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Gene Review

argA  -  N-acetylglutamate synthase

Escherichia coli CFT073

 
 
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Disease relevance of argA

 

High impact information on argA

  • L-Arginine repressed the formation of N-acetylglutamate synthase [3].
  • The expression system with fbr argA produced 7- to 35-fold more arginine than a system overexpressing carAB and argI genes on a plasmid in a strain with a wt argA gene on the chromosome [4].
  • Plasmids containing wt or fbr argA were stably maintained under normal growth conditions for at least 18 generations [4].
  • Use of inducible feedback-resistant N-acetylglutamate synthetase (argA) genes for enhanced arginine biosynthesis by genetically engineered Escherichia coli K-12 strains [4].
  • DNA sequencing identified different point mutations in each of the fbr argA mutants, specifically H15Y, Y19C, S54N, R58H, G287S, and Q432R [4].
 

Chemical compound and disease context of argA

  • Analysis of lambda insertions in the fucose utilization region of Escherichia coli K-12: use of lambda fuc and lambda argA transducing bacteriophages to partially order the fucose utilization genes [5].
  • Ornithine biosynthesis is limited due to feedback inhibition by arginine of N-acetylglutamate synthetase (NAGS), the product of the argA gene and the first enzyme in the pathway of arginine biosynthesis in E. coli [4].
 

Biological context of argA

  • A new gene, fdaB, has been mapped by transduction and partial diploid analyses and located adjacent to argA at 59.9 min on the Escherichia coli recalibrated linkage map [6].
  • Based on analysis of luxR-dependent promoters, particularly that of argA, we describe a LuxR binding site, and implicate the coordination of LuxR with ArgR [2].
  • Regulation of argA operon expression in Escherichia coli K-12: cell-free synthesis of beta-galactosidase under argA control [7].
 

Associations of argA with chemical compounds

References

 
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