The Enzyme Database

Your query returned 1 entry.    printer_iconPrintable version

Accepted name: tRNA (N6-L-threonylcarbamoyladenosine37-C2)-methylthiotransferase
Reaction: N6-L-threonylcarbamoyladenine37 in tRNA + sulfur-(sulfur carrier) + 2 S-adenosyl-L-methionine + reduced electron acceptor = 2-methylthio-N6-L-threonylcarbamoyladenine37 in tRNA + S-adenosyl-L-homocysteine + (sulfur carrier) + L-methionine + 5′-deoxyadenosine + electron acceptor (overall reaction)
(1a) N6-L-threonylcarbamoyladenine37 in tRNA + sulfur-(sulfur carrier) + S-adenosyl-L-methionine + reduced electron acceptor = 2-thio-N6-L-threonylcarbamoyladenine37 in tRNA + (sulfur carrier) + L-methionine + 5-deoxyadenosine + electron acceptor
(1b) S-adenosyl-L-methionine + 2-thio-N6-L-threonylcarbamoyladenine37 in tRNA = S-adenosyl-L-homocysteine + 2-methylthio-N6-L-threonylcarbamoyladenine37 in tRNA
For diagram of N6-L-Threonylcarbamoyladenosine37 modified tRNA biosynthesis, click here
Glossary: N6-L-threonylcarbamoyladenine37 = t6A37
2-thio-N6-L-threonylcarbamoyladenine37 = ms2t6A37
Other name(s): MtaB; methylthio-threonylcarbamoyl-adenosine transferase B; CDKAL1 (gene name)
Systematic name: tRNA (N6-L-threonylcarbamoyladenosine37):sulfur-(sulfur carrier),S-adenosyl-L-methionine C2-methylthiotransferase
Comments: The enzyme, which is a member of the S-adenosyl-L-methionine-dependent radical (radical AdoMet) enzymes superfamily, binds two [4Fe-4S] clusters as well as the transferred sulfur. 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
1.  Arragain, S., Handelman, S.K., Forouhar, F., Wei, F.Y., Tomizawa, K., Hunt, J.F., Douki, T., Fontecave, M., Mulliez, E. and Atta, M. Identification of eukaryotic and prokaryotic methylthiotransferase for biosynthesis of 2-methylthio-N6-threonylcarbamoyladenosine in tRNA. J. Biol. Chem. 285 (2010) 28425–28433. [PMID: 20584901]
[EC created 2014, modified 2015]

Data © 2001–2016 IUBMB
Web site © 2005–2016 Andrew McDonald