Titre
Regulation of enzyme synthesis in the arginine deiminase pathway of Pseudomonas aeruginosa.
Type
article
Institution
Externe
Périodique
Auteur(s)
Mercenier, A.
Auteure/Auteur
Simon, J.P.
Auteure/Auteur
Vander Wauven, C.
Auteure/Auteur
Haas, D.
Auteure/Auteur
Stalon, V.
Auteure/Auteur
Liens vers les personnes
ISSN
0021-9193
Statut éditorial
Publié
Date de publication
1980
Volume
144
Numéro
1
Première page
159
Dernière page/numéro d’article
163
Langue
anglais
Résumé
The three enzymes of the arginine deiminase pathway in Pseudomonas aeruginosa strain PAO were induced strongly (50- to 100-fold) by a shift from aerobic growth conditions to very low oxygen tension. Arginine in the culture medium was not essential for induction, but increased the maximum enzyme levels twofold. The induction of the three enzymes arginine deiminase (EC 3.5.3.6), catabolic ornithine carbamoyltransferase (EC 2.1.3.3), and carbamate kinase (EC 2.7.2.3) appeared to be coordinate. Catabolic ornithine carbamoyltransferase was studied in most detail. Nitrate and nitrite, which can replace oxygen as terminal electron acceptors in P. aeruginosa, partially prevented enzyme induction by low oxygen tension in the wild-type strain, but not in nar (nitrate reductase-negative) mutants. Glucose was found to exert catabolite repression of the deiminase pathway. Generally, conditions of stress, such as depletion of the carbon and energy source or the phosphate source, resulted in induced synthesis of catabolic ornithine carbamoyltransferase. The induction of the deiminase pathway is thought to mobilize intra- and extracellular reserves of arginine, which is used as a source of adenosine 5'-triphosphate in the absence of respiration.
PID Serval
serval:BIB_8E54328692C7
PMID
Date de création
2008-01-25T16:01:19.616Z
Date de création dans IRIS
2025-05-21T00:35:20Z