Biosynthesis of Arginine and Polyamines
- Authors: Daniel Charlier1, and Nicolas Glansdorff2
- Editor: Valley Stewart3
VIEW AFFILIATIONS HIDE AFFILIATIONSAffiliations: 1: Erfelijkheidsleer en Microbiologie (MICR), Vrije Universiteit Brussel, Pleinlaan, 2, B-1050 Brussels, Belgium; 2: J. M. Wiame Institute for Microbiological Research, 1, ave E. Gryzon, B1070 Brussels, Belgium; 3: University of California, Davis, Davis, CA
Received 30 March 2004 Accepted 17 June 2004 Published 09 September 2004
- Address correspondence to Daniel Charlier email@example.com and Nicolas Glansdorff firstname.lastname@example.org
Early investigations on arginine biosynthesis brought to light basic features of metabolic regulation. The most significant advances of the last 10 to 15 years concern the arginine repressor, its structure and mode of action in both E. coli and Salmonella typhimurium, the sequence analysis of all arg structural genes in E. coli and Salmonella typhimurium, the resulting evolutionary inferences, and the dual regulation of the carAB operon. This review provides an overall picture of the pathways, their interconnections, the regulatory circuits involved, and the resulting interferences between arginine and polyamine biosynthesis. Carbamoylphosphate is a precursor common to arginine and the pyrimidines. In both Escherichia coli and Salmonella enterica serovar Typhimurium, it is produced by a single synthetase, carbamoylphosphate synthetase (CPSase), with glutamine as the physiological amino group donor. This situation contrasts with the existence of separate enzymes specific for arginine and pyrimidine biosynthesis in Bacillus subtilis and fungi. Polyamine biosynthesis has been particularly well studied in E. coli, and the cognate genes have been identified in the Salmonella genome as well, including those involved in transport functions. The review summarizes what is known about the enzymes involved in the arginine pathway of E. coli and S. enterica serovar Typhimurium; homologous genes were identified in both organisms, except argF (encoding a supplementary OTCase), which is lacking in Salmonella. Several examples of putative enzyme recruitment (homologous enzymes performing analogous functions) are also presented.
Citation: Charlier D, Glansdorff N. 2004. Biosynthesis of Arginine and Polyamines, EcoSal Plus 2004; doi:10.1128/ecosalplus.188.8.131.52