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 (Engineering
Engineering on EC 2.1.1.184 - 23S rRNA (adenine2085-N6)-dimethyltransferase
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
E128A
kcat/KM for S-adenosyl-L-methionine is 46% of wild type value. kcat/KM for RNA is 59% of wild type value. No difference in generating erythromycin resistance when compared to the wild-type enzyme
E202A
mutant of a residues positioned on the surface of the small domain, does not display substantial defects in activity compared with the wild-type enzyme. kcat/Km for S-adenosyl-L-methionine is 32% of the wild-type value. kcat/Km for RNA is 40% of wild-type value
F163A
kcat/KM for S-adenosyl-L-methionine is 67% of wild type value. kcat/KM for RNA is 28% of wild type value. Mutant enzyme still mediates erythromycin resistance, although at reduced level
K133A
decreased ability in rendering DH5alpha cells resistant to erythromycin, suggesting that this amino acid is not absolutely indispensable for the ErmC' activity, but might be involved in important RNA-protein interactions. No change in affinity towards the RNA substrate. kcat/Km for S-adenosyl-L-methionine is% of the wild-type value. kcat/Km for RNA is 27% of wild-type value. kcat/Km for S-adenosyl-L-methionine is 13% of the wild-type value. kcat/Km for RNA is% of wild-type value
K166A
kcat/KM for S-adenosyl-L-methionine is 74% of wild type value. kcat/KM for RNA is 58% of wild type value. Little difference in generating erythromycin resistance when compared to the wild-type enzyme
K168A
kcat/KM for S-adenosyl-L-methionine is 59% of wild type value. kcat/KM for RNA is 70% of wild type value. No difference in generating erythromycin resistance when compared to the wild-type enzyme
K197A
mutant of a residues positioned on the surface of the small domain, does not display substantial defects in activity compared with the wild-type enzyme. kcat/Km for S-adenosyl-L-methionine is 67% of the wild-type value. kcat/Km for RNA is 50% of wild-type value
K197A/N200A/E202A/K204A/K205A
the five mutations together do not show a visible cumulative effect on the ErmC' activity in vivo
K204A
mutant of a residues positioned on the surface of the small domain, does not display substantial defects in activity compared with the wild-type enzyme. kcat/Km for S-adenosyl-L-methionine is 73% of the wild-type value. kcat/Km for RNA is 89% of wild-type value
K205A
mutant of a residues positioned on the surface of the small domain, does not display substantial defects in activity compared with the wild-type enzyme. kcat/Km for S-adenosyl-L-methionine is 63% of the wild-type value. kcat/Km for RNA is 92% of wild-type value
K209A
mutant of a residues positioned on the surface of the small domain, does not display substantial defects in activity compared with the wild-type enzyme. kcat/Km for S-adenosyl-L-methionine is 72% of the wild-type value. kcat/Km for RNA is 73% of wild-type value
M196A
mutant of a residues positioned on the surface of the small domain, does not display substantial defects in activity compared with the wild-type enzyme. kcat/Km for S-adenosyl-L-methionine is 42% of the wild-type value. kcat/Km for RNA is 56% of wild-type value
N101A
kcat/KM for S-adenosyl-L-methionine is 10% of wild type value. kcat/KM for RNA is 11% of wild type value. Mutant enzyme is totally unable to render DH5alpha cells resistant to erythromycin
N11A
kcat/KM for S-adenosyl-L-methionine is 32% of wild type value. kcat/KM for RNA is 33% of wild type value. Little difference in generating erythromycin resistance when compared to the wild-type enzyme
N192A
mutant of a residues positioned on the surface of the small domain, does not display substantial defects in activity compared with the wild-type enzyme. kcat/Km for S-adenosyl-L-methionine is 73% of the wild-type value. kcat/Km for RNA is 74% of wild-type value
N200A
mutant of a residues positioned on the surface of the small domain, does not display substantial defects in activity compared with the wild-type enzyme. kcat/Km for S-adenosyl-L-methionine is 42% of the wild-type value. kcat/Km for RNA is 54% of wild-type value
P165A
kcat/KM for S-adenosyl-L-methionine is 4% of wild type value. kcat/KM for RNA is 4% of wild type value. Mutant enzyme still mediates erythromycin resistance, although at reduced level
R112A
decreased ability in rendering DH5alpha cells resistant to erythromycin, suggesting that this amino acid is not absolutely indispensable for the ErmC' activity, but might be involved in important RNA-protein interactions. kcat/Km for S-adenosyl-L-methionine is 12% of the wild-type value. kcat/Km for RNA is 7% of wild-type value
R112D
decreased ability in rendering DH5alpha cells resistant to erythromycin. The R112D mutant shows a more pronounced decrease in RNA-binding affinity compared with R112A. kcat/Km for S-adenosyl-L-methionine is 5% of the wild-type value. kcat/Km for RNA is 2% of wild-type value
R134A
mutant exhibits the most severe effect on the ErmC' ability to generate erythromycin resistance, this mutant has completely lost the activity in vivo. kcat/Km for S-adenosyl-L-methionine is 3% of the wild-type value. kcat/Km for RNA is 1% of wild-type value
