2.1.1.170: 16S rRNA (guanine527-N7)-methyltransferase
This is an abbreviated version!
For detailed information about 16S rRNA (guanine527-N7)-methyltransferase, go to the full flat file.
Word Map on EC 2.1.1.170
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2.1.1.170
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aminoglycoside
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amikacin
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esbls
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carbapenemase
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carbapenem-resistant
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16s-rmtases
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blandm-1
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extended-spectrum
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carbapenemase-producing
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aminoglycoside-resistance
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blaoxa-48
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plazomicin
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coproducing
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rmtases
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kasugamycin
- 2.1.1.170
- aminoglycoside
- amikacin
-
esbls
- carbapenemase
-
carbapenem-resistant
- 16s-rmtases
- blandm-1
-
extended-spectrum
-
carbapenemase-producing
-
aminoglycoside-resistance
-
blaoxa-48
-
plazomicin
-
coproducing
-
rmtases
- kasugamycin
Reaction
Synonyms
16S rRNA methyltransferase, 16S rRNA methyltransferase RsmG, gidB, glucose-inhibited division protein B, ribosomal RNA small subunit methyltransferase G, rsmG, RsmG methyltransferase
ECTree
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Engineering
Engineering on EC 2.1.1.170 - 16S rRNA (guanine527-N7)-methyltransferase
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D56A
site-directed mutagenesis of the catalytic residue, the mutant is streptomycin-resistant and shows reduced activity compared to the wild-type enzyme
D71A
site-directed mutagenesis of the S-adenosyl-L-methionine-binding residue, the mutant is streptomycin-resistant and catalytically inactive
D96A
site-directed mutagenesis of the S-adenosyl-L-methionine-binding residue, the mutant is streptomycin-resistant and catalytically inactive
G73A
site-directed mutagenesis of the S-adenosyl-L-methionine-binding residue, the mutant is streptomycin-sensitive and shows reduced activity compared to the wild-type enzyme
G75A
G77A
site-directed mutagenesis of the S-adenosyl-L-methionine-binding residue, the mutant is streptomycin-resistant and catalytically inactive
H53A
site-directed mutagenesis of the catalytic residue, the mutant is partly streptomycin-resistant and shows reduced activity compared to the wild-type enzyme
K100A/R101A
site-directed mutagenesis of the RNA-binding residues, the mutant is streptomycin-resistant and catalytically inactive
K165A
site-directed mutagenesis of the RNA binding residue, the mutant is streptomycin-sensitive, but shows reduced activity compared to the wild-type enzyme
P79A
site-directed mutagenesis of the S-adenosyl-L-methionine-binding residue, the mutant is streptomycin-resistant and shows reduced activity compared to the wild-type enzyme
R123A
site-directed mutagenesis of the RNA-binding residue, the mutant is streptomycin-sensitive, but shows reduced activity compared to the wild-type enzyme
R139A
site-directed mutagenesis of the catalytic residue, the mutant is streptomycin-resistant and catalytically inactive
R139K
site-directed mutagenesis of the catalytic residue, the mutant is partly streptomycin-resistant and shows reduced activity compared to the wild-type enzyme
R197A
site-directed mutagenesis of the RNA binding residue, the mutant is streptomycin-resistant and shows reduced activity compared to the wild-type enzyme
additional information
site-directed mutagenesis of the S-adenosyl-L-methionine-binding residue, the mutant is streptomycin-resistant and shows reduced activity compared to the wild-type enzyme
G75A
the mutation directly affects the S-adenosyl-L-methionine binding site, presents an almost 4fold loss of affinity and maintains the enzyme active
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mutations within the gene gidB confer low-level streptomycin resistance. gidB mutations emerge spontaneously at a high frequency of 0.000001 and, once emerged, result in vigorous emergence of high-level streptomycin-resistant mutants at a frequency more than 2000 times greater than that seen in wild-type strains
additional information
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mutations within the gene gidB confer low-level streptomycin resistance. gidB mutations emerge spontaneously at a high frequency of 0.000001 and, once emerged, result in vigorous emergence of high-level streptomycin-resistant mutants at a frequency more than 2000 times greater than that seen in wild-type strains
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