The Enzyme Database

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EC 2.1.1.61     
Accepted name: tRNA 5-(aminomethyl)-2-thiouridylate-methyltransferase
Reaction: S-adenosyl-L-methionine + tRNA containing 5-(aminomethyl)-2-thiouridine = S-adenosyl-L-homocysteine + tRNA containing 5-[(methylamino)methyl]-2-thiouridylate
Other name(s): transfer ribonucleate 5-methylaminomethyl-2-thiouridylate 5-methyltransferase; tRNA 5-methylaminomethyl-2-thiouridylate 5′-methyltransferase; S-adenosyl-L-methionine:tRNA (5-methylaminomethyl-2-thio-uridylate)-methyltransferase; tRNA (5-methylaminomethyl-2-thiouridylate)-methyltransferase
Systematic name: S-adenosyl-L-methionine:tRNA 5-(aminomethyl)-2-thiouridylate N-methyltransferase
Comments: This enzyme specifically adds the terminal methyl group of 5-[(methylamino)methyl]-2-thiouridylate.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 39391-17-8
References:
1.  Taya, Y. and Nishimura, S. Biosynthesis of 5-methylaminomethyl-2-thiouridylate. I. Isolation of a new tRNA-methylase specific for 5-methylaminomethyl-2-thiouridylate. Biochem. Biophys. Res. Commun. 51 (1973) 1062–1068. [DOI] [PMID: 4703553]
2.  Taya, Y. and Nishimura, S. In: Salvatore, F., Borek, E., Zappia, V., Williams-Ashman, H.G. and Schlenk, F. (Ed.), The Biochemistry of Adenosylmethionine, Columbia University Press, New York, 1977, p. 251.
3.  Bujnicki, J.M., Oudjama, Y., Roovers, M., Owczarek, S., Caillet, J. and Droogmans, L. Identification of a bifunctional enzyme MnmC involved in the biosynthesis of a hypermodified uridine in the wobble position of tRNA. RNA 10 (2004) 1236–1242. [DOI] [PMID: 15247431]
4.  Kim, J. and Almo, S.C. Structural basis for hypermodification of the wobble uridine in tRNA by bifunctional enzyme MnmC. BMC Struct Biol 13:5 (2013). [DOI] [PMID: 23617613]
[EC 2.1.1.61 created 1982, modified 2012, modified 2021]
 
 


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