S-adenosyl-L-methionine
-
 Thermotoga maritima DSM 3109 2-methylthio-N6-dimethylallyladenine37 in tRNA + S-adenosyl-L-homocysteine + (sulfur carrier) + L-methionine + 5'-deoxyadenosine
-
 ?

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.8.4.3 65
-
 assay at Thermotoga maritima
2.8.4.4 65
-
 assay at Thermotoga maritima