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Explore antimicrobial resistance genes from the literature
Explore antimicrobial resistance genes from the literature
aspartate decarboxylase
Overview
| Protein Change | Nucleotide Change | Mechanism | Organism | Resistance To | Database | Validation Status |
|---|---|---|---|---|---|---|
| A128S | - | - | Mycobacterium tuberculosis | Pyrazinamide | ResFinder DatabaseReslit | Confirmed |
| K9A | - | decreased enzyme activity, enzymatically inactive | Mycobacterium tuberculosis | Pyrazinamide | Reslit | Candidate |
| K7A | - | partially decreased enzyme activity | Mycobacterium tuberculosis |
Pyrazinamide |
Reslit |
| Candidate |
| L132P | - | decreased enzyme activity | Mycobacterium tuberculosis | Pyrazinamide | Reslit | Candidate |
| H11A | - | decreased enzyme activity, enzymatically inactive | Mycobacterium tuberculosis | Pyrazinamide | Reslit | Candidate |
| T16A | - | partially decreased enzyme activity | Mycobacterium tuberculosis | Pyrazinamide | Reslit | Candidate |
| P134S | - | decreased enzyme activity | Mycobacterium tuberculosis | Pyrazinamide | Reslit | Candidate |
| T16S | - | partially decreased enzyme activity | Mycobacterium tuberculosis | Pyrazinamide | Reslit | Candidate |
| D31E | - | partially decreased enzyme activity | Mycobacterium tuberculosis | Pyrazinamide | Reslit | Candidate |
| E126A | - | decreased enzyme activity | Mycobacterium tuberculosis | Pyrazinamide | Reslit | Candidate |
| H119N | - | decreased enzyme activity | Mycobacterium tuberculosis | Pyrazinamide | Reslit | Candidate |
| I49V | - | - | Mycobacterium tuberculosis | Pyrazinamide | ResFinder DatabaseReslit | Confirmed |
| L136R | - | The mutation in the C-terminal tail of PanD causes POA resistance and prevents drug binding. | Mycobacterium tuberculosis, Mycobacterium bovis | Pyrazinamide | ResFinder DatabaseReslit | Confirmed |
| H21R | - | reduced affinity and residence time of POA | Mycobacterium tuberculosis | Pyrazinamide | ResFinder DatabaseReslit | Confirmed |
| M117I | - | - | Mycobacterium tuberculosis | Pyrazinamide | ResFinder DatabaseReslit | Confirmed |
| V138A | - | - | Mycobacterium tuberculosis | Pyrazinamide | ResFinder DatabaseReslit | Confirmed |
| E130G | - | - | Mycobacterium tuberculosis | Pyrazinamide | ResFinder DatabaseReslit | Confirmed |
| V138G | - | - | Mycobacterium tuberculosis | Pyrazinamide | ResFinder DatabaseReslit | Confirmed |
| V138E | - | - | Mycobacterium tuberculosis | Pyrazinamide | ResFinder DatabaseReslit | Confirmed |
| M117T | - | - | Mycobacterium tuberculosis | Pyrazinamide | Reslit | Candidate |
| E126* | - | - | Mycobacterium tuberculosis | Pyrazinamide | ResFinder Database | Established |
| R145* | - | - | Mycobacterium tuberculosis | Pyrazinamide | Reslit | Candidate |
| K209E | The mutation in the C-terminal tail of PanD causes POA resistance and prevents drug binding. | Mycobacterium bovis, Mycobacterium tuberculosis | Pyrazinamide | Reslit | Candidate |
| - | - | Mycobacterium tuberculosis | Pyrazinamide | ResFinder Database | Established |
Aspartate decarboxylase (PanD) as a new target of pyrazinamide in Mycobacterium tuberculosis.
The study identifies mutations in the panD gene as a novel mechanism of resistance to pyrazinamide (PZA) and its active form, pyrazinoic acid (POA), in Mycobacterium tuberculosis.
Pyrazinamide Resistance Is Caused by Two Distinct Mechanisms: Prevention of Coenzyme A Depletion and Loss of Virulence Factor Synthesis.
The study identifies two distinct mechanisms of pyrazinamide resistance: (1) missense mutations in the aspartate decarboxylase panD, which prevent pyrazinoic acid (POA)-mediated coenzyme A (CoA) depletion, and (2) loss-of-function mutations in the polyketide synthases mas and ppsA-E, which affect the synthesis of the virulence factor phthiocerol dimycocerosate (PDIM).
A Multinational Analysis of Mutations and Heterogeneity in PZase, RpsA, and PanD Associated with Pyrazinamide Resistance in M/XDR Mycobacterium tuberculosis.
Overcoming the Challenges of Pyrazinamide Susceptibility Testing in Clinical Mycobacterium tuberculosis Isolates.
Characterization of Fluoroquinolone-Resistant and Multidrug-Resistant Mycobacterium tuberculosis Isolates Using Whole-Genome Sequencing in Tianjin, China.
The study characterized various AMR genes and mutations in fluoroquinolone-resistant and multidrug-resistant Mycobacterium tuberculosis isolates using whole-genome sequencing, identifying key resistance mechanisms for several antibiotics.
The epidemiology and gene mutation characteristics of pyrazinamide-resistant Mycobacterium tuberculosis clinical isolates in Southern China.
The study identified pncA, rpsA, and panD mutations associated with pyrazinamide resistance in Mycobacterium tuberculosis complex isolates.
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