Browse AMR Genes
Explore antimicrobial resistance genes from the literature
Explore antimicrobial resistance genes from the literature
aminoglycoside resistance methylase
Overview
| Protein Change | Nucleotide Change | Mechanism | Organism | Resistance To | Database | Validation Status |
|---|---|---|---|---|---|---|
| G135A | - | abrogated Sgm activity | E. coli | aminoglycosides | Reslit | Candidate |
| D156A | - | abrogated Sgm activity | E. coli | aminoglycosides | Reslit | Candidate |
| D182A | - | abrogated Sgm activity | E. coli | aminoglycosides | Reslit | Candidate |
| K199A | - | abolished MT activity | E. coli | aminoglycosides | Reslit | Candidate |
| E205A | - | abolished MT activity | E. coli | aminoglycosides | Reslit | Candidate |
| R236A | - | abolished MT activity | E. coli | aminoglycosides | Reslit | Candidate |
| E267A | - | abolished MT activity | E. coli | aminoglycosides | Reslit | Candidate |
| N179A | - | wild-type phenotype | E. coli | aminoglycosides | Reslit | Candidate |
Cloning and characterization of an aminoglycoside resistance determinant from Micromonospora zionensis.
The sgm gene from Micromonospora zionensis was cloned and characterized as an aminoglycoside resistance determinant, conferring resistance to sisomicin and gentamicin.
Cloning and characterization of an aminoglycoside resistance determinant from Micromonospora zionensis.
Cloning and characterization of an aminoglycoside resistance determinant from Micromonospora zionensis.
Cloning and characterization of an aminoglycoside resistance determinant from Micromonospora zionensis.
Critical residues for cofactor binding and catalytic activity in the aminoglycoside resistance methyltransferase Sgm.
The study identifies critical residues in the aminoglycoside resistance methyltransferase Sgm involved in cofactor binding and catalytic activity, demonstrating their importance in mediating resistance to aminoglycosides.
The aminoglykoside resistance methyltransferase Sgm impedes RsmF methylation at an adjacent rRNA nucleotide in the ribosomal A site.
The study identifies Sgm as an aminoglycoside resistance methyltransferase that methylates G1405 in 16S rRNA, thereby conferring resistance to kanamycin by preventing RsmF methylation at C1407.
Structural basis for the methylation of G1405 in 16S rRNA by aminoglycoside resistance methyltransferase Sgm from an antibiotic producer: a diversity of active sites in m7G methyltransferases.
The study characterizes the aminoglycoside resistance methyltransferase Sgm from Micromonospora zionensis, which confers resistance to gentamicin and sisomicin by methylating G1405 in 16S rRNA.
Structural basis for the methylation of G1405 in 16S rRNA by aminoglycoside resistance methyltransferase Sgm from an antibiotic producer: a diversity of active sites in m7G methyltransferases.
Biological cost of aminoglycoside resistance Arm/Kam 16S rRNA methyltransferases from natural antibiotic producers and clinical pathogens.
The study characterizes the biological cost of 16S rRNA methyltransferases (ArmA, RmtA, RmtB, RmtC, RmtD, Sgm, KamB, and NpmA) in Escherichia coli, demonstrating their role in conferring high-level aminoglycoside resistance and their impact on bacterial fitness, translational fidelity, and stress response.
Biological cost of aminoglycoside resistance Arm/Kam 16S rRNA methyltransferases from natural antibiotic producers and clinical pathogens.
The study characterizes the biological cost of 16S rRNA methyltransferases (ArmA, RmtA, RmtB, RmtC, RmtD, Sgm, KamB, and NpmA) in Escherichia coli, demonstrating their role in conferring high-level aminoglycoside resistance and their impact on bacterial fitness, translational fidelity, and stress response.
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