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Gene Review

argC  -  N-acetyl-gamma-glutamylphosphate reductase...

Escherichia coli str. K-12 substr. MG1655

Synonyms: Arg2, ECK3949, JW3930, argH
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Disease relevance of argC


High impact information on argC

  • Mutations causing semi-constitutive expression of argE improve putative promoter sequences within argC [4].
  • During the 15 min after the arginine down shift, relA+ cells produced a significant burst of argF and argH enzyme synthesis when arginine was added back to the culture, whereas relA cells did not produce this burst of enzyme synthesis [5].
  • L-Arginine (2.5 mM) repressed synthesis by argR+ extracts of argECBH mRNA 2-, to 3-fold, argE enzyme 5- to 8-fold, and argH enzyme 20- to 60-fold [6].
  • Added ppGpp had no important effect upon (i) measurable argE or argH enzyme activity, (ii) total protein synthesis in the cell-free system, or (iii) the rate of decay of hybridizable argECBH mRNA [7].
  • N-Acetyl-gamma-glutamyl-phosphate reductase (AGPR) catalyses the NADPH-dependent reduction of N-acetyl-gamma-glutamyl phosphate to give the N-acetylglutamic semialdehyde [2].

Chemical compound and disease context of argC

  • Enzyme activity and size of the expressed protein in the E. coli auxotroph carrying the recombinant argC gene revealed that the cloned gene indeed codes for N-acetylglutamate 5-semialdehyde dehydrogenase [3].

Biological context of argC


Associations of argC with chemical compounds

  • The argECBH mRNA made under conditions of restricted protein synthesis had reduced ability to function in the formation of the argE and argH enzymes and was found to be predominantly 6 to 8S in sucrose density gradients [6].

Analytical, diagnostic and therapeutic context of argC


  1. Sequences required for regulation of arginine biosynthesis promoters are conserved between Bacillus subtilis and Escherichia coli. Smith, M.C., Czaplewski, L., North, A.K., Baumberg, S., Stockley, P.G. Mol. Microbiol. (1989) [Pubmed]
  2. Expression, purification and preliminary X-ray characterization of N-acetyl-gamma-glutamyl-phosphate reductase from Thermus thermophilus HB8. Goto, M., Agari, Y., Omi, R., Miyahara, I., Hirotsu, K. Acta Crystallogr. D Biol. Crystallogr. (2003) [Pubmed]
  3. Molecular cloning and analysis of the argC gene from Corynebacterium glutamicum. Chun, J.Y., Lee, E.J., Lee, H.S., Cheon, C.I., Min, K.H., Lee, M.S. Biochem. Mol. Biol. Int. (1998) [Pubmed]
  4. The regulatory region of the divergent argECBH operon in Escherichia coli K-12. Piette, J., Cunin, R., Boyen, A., Charlier, D., Crabeel, M., Van Vliet, F., Glansdorff, N., Squires, C., Squires, C.L. Nucleic Acids Res. (1982) [Pubmed]
  5. Expression of arg genes of Escherichia coli during arginine limitation dependent upon stringent control of translation. Williams, M.G., Rogers, P. J. Bacteriol. (1987) [Pubmed]
  6. Regulation and coupling of argECBH mRNA and enzyme synthesis in cell extracts of Escherichia coli. Zidwick, M.J., Keller, G., Rogers, P. J. Bacteriol. (1984) [Pubmed]
  7. Positive control of expression of the argECBH gene cluster in vitro by guanosine 5'-diphosphate 3'-diphosphate. Zidwick, M.J., Korshus, J., Rogers, P. J. Bacteriol. (1984) [Pubmed]
  8. Implication of a repression system, homologous to those of other bacteria, in the control of arginine biosynthesis genes in Streptomyces coelicolor. Soutar, A., Baumberg, S. Mol. Gen. Genet. (1996) [Pubmed]
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