EC Number   |
General Information |
Reference |
|---|
   2.1.1.180 | physiological function |
expression in Escherichia coli provides high-level resistance to kanamycin and apramycin but not to gentamicin |
755799 |
| 2.1.1.180 | 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 |
703101 |
| 2.1.1.180 | 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 |
757843 |
| 2.1.1.180 | physiological function |
resistance to kanamycin plus apramycin results from conversion of residue adenine1408 to 1-methyladenine |
705105 |
| 2.1.1.180 | 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 |
701725 |
