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tetracycline destructase Tet(56)
Overview
| Allele | Database | Papers | Drug Classes | Organisms | Countries | Years | Sequence Accession | Protein Accession |
|---|---|---|---|---|---|---|---|---|
| Tet(56) | Card DatabaseReference Gene CatalogReslit | 4 | TETRACYCLINE, Tetracycline +1 | Legionella longbeachae +2 | - | 2015, 2017 | CP020412.2 |
| ARB93503.1 |
| tet56 | Reslit | 1 | Tetracycline | Legionella longbeachae | - | 2018 | PDB:4a6n | - |
| Tet56 | Reslit | 1 | Tetracycline | Legionella longbeachae | - | 2023 | - | - |
| Tet(56-6) | Reslit | 1 | Tetracycline, Doxycycline | Escherichia coli | - | 2024 | 8TWG|8TWF | - |
| Tet(56-2) | Reslit | 1 | Tetracycline, Doxycycline +1 | Escherichia coli | - | 2024 | 8TWG|8TWF | - |
| Tet(56-3) | Reslit | 1 | Tetracycline, Doxycycline +1 | Escherichia coli | - | 2024 | 8TWG|8TWF | - |
| Tet(56-4) | Reslit | 1 | Tetracycline, Doxycycline | Escherichia coli | - | 2024 | 8TWG|8TWF | - |
| Tet(56-5) | Reslit | 1 | Tetracycline, Doxycycline | Escherichia coli | - | 2024 | 8TWG|8TWF | - |
| Tet(56-7) | Reslit | 1 | Tetracycline, Doxycycline | Escherichia coli | - | 2024 | 8TWG|8TWF | - |
| tet(56) | Card Database | 1 | - | Legionella longbeachae | - | - | CP020412.2 | ARB93503.1 |
The Tetracycline Destructases: A Novel Family of Tetracycline-Inactivating Enzymes.
The Tetracycline Destructases: A Novel Family of Tetracycline-Inactivating Enzymes.
Plasticity, dynamics, and inhibition of emerging tetracycline resistance enzymes.
The study identifies and characterizes several tetracycline destructases, including tet(56), tet(X), tet(50), tet(51), and tet(55), which confer tetracycline resistance through enzymatic inactivation. These enzymes degrade tetracycline, leading to increased minimum inhibitory concentrations (MICs) in E. coli. Additionally, anhydrotetracycline is identified as an inhibitor of these enzymes, restoring tetracycline activity.
Plasticity, dynamics, and inhibition of emerging tetracycline resistance enzymes.
The study identifies and characterizes several tetracycline destructases, including tet(56), tet(X), tet(50), tet(51), and tet(55), which confer tetracycline resistance through enzymatic inactivation. These enzymes degrade tetracycline, leading to increased minimum inhibitory concentrations (MICs) in E. coli. Additionally, anhydrotetracycline is identified as an inhibitor of these enzymes, restoring tetracycline activity.
Tetracycline-Inactivating Enzymes.
The paper reviews the structure, mechanism, and inhibition of tetracycline-destructase enzymes, highlighting their role in enzymatic inactivation of tetracyclines and the identification of new tetracycline destructase genes such as tetX, tetX1, tetX2, tet49, tet50, tet51, tet55, and tet56.
Monooxygenases and Antibiotic Resistance: A Focus on Carbapenems.
This review discusses the role of flavin-dependent monooxygenases (FMOs) and Baeyer-Villiger monooxygenases (BVMOs) in antibiotic resistance, focusing on their mechanisms in modifying antibiotics such as tetracyclines, rifamycins, and sulfonamides. Key genes like TetX, MabTetX, Tet56, RIFMO, SadA, SadB, SulX, and SulR were identified as conferring resistance through enzymatic modifications.
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.
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.
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.
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.
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.
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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