The pathway of oxidation of picolinamide (pyridine-2-carboxamide) by a Gram-negative rod has been elucidated. Under conditions of high pH, restricted aeration and high substrate concentration, whole cells released 2,5-dihydroxypyridine into culture supernatants. Sodium arsenite at 5mm caused whole cells to accumulate 6-hydroxypicolinate, and, at 1mm, pyruvate, in culture media. Whole cells oxidized picolinamide, picolinate, 6-hydroxypicolinate, maleamate and maleate without lag. Cell-free extracts converted picolinamide into picolinate, and hydroxylated picolinate to 6-hydroxypicolinate. The hydroxylase was particulate, but could be solubilized by ultrasonic treatment; it required NAD+ for activity, and did not require molecular oxygen. 2,5-Dihydroxypyridine was converted into maleamate and formate by an oxygenase requiring GSH and Fe2+. Maleamate was deamidated to maleate, and maleate isomerized to fumarate, by unsupplemented extracts.
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Research Article| May 01 1972
The bacterial oxidation of picolinamide, a photolytic product of Diquat
C. G. Orpin ;
M. Knight ;
Biochem J (1972) 127 (5): 819–831.
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C. G. Orpin, M. Knight, W. C. Evans; The bacterial oxidation of picolinamide, a photolytic product of Diquat. Biochem J 1 May 1972; 127 (5): 819–831. doi: https://doi.org/10.1042/bj1270819
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