par Vander Wauven, Corinne 
;Jann, Alfred;Haas, Didier ;Leisinger, Thomas;Stalon, Victor
Référence Archives of microbiology, 150, 4, page (400-404)
Publication Publié, 1988-08
;Jann, Alfred;Haas, Didier ;Leisinger, Thomas;Stalon, Victor Référence Archives of microbiology, 150, 4, page (400-404)
Publication Publié, 1988-08
Article révisé par les pairs
| Résumé : | Most Pseudomonas aeruginosa PAO mutants which were unable to utilize l-arginine as the sole carbon and nitrogen source (aru mutants) under aerobic conditions were also affected in l-ornithine utilization. These aru mutants were impaired in one or several enzymes involved in the conversion of N2-succinylornithine to glutamate and succinate, indicating that the latter steps of the arginine succinyltransferase pathway can be used for ornithine catabolism. Addition of aminooxyacetate, an inhibitor of the N2-succinylornithine 5-aminotransferase, to resting cells of P. aeruginosa in ornithine medium led to the accumulation of N2-succinylornithine. In crude extracts of P. aeruginosa an ornithine succinyltransferase (l-ornithine:succinyl-CoA N2-succinyltransferase) activity could be detected. An aru mutant having reduced arginine succinyltransferase activity also had correspondingly low levels of ornithine succinyltransferase. Thus, in P. aeruginosa, these two activities might be due to the same enzyme, which initiates aerobic arginine and ornithine catabolism. © 1988 Springer-Verlag. |
