Novel degradative pathway of 4-nitrobenzoate in Comamonas acidovorans NBA-10.

Autor: Groenewegen PE; Department of Food Science, Agricultural University, Wageningen, The Netherlands., Breeuwer P, van Helvoort JM, Langenhoff AA, de Vries FP, de Bont JA
Jazyk: angličtina
Zdroj: Journal of general microbiology [J Gen Microbiol] 1992 Aug; Vol. 138 Pt 8, pp. 1599-605.
DOI: 10.1099/00221287-138-8-1599
Abstrakt: A Comamonas acidovorans strain, designated NBA-10, was isolated on 4-nitrobenzoate as sole carbon and energy source. When grown on 4-nitrobenzoate, it was simultaneously adapted to 4-nitrosobenzoate and 4-hydroxylaminobenzoate but not to 4-hydroxybenzoate or 4-aminobenzoate. In cell extracts with NADPH present, 4-nitrobenzoate was degraded to 4-hydroxylaminobenzoate and 3,4-dihydroxybenzoate. Partial purification of the 4-nitrobenzoate reductase revealed that 4-nitrobenzoate is degraded via 4-nitrosobenzoate to 4-hydroxylamino-benzoate. The substrate specificity of the enzyme was narrow and NADPH was 15 times more effective as a cofactor than NADH. The results provide evidence for a novel pathway for aerobic degradation of 4-nitrobenzoate, since neither 4-hydroxybenzoate nor 4-aminobenzoate were involved in the degradative pathway.
Databáze: MEDLINE