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Explore antimicrobial resistance genes from the literature
Explore antimicrobial resistance genes from the literature
tetracycline-inactivating enzyme
Overview
| Allele | Database | Papers | Drug Classes | Organisms | Countries | Years | Sequence Accession | Protein Accession |
|---|---|---|---|---|---|---|---|---|
| tet(X7) | Reslit | 4 | tigecycline, tetracycline +1 | Escherichia coli +2 | Peru|Pakistan, Egypt, China | 2020, 2021, 2024 | MN990692|CP079805 | - |
| Tet(X7) | Reslit | 1 | tetracycline | Escherichia coli | - | 2023 | - | - |
Tetracycline-inactivating enzymes from environmental, human commensal, and pathogenic bacteria cause broad-spectrum tetracycline resistance.
The study identifies and characterizes the tetracycline-inactivating enzyme Tet(X7), which confers resistance to multiple tetracycline antibiotics, including tigecycline, eravacycline, and omadacycline. Tet(X7) was found in a clinical Pseudomonas aeruginosa isolate and shows enhanced catalytic efficiency compared to other tetracycline-inactivating enzymes.
Coproduction of Tet(X7) Conferring High-Level Tigecycline Resistance, Fosfomycin FosA4, and Colistin Mcr-1.1 in Escherichia coli Strains from Chickens in Egypt.
The study identifies the coproduction of Tet(X7), FosA4, and Mcr-1.1 in E. coli strains from chickens in Egypt, highlighting the emergence of multidrug-resistant bacteria with resistance to tigecycline, fosfomycin, and colistin.
Evolutionary Trajectory of the Tet(X) Family: Critical Residue Changes towards High-Level Tigecycline Resistance.
The study identifies five key residue changes (L282S, A339T, D340N, V350I, and K351E) in Tet(X2) that enhance tigecycline resistance, demonstrating their critical role in the molecular evolution of Tet(X) towards high-level resistance.
Structure-Based Design of Bisubstrate Tetracycline Destructase Inhibitors That Block Flavin Redox Cycling.
The study identifies and characterizes novel bisubstrate inhibitors of tetracycline destructases (TDases), which are responsible for enzymatic inactivation of tetracycline antibiotics. These inhibitors effectively block the redox cycling of FAD, thereby preventing the inactivation of tetracyclines by TDases.
Sequence-structure-function characterization of the emerging tetracycline destructase family of antibiotic resistance enzymes.
The study identified 14 new tetracycline destructases (TDases) through HMM screening and functional validation, expanding the diversity of TDase sequences and providing insights into their sequence-structure-function relationships.
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