Abstract
A bacterium tentatively classified as Arthrobacter strain Py1 being capable to degrade pyrrole-2-carboxylate as only source of carbon, nitrogen, and energy was isolated from soil. In contrast to many other N-heterocyclic compounds, growth of the isolate on pyrrole-2-carboxylate was not affected by molybdate or its specific inhibitor tungstate, indicating a molybdoenzyme-independent breakdown. The latter was initiated by a hydroxylation reaction catalyzed by a pyrrole-2-carboxylate oxygenase, which also exhibited an NADH-cytochrome c reductase activity. The pyrrole-2-carboxylate oxygenase reaction as examined in cell extracts depended on NADH, FAD, and pyrrole-2-carboxylate; the apparent K m values were 44, 6, and 43 μM, respectively. A degradation pathway for pyrrole-2-carboxylate is proposed which involves 5-hydroxy-pyrrole-2-carboxylate and 2-oxoglutarate.
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Hormann, K., Andreesen, J.R. A flavin-dependent oxygenase reaction initiates the degradation of pyrrole-2-carboxylate in Arthrobacter strain Py1 (DSM 6386). Arch. Microbiol. 157, 43–48 (1991). https://doi.org/10.1007/BF00245333
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DOI: https://doi.org/10.1007/BF00245333