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A 2-Hydroxypyridine Catabolism Pathway in Rhodococcus rhodochrous Strain PY11.


ABSTRACT: Rhodococcus rhodochrous PY11 (DSM 101666) is able to use 2-hydroxypyridine as a sole source of carbon and energy. By investigating a gene cluster (hpo) from this bacterium, we were able to reconstruct the catabolic pathway of 2-hydroxypyridine degradation. Here, we report that in Rhodococcus rhodochrous PY11, the initial hydroxylation of 2-hydroxypyridine is catalyzed by a four-component dioxygenase (HpoBCDF). A product of the dioxygenase reaction (3,6-dihydroxy-1,2,3,6-tetrahydropyridin-2-one) is further oxidized by HpoE to 2,3,6-trihydroxypyridine, which spontaneously forms a blue pigment. In addition, we show that the subsequent 2,3,6-trihydroxypyridine ring opening is catalyzed by the hypothetical cyclase HpoH. The final products of 2-hydroxypyridine degradation in Rhodococcus rhodochrous PY11 are ammonium ion and ?-ketoglutarate.

SUBMITTER: Vaitekunas J 

PROVIDER: S-EPMC4751826 | biostudies-literature | 2016 Feb

REPOSITORIES: biostudies-literature

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A 2-Hydroxypyridine Catabolism Pathway in Rhodococcus rhodochrous Strain PY11.

Vaitekūnas Justas J   Gasparavičiūtė Renata R   Rutkienė Rasa R   Tauraitė Daiva D   Meškys Rolandas R  

Applied and environmental microbiology 20151211 4


Rhodococcus rhodochrous PY11 (DSM 101666) is able to use 2-hydroxypyridine as a sole source of carbon and energy. By investigating a gene cluster (hpo) from this bacterium, we were able to reconstruct the catabolic pathway of 2-hydroxypyridine degradation. Here, we report that in Rhodococcus rhodochrous PY11, the initial hydroxylation of 2-hydroxypyridine is catalyzed by a four-component dioxygenase (HpoBCDF). A product of the dioxygenase reaction (3,6-dihydroxy-1,2,3,6-tetrahydropyridin-2-one)  ...[more]

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