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

scientific article published on 11 December 2015

A 2-Hydroxypyridine Catabolism Pathway in Rhodococcus rhodochrous Strain PY11. is …
instance of (P31):
scholarly articleQ13442814

External links are
P356DOI10.1128/AEM.02975-15
P932PMC publication ID4751826
P698PubMed publication ID26655765

P2093author name stringRolandas Meškys
Daiva Tauraitė
Rasa Rutkienė
Justas Vaitekūnas
Renata Gasparavičiūtė
P2860cites workCDD: a Conserved Domain Database for the functional annotation of proteinsQ24610576
Deciphering the genetic determinants for aerobic nicotinic acid degradation: the nic cluster from Pseudomonas putida KT2440Q24644289
Improved tools for biological sequence comparisonQ24652199
A Proton Wire and Water Channel Revealed in the Crystal Structure of Isatin HydrolaseQ27684294
Microbial metabolism of pyridine, quinoline, acridine, and their derivatives under aerobic and anaerobic conditionsQ28379188
Isolation and characterization of a rolling-circle-type plasmid from Rhodococcus erythropolis and application of the plasmid to multiple-recombinant-protein expressionQ28770122
Simultaneous identification of two cyclohexanone oxidation genes from an environmental Brevibacterium isolate using mRNA differential displayQ33602734
Aromatic hydrocarbon dioxygenases in environmental biotechnologyQ33941468
Homologous gene clusters of nicotine catabolism, including a new ω-amidase for α-ketoglutaramate, in species of three genera of Gram-positive bacteriaQ34162199
Plasmids for nicotine-dependent and -independent gene expression in Arthrobacter nicotinovorans and other arthrobacter speciesQ34473571
2-Hydroxypyridine Metabolism and Pigment Formation in Three Arthrobacter SpeciesQ36413907
Laboratory evolution of toluene dioxygenase to accept 4-picoline as a substrateQ39492303
Gene cluster on pAO1 of Arthrobacter nicotinovorans involved in degradation of the plant alkaloid nicotine: cloning, purification, and characterization of 2,6-dihydroxypyridine 3-hydroxylaseQ39504701
Microbial metabolism of the pyridine ring. Metabolism of 2- and 3-hydroxypyridines by the maleamate pathway in Achromobacter sp.Q41873305
Construction of Escherichia coli-Arthrobacter-Rhodococcus shuttle vectors based on a cryptic plasmid from Arthrobacter rhombi and investigation of their application for functional screening.Q42625600
A rapid and effective method of extracting fully intact RNA from thermophilic geobacilli that is suitable for gene expression analysisQ43015380
The structure of nicotine blue from Arthrobacter oxidans.Q44362130
Nocardioform arsenic resistance plasmid characterization and improved Rhodococcus cloning vectors.Q54251256
Microbial metabolism of 2-hydroxypyridineQ67377740
Characterization of a novel cis-benzene dihydrodiol dehydrogenase from Pseudomonas putida ML2Q77838112
P433issue4
P407language of work or nameEnglishQ1860
P921main subjectRhodococcus rhodochrousQ7321109
P304page(s)1264-1273
P577publication date2015-12-11
P1433published inApplied and Environmental MicrobiologyQ4781593
P1476titleA 2-Hydroxypyridine Catabolism Pathway in Rhodococcus rhodochrous Strain PY11.
P478volume82

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cites work (P2860)
Q88228850Catabolism of 2-Hydroxypyridine by Burkholderia sp. Strain MAK1: a 2-Hydroxypyridine 5-Monooxygenase Encoded by hpdABCDE Catalyzes the First Step of Biodegradation
Q92192980Exploration of Nicotine Metabolism in Paenarthrobacter nicotinovorans pAO1 by Microbial Proteomics
Q92500840Identification and Characterization of a Novel pic Gene Cluster Responsible for Picolinic Acid Degradation in Alcaligenes faecalis JQ135
Q38639866Indole Biodegradation in Acinetobacter sp. Strain O153: Genetic and Biochemical Characterization
Q92127032Isolation of a 3-hydroxypyridine degrading bacterium, Agrobacterium sp. DW-1, and its proposed degradation pathway
Q28817255Oxyfunctionalization of pyridine derivatives using whole cells of Burkholderia sp. MAK1
Q58618157Proteomics based analysis of the nicotine catabolism in Paenarthrobacter nicotinovorans pAO1

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