2.1.1.184: 23S rRNA (adenine2085-N6)-dimethyltransferase
This is an abbreviated version!
For detailed information about 23S rRNA (adenine2085-N6)-dimethyltransferase, go to the full flat file.
Word Map on EC 2.1.1.184
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2.1.1.184
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macrolide
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macrolide-lincosamide-streptogramin
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methyltransferases
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lincosamide
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unmethylated
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mtases
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streptogramine
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medicine
- 2.1.1.184
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macrolide
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macrolide-lincosamide-streptogramin
- methyltransferases
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lincosamide
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unmethylated
- mtases
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streptogramine
- medicine
Reaction
2 S-adenosyl-L-methionine
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Synonyms
23S ribosomal RNA adenine N-6 methyltransferase, EC 2.1.1.48, ErmC, ermC 23 S rRNA methyltransferase, ErmC 23S rRNA methyltransferase, ermC methylase, ErmC methyltransferase, ErmC', ErmC' methyltransferase, ErmC' MTase, erythromycin resistance protein, rRNA methyltransferase ErmC', rRNA:m6A methyltransferase ErmC'
ECTree
2.1.1.184 23S rRNA (adenine2085-N6)-dimethyltransferaseAdvanced search results
results (
results (Substrates Products
Substrates Products on EC 2.1.1.184 - 23S rRNA (adenine2085-N6)-dimethyltransferase
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SUBSTRATE 
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2 S-adenosyl-L-methionine + adenine2085 in 23S rRNA
2 S-adenosyl-L-homocysteine + N6-dimethyladenine2085 in 23S rRNA
2 S-adenosyl-L-methionine + adenine2085 in a 262-nucleotide RNA fragment within domain V of Bacillus subtilis 23S rRNA
2 S-adenosyl-L-homocysteine + N6-dimethyladenine2085 in 262-nucleotide RNA fragment within domain V of Bacillus subtilis 23S rRNA
a 262-nucleotide RNA fragment within domain V of Bacillus subtilis 23S rRNA can be utilized efficiently as a substrate for methylation at adenine2085
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2 S-adenosyl-L-methionine + adenine2085 in a 623-nucleotide RNA fragment within domain V of Bacillus subtilis 23S rRNA
2 S-adenosyl-L-homocysteine + N6-dimethyladenine2085 in a 623-nucleotide RNA fragment within domain V of Bacillus subtilis 23S rRNA
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2 S-adenosyl-L-methionine + adenine2085 in a 623-nucleotide RNA fragment within domain V of Bacillus subtilis 23S rRNA with mutation A2086T
2 S-adenosyl-L-homocysteine + N6-dimethyladenine2085 in a 623-nucleotide RNA fragment within domain V of Bacillus subtilis 23S rRNA with mutation A2086T
the A2086T change is methylated to ca. 50% of the level of wild-type domain V
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S-adenosyl-L-methionine + 23S rRNA
S-adenosyl-L-homocysteine + 23S rRNA containing N6-dimethyladenine
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S-adenosyl-L-methionine + 262-nucleotide RNA fragment within domain V of Bacillus subtilis 23S rRNA
S-adenosyl-L-homocysteine + 262-nucleotide RNA fragment within domain V of Bacillus subtilis 23S rRNA containing N6-dimethyladenine
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S-adenosyl-L-methionine + 623-nucleotide RNA fragment within domain V of Bacillus subtilis 23S rRNA
S-adenosyl-L-homocysteine + 623-nucleotide RNA fragment within domain V of Bacillus subtilis 23S rRNA containing N6-dimethyladenine
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S-adenosyl-L-methionine + 623-nucleotide RNA fragment within domain V of Bacillus subtilis 23S rRNA with mutation A2086T
S-adenosyl-L-homocysteine + 623-nucleotide RNA fragment within domain V of Bacillus subtilis 23S rRNA with mutation A2086T containing N6-dimethyladenine
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S-adenosyl-L-methionine + adenine2085 in 23S rRNA
S-adenosyl-L-homocysteine + N6-dimethyladenine2085 in 23S rRNA
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adenine2085 in 23S rRNA from Bacillus subtilis equals adenine2058 in Escherichia coli 23S rRNA
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2 S-adenosyl-L-methionine + adenine2085 in 23S rRNA
2 S-adenosyl-L-homocysteine + N6-dimethyladenine2085 in 23S rRNA
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2 S-adenosyl-L-methionine + adenine2085 in 23S rRNA
2 S-adenosyl-L-homocysteine + N6-dimethyladenine2085 in 23S rRNA
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2 S-adenosyl-L-methionine + adenine2085 in 23S rRNA
2 S-adenosyl-L-homocysteine + N6-dimethyladenine2085 in 23S rRNA
