Browse AMR Genes
Explore antimicrobial resistance genes from the literature
Explore antimicrobial resistance genes from the literature
aminoglycoside 3-N-acetyltransferase
Overview
| Protein Change | Nucleotide Change | Mechanism | Organism | Resistance To | Database | Validation Status |
|---|---|---|---|---|---|---|
| - | - | Streptomyces griseus, Streptomyces lividans | - | Reslit | Candidate |
| Allele | Database | Papers | Drug Classes | Organisms | Countries | Years | Sequence Accession | Protein Accession |
|---|---|---|---|---|---|---|---|---|
| AAC(3)-Xa | Card DatabaseReference Gene CatalogReslit | 5 | kanamycin, AMINOGLYCOSIDE +2 | Streptomyces griseus SS-1198 +4 | - | 2000, 2010, 2022 | AB028210.1 | BAA78619.1 |
| aac(3)-X | Reslit | 1 | aminoglycosides | Sphingomonas sp. | Stockholm|Sweden | 2020 | - | - |
| aac(3)-Xa | ResFinder Database | 1 | AMIKACIN, PAROMOMYCIN +5 | Streptomyces griseus | - | - | AB028210 | - |
Identification and characterization of the point mutation which affects the transcription level of the chromosomal 3-N-acetyltransferase gene of Streptomyces griseus SS-1198.
The study identifies a point mutation in the promoter region of the aac(3)-Xa gene in Streptomyces griseus SS-1198, which increases the transcription level of the gene and leads to kanamycin resistance.
Identification and characterization of the point mutation which affects the transcription level of the chromosomal 3-N-acetyltransferase gene of Streptomyces griseus SS-1198.
Identification and characterization of the point mutation which affects the transcription level of the chromosomal 3-N-acetyltransferase gene of Streptomyces griseus SS-1198.
Aminoglycoside modifying enzymes.
The paper discusses various aminoglycoside modifying enzymes, particularly focusing on AAC(6')-Ib, AAC(6')-Ib-cr, and AAC(6')-Ib 11, which confer resistance to aminoglycosides like amikacin and gentamicin, and in some cases, quinolones.
Revealing antimicrobial resistance in stormwater with MinION.
The study identified several AMR genes in stormwater samples from Stockholm, including aac(3)-X, aac(6')-I, aph(3')-I, aph(3')-IIb, bacA, chloramphenicol, rosA, ermO, abeS, major facilitator superfamily transporter, mexE, mexX, ompR, opcM, oprA, oprN, qacG, puromycin, ADP-ribosylating, dfrA12, vanH, vanR, and vanS, which confer resistance to various antibiotics such as aminoglycosides, beta-lactams, chloramphenicol, fosmidomycin, MLS, multidrug, puromycin, rifamycin, trimethoprim, and vancomycin.
Structural and molecular rationale for the diversification of resistance mediated by the Antibiotic_NAT family.
The study identifies and characterizes several aminoglycoside acetyltransferases from environmental and clinical sources, highlighting their broad-spectrum resistance to aminoglycosides, including apramycin. Key findings include the structural and functional analysis of these enzymes, showing their role in conferring resistance and their potential for mobilization to pathogenic bacteria.
No comments yet. Be the first to comment!