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Link to original content: https://pubmed.ncbi.nlm.nih.gov/16347070
Degradation of Pyridine by Micrococcus luteus Isolated from Soil - PubMed Skip to main page content
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. 1986 May;51(5):963-8.
doi: 10.1128/aem.51.5.963-968.1986.

Degradation of Pyridine by Micrococcus luteus Isolated from Soil

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Degradation of Pyridine by Micrococcus luteus Isolated from Soil

G K Sims et al. Appl Environ Microbiol. 1986 May.

Abstract

An organism capable of growth on pyridine was isolated from soil by enrichment culture techniques and identified as Micrococcus luteus. The organism oxidized pyridine for energy and released N contained in the pyridine ring as ammonium. The organism could not grow on mono- or disubstituted pyridinecarboxylic acids or hydroxy-, chloro-, amino-, or methylpyridines. Cell extracts of M. luteus could not degrade pyridine, 2-, 3-, or 4-hydroxypyridines or 2,3-dihydroxypyridine, regardless of added cofactors or cell particulate fraction. The organism had a NAD-linked succinate-semialdehyde dehydrogenase which was induced by pyridine. Cell extracts of M. luteus had constitutive amidase activity, and washed cells degraded formate and formamide without a lag. These data are consistent with a previously reported pathway for pyridine metabolism by species of Bacillus, Brevibacterium, and Corynebacterium. Cells of M. luteus were permeable to pyridinecarboxylic acids, monohydroxypyridines, 2,3-dihydroxypyridine, and monoamino- and methylpyridines. The results provide new evidence that the metabolism of pyridine by microorganisms does not require initial hydroxylation of the ring and that permeability barriers do not account for the extremely limited range of substrate isomers used by pyridine degraders.

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References

    1. Ecotoxicol Environ Saf. 1983 Jun;7(3):251-75 - PubMed
    1. Arch Mikrobiol. 1963 Dec 10;47:137-53 - PubMed
    1. Biochem J. 1950 Sep;47(3):347-55 - PubMed
    1. Biochem J. 1975 Jan;146(1):157-72 - PubMed
    1. J Biol Chem. 1959 Jan;234(1):5-10 - PubMed

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