Browse AMR Mutations
Explore antimicrobial resistance mutations from the literature
Explore antimicrobial resistance mutations from the literature
Explore antimicrobial resistance mutations from the literature
| Gene | Protein Change | Nucleotide Change | Mechanism | Organism | Resistance To | Database | Validation Status |
|---|---|---|---|---|---|---|---|
bioC O-methyltransferase | D75A | - | The D75A mutation disrupts SAM binding and reduces enzymatic activity, indicating a critical role in BioC function. | Acinetobacter baumannii, Klebsiella pneumoniae | polymyxins | Reslit | Candidate |
bioC O-methyltransferase | E50A | - | The E50A mutation disrupts SAM binding and reduces enzymatic activity, indicating a critical role in BioC function. | Acinetobacter baumannii, Klebsiella pneumoniae | polymyxins | Reslit | Candidate |
bioC O-methyltransferase | K194A | - | The K194A mutation affects the interaction with the ACP carrier, reducing enzymatic activity. | Acinetobacter baumannii, Klebsiella pneumoniae | polymyxins | Reslit | Candidate |
bioC O-methyltransferase | K201A | - | The K201A mutation affects the interaction with the ACP carrier, reducing enzymatic activity. | Acinetobacter baumannii, Klebsiella pneumoniae | polymyxins | Reslit | Candidate |
bioC O-methyltransferase | K215A | - | The K215A mutation affects the interaction with the ACP carrier, reducing enzymatic activity. | Acinetobacter baumannii, Klebsiella pneumoniae | polymyxins | Reslit | Candidate |
bioC O-methyltransferase | Q116A | - | The Q116A mutation disrupts the neutralization of the malonyl group, affecting substrate binding and enzymatic activity. | Acinetobacter baumannii, Klebsiella pneumoniae | polymyxins | Reslit | Candidate |
bioC O-methyltransferase | Q26A | - | The Q26A mutation disrupts the neutralization of the malonyl group, affecting substrate binding and enzymatic activity. | Acinetobacter baumannii, Klebsiella pneumoniae | polymyxins | Reslit | Candidate |
bioC O-methyltransferase | R212A | - | The R212A mutation affects the interaction with the ACP carrier, reducing enzymatic activity. | Acinetobacter baumannii, Klebsiella pneumoniae | polymyxins | Reslit | Candidate |
bioC O-methyltransferase | W117A | - | The W117A mutation disrupts SAM binding and reduces enzymatic activity, indicating a critical role in BioC function. | Acinetobacter baumannii, Klebsiella pneumoniae | polymyxins | Reslit | Candidate |
bla CMY-16 beta-lactamase | N346H | - | reduced inhibition efficacy of avibactam | Klebsiella pneumoniae | aztreonamavibactam | Reslit | Candidate |
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