2.1.1.180: 16S rRNA (adenine1408-N1)-methyltransferase
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For detailed information about 16S rRNA (adenine1408-N1)-methyltransferase, go to the full flat file.
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
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General Information
General Information on EC 2.1.1.180 - 16S rRNA (adenine1408-N1)-methyltransferase
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physiological function
microorganisms that produce aminoglycosides have developed a special mechanism of high level resistance by posttranscriptional methylation of 16S rRNA in the aminoglycoside binding site. N1-methylation of A1408 confers resistance to kanamycin, tobramycin, sisomycin and apramycin, but not to gentamycin. The M1A1408 methylation is carried out by methyltransferases from the Kam family
physiological function
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resistance to kanamycin plus apramycin results from conversion of residue adenine1408 to 1-methyladenine
physiological function
the introduction of a recombinant plasmid carrying npmA confers on Escherichia coli consistent resistance to both 4,6-disubstituted 2-deoxystreptamines, such as amikacin and gentamicin, and 4,5-disubstituted 2-deoxystreptamines, including neomycin and ribostamycin. The enzyme provides a panaminoglycoside-resistant nature through interference with the binding of aminoglycosides toward the A site of 16S rRNA through N1-methylation at position A1408
physiological function
expression in Escherichia coli provides high-level resistance to kanamycin and apramycin but not to gentamicin
physiological function
NpmA confers resistance to aminoglycosides. Structure of the bacterial ribosomal decoding A site with an A1408m1A antibiotic-resistance mutation both in the presence and absence of aminoglycosides shows that G418 and paromomycin both possessing a 6'-OH group specifically bind to the mutant A site and disturb its function as a molecular switch in the decoding process. Binding of gentamicin with a 6'-NH3+ group to the mutant A site cannot be observed. Adenine 1408 may change ist conformation during the N1-methylation reaction by NpmA