2.1.1.179: 16S rRNA (guanine1405-N7)-methyltransferase
This is an abbreviated version!
For detailed information about 16S rRNA (guanine1405-N7)-methyltransferase, go to the full flat file.
Word Map on EC 2.1.1.179
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2.1.1.179
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aminoglycoside
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drug development
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esbls
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micromonospora
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extended-spectrum
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carbapenemases
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aminoglycoside-resistant
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4,6-disubstituted
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carbapenem-resistant
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plazomicin
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methyltranferase
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aac6\'-ib
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worrisome
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carbapenemase-producing
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blakpc-2
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fosfomycin
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blatem-1b
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aminoglycoside-producing
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deoxystreptamine
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tigecycline
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mtases
- 2.1.1.179
- aminoglycoside
- drug development
-
esbls
- micromonospora
-
extended-spectrum
- carbapenemases
-
aminoglycoside-resistant
-
4,6-disubstituted
-
carbapenem-resistant
-
plazomicin
-
methyltranferase
-
aac6\'-ib
-
worrisome
-
carbapenemase-producing
- blakpc-2
- fosfomycin
-
blatem-1b
-
aminoglycoside-producing
-
deoxystreptamine
- tigecycline
- mtases
Reaction
Synonyms
16S rRNA (m7G1405) methyltransferase, 16S rRNA methyltransferase, 16S rRNA N7 G1405 methyltransferase, 16S-RMTase, ArmA, FmrO, G1405 methyltransferase ArmA, GrmA, GrmB, Kmr, Krm, M7G1405 MTase, methyltransferase RmtC, methyltransferase Sgm, N7-G1405 16S-RMTase, NbrB, RmtA, RmtB, RmtC, RmtD, RmtD2, RmtF, RmtG, sgm, Sgm methyltransferase, Sgm MTase, sisomicin-gentamicin methylase, sisomicin-gentamicin methyltransferase, sisomicin-gentamicin resistance methylase, Smr1
ECTree
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Engineering
Engineering on EC 2.1.1.179 - 16S rRNA (guanine1405-N7)-methyltransferase
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H81A
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tobramycin MIC is identical with that of wild-type RmtB. No change in methylation activity compared to wild-type enzyme
K14A
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tobramycin MIC is identical with that of wild-type RmtB. 36% of the methylation activity compared to wild-type enzyme
K174A
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tobramycin MIC is drastically reduced compared to wild-type enzyme. 0.7% of the methylation activity compared to wild-type enzyme
S83A
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tobramycin MIC is identical with that of wild-type RmtB. 18% of the methylation activity compared to wild-type enzyme
D156A
D158A
mutant with drastically increased sensitivity to kanamycin
D182A
E205A
E267A
G135A
K199A
K54A
mutant with drastically increased sensitivity to kanamycin
R108A
mutant with drastically increased sensitivity to kanamycin
R187S
mutant with drastically increased sensitivity to kanamycin
R236A
R433A
mutant with drastically increased sensitivity to kanamycin
H54A
inactive. Mutation dos not impact 30S binding affinity. Mutant strain is sensitive to kanamycin and gentamicin
H54E
inactive. Mutation dos not impact 30S binding affinity. Mutant strain is sensitive to kanamycin and gentamicin
K20E
mutation eliminates 30S binding affinity, mutant strain is sensitive to kanamycin and gentamicin
K72E
mutation reduces 30S binding affinity about 5fold, resistance to kanamycin and gentamcin is reduced
R50E
mutation reduces 30S binding affinity about 11-13fold. Mutant strain is sensitive to kanamycin and gentamicin
R68E
mutation reduces 30S binding affinity about 11-13fold, resistance to kanamycin and gentamcin is reduced
additional information
mutant with drastically increased sensitivity to kanamycin
mutant with drastically increased sensitivity to kanamycin
E205A
mutant with drastically increased sensitivity to kanamycin
E267A
mutant with drastically increased sensitivity to kanamycin
mutant with drastically increased sensitivity to kanamycin
K199A
mutant with drastically increased sensitivity to kanamycin
R236A
mutant with drastically increased sensitivity to kanamycin
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construction of a series of in-frame knockout and knock-in mutants of Escherichia coli, corresponding to the genotypes rsmF+, DELTArsmF, rsmF+ rmtC+, and DELTArsmF rmtC+, mutant strain growth kinetics, overview
additional information
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construction of a series of in-frame knockout and knock-in mutants of Escherichia coli, corresponding to the genotypes rsmF+, DELTArsmF, rsmF+ rmtC+, and DELTArsmF rmtC+, mutant strain growth kinetics, overview
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additional information
analysis of sequencefunction relationships of Sgm MTase by limited proteolysis and site-directed and random mutagenesis
additional information
replacement of the RmtC loop with four Ala residues (Loop237-246 ->A4) ablates the enzyme's ability to confer resistance to kanamycin and gentamicin. Conserved C-terminal domain residues surrounding the SAM-binding pocket are functionally critical but do not contribute to 30S binding affinity