Arginine catabolism in the phototrophic bacterium Rhodobacter capsulatus E1F1. Purification and properties of arginase.

The phototrophic bacterium Rhodobacter capsulatus E1F1 grew with L-arginine or L-homoarginine as nitrogen source under light/anaerobiosis. However, when L-arginine was used as the only source of both carbon and nitrogen, the bacterium exhibited weak growth levels and the excess of nitrogen was excreted to the medium as ammonia. By contrast, L-ornithine was used under phototrophic conditions as either nitrogen or carbon source. Other compounds of the arginine catabolic pathways, such as putrescine or proline, also supported phototrophic growth of this bacterium. Under heterotrophic/dark conditions, R. capsulatus always showed a low growth rate with those nitrogen compounds. Cells growing on media containing L-arginine, L-homoarginine or L-ornithine induced an Mn(2+)-dependent arginase activity regardless of the presence of ammonium ions and other readily utilizable nitrogen sources. Arginase activity was strongly inhibited by Zn2+, Cu2+, borate, L-cysteine, L-ornithine and gamma-guanidinobutyrate. Mercurials also inactivated arginase, the activity being partially restored by the presence of thiols. Arginase was purified to electrophoretic homogeneity and found to consist of four identical subunits of 31 kDa. The molecular parameters and kinetic constants of arginase from R. capsulatus E1F1 resembled those previously described for the Saccharomyces cerevisiae enzyme rather than those of bacterial arginases.