Centrifuge prior to opening to pellet contents.
Resuspend in sterile deionized water (0.1–1.0 mg/mL).
ArgS is indispensable for protein synthesis, charging tRNA with arginine—a process critical for:
Ammonia Oxidation: Supporting enzymes involved in converting NH₃ to NO₂⁻ .
Stress Adaptation: Potential coordination with toxin-antitoxin systems under nutrient-limited conditions .
While the full-length ArgS is essential, the recombinant partial form may retain catalytic activity for structural or functional studies, though empirical data on its kinetic properties remain unpublished.
The argS gene in N. europaea is part of a streamlined genome optimized for chemolithoautotrophy, with limited metabolic versatility but specialized transporters for inorganic ions . Its recombinant production enables:
Enzyme Kinetics Studies: Probing substrate specificity and inhibitor interactions.
Structural Biology: Crystallography or cryo-EM to resolve active-site architecture.
Bioremediation: Enhancing arginine availability in bioengineered strains for wastewater treatment.
Synthetic Biology: Modular integration into microbial consortia for nitrogen-cycle modulation.
Functional Validation: The partial enzyme’s activity relative to the native protein requires empirical verification.
Structural Elucidation: Mapping truncated regions to assess functional compromises.
KEGG: neu:NE0364
STRING: 228410.NE0364