2.1.1.180: 16S rRNA (adenine1408-N1)-methyltransferase
This is an abbreviated version!
For detailed information about 16S rRNA (adenine1408-N1)-methyltransferase, go to the full flat file.
Word Map on EC 2.1.1.180
Reaction
Synonyms
16S rRNA (m1A1408) methyltransferase, 16S rRNA m1A1408 methyltransferase, 16S rRNA:m(1)A1408 methyltransferase, A1408 16S rRNA methyltransferase, KAM, KamB, kanamycin-apramycin resistance methylase, Kmr, m1A1408, Npm, NpmA, plasmid-mediated 16S rRNA methyltransferase A, ShKam
ECTree
2.1.1.180 16S rRNA (adenine1408-N1)-methyltransferaseAdvanced search results
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results (Engineering
Engineering on EC 2.1.1.180 - 16S rRNA (adenine1408-N1)-methyltransferase
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
D21A
-
the mutant shows reduced binding affinity with S-adenosyl-L-methionine compared to the wild type enzyme
E94A
-
the mutant shows reduced binding affinity with S-adenosyl-L-methionine compared to the wild type enzyme
K115A
-
the mutant shows reduced binding affinity with S-adenosyl-L-methionine compared to the wild type enzyme
R43A/R73A
-
the mutant shows reduced binding affinity with S-adenosyl-L-methionine compared to the wild type enzyme
R66A
-
the mutant shows reduced binding affinity with S-adenosyl-L-methionine compared to the wild type enzyme
S201A
-
the mutant shows increased binding affinity with S-adenosyl-L-methionine compared to the wild type enzyme
S202A
-
the mutant shows reduced binding affinity with S-adenosyl-L-methionine compared to the wild type enzyme
W113A
-
the mutant shows reduced binding affinity with S-adenosyl-L-methionine compared to the wild type enzyme
W113F
-
the mutant shows increased binding affinity with S-adenosyl-L-methionine compared to the wild type enzyme
W203A
-
the mutant shows increased binding affinity with S-adenosyl-L-methionine compared to the wild type enzyme
W203F
-
the mutant shows reduced binding affinity with S-adenosyl-L-methionine compared to the wild type enzyme
E184C
introduction of a residue displaying high modification efficiency with other Cys-reactive reagents for fluorescence assays. Mutant binds to 30S and dissociates upon addition of SAM
E188C
introduction of a residue displaying high modification efficiency with other Cys-reactive reagents for fluorescence assays. Mutant binds to 30S but fails to dissociate upon addition of SAM
K131C
introduction of a residue displaying high modification efficiency with other Cys-reactive reagents for fluorescence assays. Mutation blocks 30S-NpmA interaction
S89C
introduction of a residue displaying high modification efficiency with other Cys-reactive reagents for fluorescence assays. Mutant binds to 30S but fails to dissociate upon addition of SAM
W107F
mutant enzyme has a kanamycin MIC indistinguishable from that of wild-type Kmr
D30A
mutant protein is tested for its ability to support bacterial growth in the presence of kanamycin. Proposed function SAM-binding: mutant highly affected
D55A
mutant protein is tested for its ability to support bacterial growth in the presence of kanamycin. Proposed function SAM-binding: mutant highly affected
E88A
mutant protein is tested for its ability to support bacterial growth in the presence of kanamycin. Proposed function RNA/30S binding: mutant moderately affected
K174A
mutant protein is tested for its ability to support bacterial growth in the presence of kanamycin. Proposed function RNA/30S binding: no difference to wild-type
K37A
mutant protein is tested for its ability to support bacterial growth in the presence of kanamycin. Proposed function RNA/30S binding: mutant highly affected
K58A
mutant protein is tested for its ability to support bacterial growth in the presence of kanamycin. Proposed function RNA/30S binding: mutant slightly affected
K63A
mutant protein is tested for its ability to support bacterial growth in the presence of kanamycin. Proposed function RNA/30S binding: mutant slightly affected
K67A
mutant protein is tested for its ability to support bacterial growth in the presence of kanamycin. Proposed function RNA/30S binding: mutant moderately affected
K71A
mutant protein is tested for its ability to support bacterial growth in the presence of kanamycin. Proposed function RNA/30S binding: mutant moderately affected
K74A
mutant protein is tested for its ability to support bacterial growth in the presence of kanamycin. Proposed function RNA/30S binding: mutant moderately affected
N138A
mutant protein is tested for its ability to support bacterial growth in the presence of kanamycin. Proposed function A1408 Positioning/catalysis: mutant highly affected
R179A
mutant protein is tested for its ability to support bacterial growth in the presence of kanamycin. Proposed function RNA/30S binding: mutant moderately affected
R195A
mutant protein is tested for its ability to support bacterial growth in the presence of kanamycin. Proposed function RNA/30S binding: mutant moderately affected
R196A
mutant protein is tested for its ability to support bacterial growth in the presence of kanamycin. Proposed function RNA/30S binding: mutant highly affected
R201A
mutant protein is tested for its ability to support bacterial growth in the presence of kanamycin. Proposed function RNA/30S binding: mutant highly affected
R203A
mutant protein is tested for its ability to support bacterial growth in the presence of kanamycin. Proposed function RNA/30S binding: mutant slightly affected
R60A
mutant protein is tested for its ability to support bacterial growth in the presence of kanamycin. Proposed function RNA/30S binding: mutant slightly affected
R8A
mutant protein is tested for its ability to support bacterial growth in the presence of kanamycin. Proposed function RNA/30S binding: mutant moderately affected
S107A
mutant protein is tested for its ability to support bacterial growth in the presence of kanamycin. Proposed function RNA/30S binding: mutant slightly affected
T191A
mutant protein is tested for its ability to support bacterial growth in the presence of kanamycin. Proposed function SAM-binding: mutant highly affected
W105A
mutant protein is tested for its ability to support bacterial growth in the presence of kanamycin. Proposed function A1408 Positioning/catalysis: mutant highly affected
W105F
mutant protein is tested for its ability to support bacterial growth in the presence of kanamycin. Proposed function A1408 Positioning/catalysis: mutant highly affected
W193A
mutant protein is tested for its ability to support bacterial growth in the presence of kanamycin. Proposed function A1408 Positioning/catalysis: mutant highly affected
W193F
mutant protein is tested for its ability to support bacterial growth in the presence of kanamycin. Proposed function A1408 Positioning/catalysis: mutant highly affected
