ArticleApplied and environmental microbiology2016
A 2-Hydroxypyridine Catabolism Pathway in Rhodococcus rhodochrous Strain PY11.
Article in Applied and environmental microbiology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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12 citing papers in PubMed, 27 citations in OpenAlex.
- The Novel Monooxygenase GeneApplied and environmental microbiology · 2022Article
- A complete nicotinate degradation pathway in the microbial eukaryote Aspergillus nidulans.Communications biology · 2022Article
- 3-Hydroxypyridine Dehydrogenase HpdA Is Encoded by a Novel Four-Component Gene Cluster and Catalyzes the First Step of 3-Hydroxypyridine Catabolism in Ensifer adhaerens HP1.Applied and environmental microbiology · 2020Article
- Microbial Degradation of Pyridine: a Complete Pathway inApplied and environmental microbiology · 2020Article
- Biochemical and Genetic Analysis of 4-Hydroxypyridine Catabolism inMicroorganisms · 2020Article
- A soil bacterial catabolic pathway on the move: Transfer of nicotine catabolic genes betweenJournal of biosciences · 2020Article
- Identification and Characterization of a NovelJournal of bacteriology · 2019Article
- Isolation of a 3-hydroxypyridine degrading bacterium, Agrobacterium sp. DW-1, and its proposed degradation pathway.AMB Express · 2019Article
- Proteomics based analysis of the nicotine catabolism in Paenarthrobacter nicotinovorans pAO1.Scientific reports · 2018Article
- Catabolism of 2-Hydroxypyridine by Burkholderia sp. Strain MAK1: a 2-Hydroxypyridine 5-Monooxygenase Encoded byApplied and environmental microbiology · 2018Article
- Indole Biodegradation in Acinetobacter sp. Strain O153: Genetic and Biochemical Characterization.Applied and environmental microbiology · 2017Article
- Oxyfunctionalization of pyridine derivatives using whole cells of Burkholderia sp. MAK1.Scientific reports · 2016Article
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5 authors at 1 institution in 1 country.
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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 α-ketoglutarate.
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