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 + = 2 S-adenosyl-L-homocysteine +
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
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KM Value
KM Value on EC 2.1.1.184 - 23S rRNA (adenine2085-N6)-dimethyltransferase
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0.0000375
23S rRNA
pH 7.5, 37°C, a 262-nucleotide RNA fragment within domain V of Bacillus subtilis 23S rRNA
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0.00091
262-nucleotide RNA fragment within domain V of Bacillus subtilis 23S rRNA
pH 7.5, 37°C, a 262-nucleotide RNA fragment within domain V of Bacillus subtilis 23S rRNA
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0.0000344
623-nucleotide RNA fragment within domain V of Bacillus subtilis 23S rRNA
pH 7.5, 37°C, a 262-nucleotide RNA fragment within domain V of Bacillus subtilis 23S rRNA
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0.000144
623-nucleotide RNA fragment within domain V of Bacillus subtilis 23S rRNA with mutation A2086T
pH 7.5, 37°C, a 262-nucleotide RNA fragment within domain V of Bacillus subtilis 23S rRNA
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0.00121
adenine2085 in 23S rRNA
pH 7.5, 25°C, mutant enzyme K197A/N200A/E202A/K204A/K205A
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0.0028
S-adenosyl-L-methionine
pH 7.5, 25°C, wild-type enzyme
0.0066
S-adenosyl-L-methionine
pH 7.5, 25°C, mutant enzyme K197A/N200A/E202A/K204A/K205A
additional information
interaction between 23s rRNA and ermC' methyltransferase. Kinetic and thermodynamic parameters of binding are determined
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additional information
additional information
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interaction between 23s rRNA and ermC' methyltransferase. Kinetic and thermodynamic parameters of binding are determined
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