The Enzyme Database

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EC 2.1.1.230     
Accepted name: 23S rRNA (adenosine1067-2′-O)-methyltransferase
Reaction: S-adenosyl-L-methionine + adenosine1067 in 23S rRNA = S-adenosyl-L-homocysteine + 2′-O-methyladenosine1067 in 23S rRNA
Other name(s): 23S rRNA A1067 2′-methyltransferase; thiostrepton-resistance methylase; nosiheptide-resistance methyltransferase
Systematic name: S-adenosyl-L-methionine:23S rRNA (adenosine1067-2′-O)-methyltransferase
Comments: The methylase that is responsible for autoimmunity in the thiostrepton producer Streptomyces azureus, renders ribosomes completely resistant to thiostrepton [2].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Bechthold, A. and Floss, H.G. Overexpression of the thiostrepton-resistance gene from Streptomyces azureus in Escherichia coli and characterization of recognition sites of the 23S rRNA A1067 2′-methyltransferase in the guanosine triphosphatase center of 23S ribosomal RNA. Eur. J. Biochem. 224 (1994) 431–437. [PMID: 7925357]
2.  Thompson, J., Schmidt, F. and Cundliffe, E. Site of action of a ribosomal RNA methylase conferring resistance to thiostrepton. J. Biol. Chem. 257 (1982) 7915–7917. [PMID: 6806287]
3.  Thompson, J. and Cundliffe, E. Purification and properties of an RNA methylase produced by Streptomyces azureus and involved in resistance to thiostrepton. J. Gen. Microbiol. 124 (1981) 291–297.
4.  Yang, H., Wang, Z., Shen, Y., Wang, P., Jia, X., Zhao, L., Zhou, P., Gong, R., Li, Z., Yang, Y., Chen, D., Murchie, A.I. and Xu, Y. Crystal structure of the nosiheptide-resistance methyltransferase of Streptomyces actuosus. Biochemistry 49 (2010) 6440–6450. [PMID: 20550164]
[EC 2.1.1.230 created 2011]
 
 


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