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2 S-adenosyl-L-methionine + adenine2085 in 23S rRNA
2 S-adenosyl-L-homocysteine + N6-dimethyladenine2085 in 23S rRNA
ErmC is a methyltransferase that confers resistance to the macrolide-lincosamide-streptogramin B group of antibiotics by catalyzing the methylation of 23S rRNA at a specific adenine residue (A2085 in Bacillus subtilis)
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2 S-adenosyl-L-methionine + adenine2085 in 23S rRNA
2 S-adenosyl-L-homocysteine + N6-dimethyladenine2085 in 23S rRNA
the rRNA methyltransferase ErmC0 transfers methyl groups from S-adenosyl-L-methionine to atom N6 of an adenine base within the peptidyltransferase loop of 23 S rRNA, thus conferring antibiotic resistance against a number of macrolide antibiotics
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2 S-adenosyl-L-methionine + adenine2085 in 23S rRNA
2 S-adenosyl-L-homocysteine + N6-dimethyladenine2085 in 23S rRNA
ermC methyltransferase produces both N6-mono and N6,N6-dimethylated adenine residues in Bacillus subtilis 23 S rRNA during the course of the reaction in vitro. The addition of the two methyl groups to each 23 S rRNA molecule takes place through a monomethylated intermediate and suggest that the enzyme dissociates from its RNA substrate between the two consecutive methylation reactions. The enzyme is able to utilize monomethylated RNA as substrate for the addition of a second methyl group with an efficiency approximately comparable to that obtained when unmethylated RNA is the initial substrate
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2 S-adenosyl-L-methionine + adenine2085 in 23S rRNA
2 S-adenosyl-L-homocysteine + N6-dimethyladenine2085 in 23S rRNA
since methyl groups are incorporated in protein-free 23S rRNA molecules, the structure of rRNA alone must contain sufficient information to specify the methylation site. Highest incorporation is obtained with Bacillus subtilis 23S rRNA. Escherichia coli 23S rRNA acts as a poorer substrate (35% of the methylation obtained with Bacillus subtilis 23S rRNA)
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2 S-adenosyl-L-methionine + adenine2085 in 23S rRNA
2 S-adenosyl-L-homocysteine + N6-dimethyladenine2085 in 23S rRNA
synthetic 32-nt RNA oligonucleotide (5-GCGACGGACGGA2085AAGACCCCUAUCCGUCGCG-3, hairpin structure) designed to mimic the adenine loop in domain V of Bacillus subtilis 23S rRNA (residues 20732090 and 26382651)
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2 S-adenosyl-L-methionine + adenine2085 in 23S rRNA
2 S-adenosyl-L-homocysteine + N6-dimethyladenine2085 in 23S rRNA
the specificity of methylation on adenine2085 is confirmed by site-directed mutagenesis. All three mutated domain V fragments, A2085T, A2085G, and A2085C, are methylated to less than 10% of the level observed with the correct domain V RNA fragment. The G2084A change reduces the methylation of the resultant domain V fragment to ca. 12% of the level of the wild-type domain V fragment
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2 S-adenosyl-L-methionine + adenine2085 in 23S rRNA
2 S-adenosyl-L-homocysteine + N6-dimethyladenine2085 in 23S rRNA
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2 S-adenosyl-L-methionine + adenine2085 in 23S rRNA
2 S-adenosyl-L-homocysteine + N6-dimethyladenine2085 in 23S rRNA
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2 S-adenosyl-L-methionine + adenine2085 in 23S rRNA
2 S-adenosyl-L-homocysteine + N6-dimethyladenine2085 in 23S rRNA
ermC methyltransferase produces both N6-mono and N6,N6-dimethylated adenine residues in Bacillus subtilis 23 S rRNA during the course of the reaction in vitro. The addition of the two methyl groups to each 23 S rRNA molecule takes place through a monomethylated intermediate and suggest that the enzyme dissociates from its RNA substrate between the two consecutive methylation reactions. The enzyme is able to utilize monomethylated RNA as substrate for the addition of a second methyl group with an efficiency approximately comparable to that obtained when unmethylated RNA is the initial substrate
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additional information
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direct autoregulatory mechanism operating at the posttranscriptional level and independently of the ermC methylase-mediated methylation of ribosomes. A translational repression model is suggested in which the ermC methyltransferase binds to its own mRNA, at a region that resembles the methylation target site on 23S rRNA
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additional information
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direct autoregulatory mechanism operating at the posttranscriptional level and independently of the ermC methylase-mediated methylation of ribosomes. A translational repression model is suggested in which the ermC methyltransferase binds to its own mRNA, at a region that resembles the methylation target site on 23S rRNA
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