N 2 -Succinylated intermediates in an arginine catabolic pathway of Pseudomonas aeruginosa
| Autor: | Dieter Haas, Alfred Jann, Thomas Leisinger, Corinne Vander Wauven, Victor Stalon |
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| Rok vydání: | 1986 |
| Předmět: | |
| Zdroj: | Proceedings of the National Academy of Sciences. 83:4937-4941 |
| ISSN: | 1091-6490 0027-8424 |
| DOI: | 10.1073/pnas.83.13.4937 |
| Popis: | Arginine-nonutilizing ( aru ) mutants of Pseudomonas aeruginosa strain PAO converted L-arginine to N 2 -succinylarginine or N -succinylglutamate, which were identified by high-voltage electrophoresis and HPLC. Addition of aminooxyacetate, an inhibitor of pyridoxal phosphate-dependent enzymes, to resting cells of the wild-type PAO1 in arginine medium led to the accumulation of N 2 -succinylornithine. Enzyme assays with crude P. aeruginosa extracts established the following pathway: L-arginine + succinyl-CoA → N 2 -succinylarginine → N 2 -succinylornithine → N _succinylglutamate 5-semialdehyde → N -succinylglutamate → succinate + glutamate. Succinyl-CoA may be regenerated from glutamate via 2-ketoglutarate. L-Arginine induced the enzymes of the pathway, and succinate caused catabolite repression. Purified N 2 -acetylornithine 5-aminotransferase ( N 2 -acetyl-L-ornithine: 2-oxoglutarate aminotransferase, EC 2.6.1.11), an arginine biosynthetic enzyme, efficiently transaminated N 2 -succinylornithine; this explains the enzyme's dual role in arginine biosynthesis and catabolism. The succinylarginine pathway enables P. aeruginosa to utilize arginine efficiently as a carbon source under aerobic conditions, whereas the other three arginine catabolic pathways previously established in P. aeruginosa fulfill different functions. |
| Databáze: | OpenAIRE |
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