The world's first wiki where authorship really matters (Nature Genetics, 2008). Due credit and reputation for authors. Imagine a global collaborative knowledge base for original thoughts. Search thousands of articles and collaborate with scientists around the globe.

wikigene or wiki gene protein drug chemical gene disease author authorship tracking collaborative publishing evolutionary knowledge reputation system wiki2.0 global collaboration genes proteins drugs chemicals diseases compound
Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 
Gene Review

argI  -  ornithine carbamoyltransferase subunit I

Escherichia coli O157:H7 str. EDL933

 
 
Welcome! If you are familiar with the subject of this article, you can contribute to this open access knowledge base by deleting incorrect information, restructuring or completely rewriting any text. Read more.
 

Disease relevance of argI

  • Pseudomonas aeruginosa has an anabolic and a catabolic ornithine carbamoyltransferase (OTCase) [1].
  • In the anabolic OTCase of Escherichia coli the glutamine residue corresponding to Glu-106 was exchanged for glutamate; however, in this case no CP cooperativity was acquired [1].
  • Metabolic enzymes from psychrophilic bacteria: challenge of adaptation to low temperatures in ornithine carbamoyltransferase from Moritella abyssi [2].
  • A significant difference in the serum level of OCT was observed between chronic hepatitis patients (110.7+/-80 ng/ml) and healthy subjects (34.4+/-20.7 ng/ml) (p<0.0001) [3].
 

High impact information on argI

  • Thus, in catabolic OTCase, sequence features in addition to Glu-106 are important for sigmoidal CP saturation, and such a sequence was identified in the C-terminal part [1].
  • The catabolic OTCase lost most of its homotropic cooperativity and gained anabolic activity when an amino acid residue near the CP binding site, Glu-106, was replaced by alanine or glycine [1].
  • By an in vivo gene fusion technique the 9 C-terminal amino acids of catabolic OTCase were replaced by the homologous 8 amino acids from anabolic OTCase of E. coli; the hybrid enzyme had a markedly reduced homotropic cooperativity [1].
  • Activation by AMP and inhibition by spermidine of this chimaeric OTCase do not affect carbamoylphosphate homotropic co-operativity [4].
  • Allosteric regulation in Pseudomonas aeruginosa catabolic ornithine carbamoyltransferase revisited: association of concerted homotropic cooperative interactions and local heterotropic effects [4].
 

Chemical compound and disease context of argI

  • In Pseudomonas aeruginosa PAO the anabolic ornithine carbamoyltransferase (OTCase, EC 2.1.3.3) is the product of the argF gene and the only arginine biosynthetic enzyme whose synthesis is repressible by arginine [5].
 

Biological context of argI

 

Associations of argI with chemical compounds

  • However, when an arginine auxotroph was cultured in limiting arginine, ornithine carbamoyltransferase (OCT) activities rose by as much as 100-fold [7].
 

Analytical, diagnostic and therapeutic context of argI

  • CONCLUSIONS: Our newly established ELISA for OCT using monoclonal antibodies is sensitive enough for clinical application [3].

References

  1. Converting catabolic ornithine carbamoyltransferase to an anabolic enzyme. Baur, H., Tricot, C., Stalon, V., Haas, D. J. Biol. Chem. (1990) [Pubmed]
  2. Metabolic enzymes from psychrophilic bacteria: challenge of adaptation to low temperatures in ornithine carbamoyltransferase from Moritella abyssi. Xu, Y., Feller, G., Gerday, C., Glansdorff, N. J. Bacteriol. (2003) [Pubmed]
  3. A sensitive ELISA for serum ornithine carbamoyltransferase utilizing the enhancement of immunoreactivity at alkaline pH. Murayama, H., Igarashi, M., Mori, M., Fukuda, Y., Ikemoto, M., Nagata, A. Clin. Chim. Acta (2006) [Pubmed]
  4. Allosteric regulation in Pseudomonas aeruginosa catabolic ornithine carbamoyltransferase revisited: association of concerted homotropic cooperative interactions and local heterotropic effects. Tricot, C., Villeret, V., Sainz, G., Dideberg, O., Stalon, V. J. Mol. Biol. (1998) [Pubmed]
  5. Anabolic ornithine carbamoyltransferase of Pseudomonas aeruginosa: nucleotide sequence and transcriptional control of the argF structural gene. Itoh, Y., Soldati, L., Stalon, V., Falmagne, P., Terawaki, Y., Leisinger, T., Haas, D. J. Bacteriol. (1988) [Pubmed]
  6. Sequence analysis and expression of the arginine-deiminase and carbamate-kinase genes of Pseudomonas aeruginosa. Baur, H., Luethi, E., Stalon, V., Mercenier, A., Haas, D. Eur. J. Biochem. (1989) [Pubmed]
  7. 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]
 
WikiGenes - Universities