The Enzyme Database

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EC 2.8.4.3     
Accepted name: tRNA-2-methylthio-N6-dimethylallyladenosine synthase
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)
(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
(1b) S-adenosyl-L-methionine + 2-sulfanyl-N6-dimethylallyladenine37 in tRNA = S-adenosyl-L-homocysteine + 2-methylsulfanyl-N6-dimethylallyladenine37 in tRNA
For diagram of N6-(Dimethylallyl)adenosine37 modified tRNA biosynthesis, click here
Other name(s): MiaB; 2-methylthio-N-6-isopentenyl adenosine synthase; tRNA-i6A37 methylthiotransferase; tRNA (N6-dimethylallyladenosine37):sulfur-(sulfur carrier),S-adenosyl-L-methionine C2-methylthiotransferase
Systematic name: tRNA (N6-dimethylallyladenosine37):sulfur-(sulfur carrier),S-adenosyl-L-methionine C2-(methylsulfanyl)transferase
Comments: This bacterial enzyme binds two [4Fe-4S] clusters as well as the transferred sulfur [3]. The enzyme is a member of the superfamily of S-adenosyl-L-methionine-dependent radical (radical AdoMet) enzymes. The sulfur donor is believed to be one of the [4Fe-4S] clusters, which is sacrificed in the process, so that in vitro the reaction is a single turnover. The identity of the electron donor is not known.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Pierrel, F., Bjork, G.R., Fontecave, M. and Atta, M. Enzymatic modification of tRNAs: MiaB is an iron-sulfur protein. J. Biol. Chem. 277 (2002) 13367–13370. [PMID: 11882645]
2.  Pierrel, F., Hernandez, H.L., Johnson, M.K., Fontecave, M. and Atta, M. MiaB protein from Thermotoga maritima. Characterization of an extremely thermophilic tRNA-methylthiotransferase. J. Biol. Chem. 278 (2003) 29515–29524. [PMID: 12766153]
3.  Pierrel, F., Douki, T., Fontecave, M. and Atta, M. MiaB protein is a bifunctional radical-S-adenosylmethionine enzyme involved in thiolation and methylation of tRNA. J. Biol. Chem. 279 (2004) 47555–47563. [PMID: 15339930]
4.  Hernandez, H.L., Pierrel, F., Elleingand, E., Garcia-Serres, R., Huynh, B.H., Johnson, M.K., Fontecave, M. and 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 (2007) 5140–5147. [PMID: 17407324]
5.  Landgraf, B.J., Arcinas, A.J., Lee, K.H. and Booker, S.J. Identification of an intermediate methyl carrier in the radical S-adenosylmethionine methylthiotransferases RimO and MiaB. J. Am. Chem. Soc. 135 (2013) 15404–15416. [PMID: 23991893]
[EC 2.8.4.3 created 2014, modified 2015]
 
 


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