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EC Number Substrates Commentary Substrates Organism Products Commentary (Products) Reversibility
Display the word mapDisplay the reaction diagram Show all sequences 2.1.1.230more compared the methylation activity of the Arg135Ala NHR heterodimer with the wild-type NHR homodimer and a series of 29 nt wild-type and mutant RNA substrates. The inactive heterodimer complex binds the RNA more efficiently than the inactive mutant homodimer. Construction of diverse mutant RNA substrates in which A1067 is replaced by adenine structural analogues, A1067G retains significant activity, while 7-deaza-A and 1-methyl-A substitutions at A1067 reduce the activity, overview Streptomyces actuosus ? - ?
Display the word mapDisplay the reaction diagram Show all sequences 2.1.1.230S-adenosyl-L-methionine + adenosine in an RNA fragment containing nucleotides 1029-1122 of the 23S ribosomal RNA from Escherichia coli - Streptomyces azureus S-adenosyl-L-homocysteine + 2'-O-methyladenosine in an RNA fragment containing nucleotides 1029-1122 of the 23S ribosomal RNA from Escherichia coli - ?
Display the word mapDisplay the reaction diagram Show all sequences 2.1.1.230S-adenosyl-L-methionine + adenosine1067 in 23S rRNA - Streptomyces azureus S-adenosyl-L-homocysteine + 2'-O-methyladenosine1067 in 23S rRNA - ?
Display the word mapDisplay the reaction diagram Show all sequences 2.1.1.230S-adenosyl-L-methionine + adenosine1067 in 23S rRNA - Streptomyces actuosus S-adenosyl-L-homocysteine + 2'-O-methyladenosine1067 in 23S rRNA - ?
Display the word mapDisplay the reaction diagram Show all sequences 2.1.1.230S-adenosyl-L-methionine + adenosine1067 in 23S rRNA Streptomyces azureus is the producer of the peptide antibiotic thiostrepton. Thiostrepton inhibits protein synthesis by binding to the complex of 23S rRNA and protein L-11 which blocks processes associated with the GTP-hydrolysis center of the ribosome including the binding of guanine nucleotides, elongation factor proteins and tRNA. 23S rRNA (adenosine1067-2'-O)-methyltransferase confers resistance to tthiostrepton Streptomyces azureus S-adenosyl-L-homocysteine + 2'-O-methyladenosine1067 in 23S rRNA - ?
Display the word mapDisplay the reaction diagram Show all sequences 2.1.1.230S-adenosyl-L-methionine + adenosine1067 in 23S rRNA the enzyme is involved in resistance to thiostrepton Streptomyces azureus S-adenosyl-L-homocysteine + 2'-O-methyladenosine1067 in 23S rRNA - ?
Display the word mapDisplay the reaction diagram Show all sequences 2.1.1.230S-adenosyl-L-methionine + adenosine1067 in 23S rRNA the methylase enzyme, responsible for autoimmunity in the thiostrepton producer Streptomyces azureus, renders ribosomes completely resistant to thiostrepton Streptomyces azureus S-adenosyl-L-homocysteine + 2'-O-methyladenosine1067 in 23S rRNA - ?
Display the word mapDisplay the reaction diagram Show all sequences 2.1.1.230S-adenosyl-L-methionine + adenosine1067 in 23S rRNA RNA sequence variants of the RNA fragment with mutations in nucleotides 1051-1108 are tested as substrates for the methylase. Methylation is dependent on the secondary structure of the hairpin including nucleotide A1067 and the exact sequence U(1066)-A(1067)-G(1068)-A(1O69)-A(1070) of the single strand Streptomyces azureus S-adenosyl-L-homocysteine + 2'-O-methyladenosine1067 in 23S rRNA - ?
Display the word mapDisplay the reaction diagram Show all sequences 2.1.1.230S-adenosyl-L-methionine + adenosine1067 in 23S rRNA enzyme Tsr uses the co-substrate AdoMet to methylate the 23 S rRNA, presumably prior to the assembly of the 50 S subunit as the L11 and proposed Tsr binding surfaces are overlapping Streptomyces azureus S-adenosyl-L-homocysteine + 2'-O-methyladenosine1067 in 23S rRNA - ?
Display the word mapDisplay the reaction diagram Show all sequences 2.1.1.230S-adenosyl-L-methionine + adenosine1067 in 23S rRNA 58-nt RNA substrate secondary structure, and key longrange interactions within the 58-nt domain tertiary fold, overview Streptomyces azureus S-adenosyl-L-homocysteine + 2'-O-methyladenosine1067 in 23S rRNA - ?
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