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Target intelligence / Profile preview
Bacterial Isoleucyl-tRNA Synthetase (IleRS)
- Target
- IleRS
- Molecular classification
- Enzyme, Aminoacyl-tRNA Synthetase, Class I Aminoacyl-tRNA Synthetase
01
Overview
Bacterial isoleucyl-tRNA synthetase (IleRS) is an essential enzyme responsible for catalyzing the attachment of the amino acid isoleucine to its corresponding tRNA (tRNA^Ile). This reaction is a critical step in protein synthesis, ensuring the genetic code is accurately translated. IleRS employs a double-sieve mechanism to discriminate against similar amino acids, especially valine. Mupirocin specifically inhibits bacterial IleRS, and resistance arises through mutations or acquisition of alternative ileS genes.
- Other names
- Isoleucyl-tRNA SynthetaseileS1ileS2
02
Mechanism of action
Mupirocin inhibits bacterial IleRS by mimicking its natural substrate intermediate, thereby blocking isoleucine binding and tRNA aminoacylation.
03
Biological functions
Aminoacylation of tRNAProtein synthesistRNA chargingProofreadingError correctionTranslation fidelity
04
Disease associations
InfectionAntibiotic resistance
05
Safety considerations
Development of antibiotic resistance through mutations in ileS or acquisition of resistant isoforms (ileS2).Potential for off-target effects, though eukaryotic IleRS versions differ structurally from prokaryotic ones, explaining selective toxicity.
06
Interacting drugs
Mupirocin
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