R140A
decreased ability in rendering DH5alpha cells resistant to erythromycin, suggesting that this amino acid is not absolutely indispensable for the ErmC' activity, but might be involved in important RNA-protein interactions. kcat/Km for S-adenosyl-L-methionine is 1% of the wild-type value. kcat/Km for RNA is 3% of wild-type value
T108A
decreased ability in rendering DH5alpha cells resistant to erythromycin, suggesting that this amino acid is not absolutely indispensable for the ErmC' activity, but might be involved in important RNA-protein interactions. kcat/Km for S-adenosyl-L-methionine is 4% of the wild-type value. kcat/Km for RNA is 3% of wild-type value
Y104A
mutant enzyme is totally unable to render DH5alpha cells resistant to erythromycin
E128A
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kcat/KM for S-adenosyl-L-methionine is 46% of wild type value. kcat/KM for RNA is 59% of wild type value. No difference in generating erythromycin resistance when compared to the wild-type enzyme
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E202A
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mutant of a residues positioned on the surface of the small domain, does not display substantial defects in activity compared with the wild-type enzyme. kcat/Km for S-adenosyl-L-methionine is 32% of the wild-type value. kcat/Km for RNA is 40% of wild-type value
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K133A
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decreased ability in rendering DH5alpha cells resistant to erythromycin, suggesting that this amino acid is not absolutely indispensable for the ErmC' activity, but might be involved in important RNA-protein interactions. No change in affinity towards the RNA substrate. kcat/Km for S-adenosyl-L-methionine is% of the wild-type value. kcat/Km for RNA is 27% of wild-type value. kcat/Km for S-adenosyl-L-methionine is 13% of the wild-type value. kcat/Km for RNA is% of wild-type value
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K168A
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kcat/KM for S-adenosyl-L-methionine is 59% of wild type value. kcat/KM for RNA is 70% of wild type value. No difference in generating erythromycin resistance when compared to the wild-type enzyme
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K197A
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mutant of a residues positioned on the surface of the small domain, does not display substantial defects in activity compared with the wild-type enzyme. kcat/Km for S-adenosyl-L-methionine is 67% of the wild-type value. kcat/Km for RNA is 50% of wild-type value
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N11A
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kcat/KM for S-adenosyl-L-methionine is 32% of wild type value. kcat/KM for RNA is 33% of wild type value. Little difference in generating erythromycin resistance when compared to the wild-type enzyme
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R112A
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decreased ability in rendering DH5alpha cells resistant to erythromycin, suggesting that this amino acid is not absolutely indispensable for the ErmC' activity, but might be involved in important RNA-protein interactions. kcat/Km for S-adenosyl-L-methionine is 12% of the wild-type value. kcat/Km for RNA is 7% of wild-type value
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Y104A
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mutant enzyme is totally unable to render DH5alpha cells resistant to erythromycin
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additional information
additional information
to validate the structure-based predictions of presumably essential residues in the catalytic pocket of ErmC', site-directed mutagenesis is carried out and the function of the mutants is studied in vitro and in vivo
additional information
With the aim of identification of essential protein-RNA interactions, charged side chains on the predicted target-binding surface of ErmC' are replaced systematically with alanine and the function of the single- and multiple-site mutants is studied in vitro and in vivo. kcat/Km for S-adenosyl-L-methionine is 21% of the wild-type value. kcat/Km for RNA is 17% of wild-type value
additional information
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to validate the structure-based predictions of presumably essential residues in the catalytic pocket of ErmC', site-directed mutagenesis is carried out and the function of the mutants is studied in vitro and in vivo
-
additional information
-
With the aim of identification of essential protein-RNA interactions, charged side chains on the predicted target-binding surface of ErmC' are replaced systematically with alanine and the function of the single- and multiple-site mutants is studied in vitro and in vivo. kcat/Km for S-adenosyl-L-methionine is 21% of the wild-type value. kcat/Km for RNA is 17% of wild-type value
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