A Combined Hydroxylation of 3-Cyanopyridine to 3-Cyano-6-hydroxypyridine and 6-Hydroxynicotinic Acid by Resting Cells ofComamonas testosteroni JA1 Grown on Nicotinic Acid

Yuan, Sheng; Yang, Yao; Sun, Junlin; Liang, Ming; Dai, Yinming; Zhang, X.-N.; Xu, Shang-Cheng

doi:10.1002/elsc.200520063

Cited by 5 publications

(2 citation statements)

References 15 publications

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“…The substrate preference of NDHase from diverse sources also significantly varies. For instance, NDHase from Pseudomonas fluorescens TN5 and Comamonas testosteroni JA1 was both specific to 3-cyanopyridine and nicotinic acid [ 24 , 35 ]. NDHase derived from Comamonas teststeroni JA1 is against hydroxylating pyridine 3-sulfonate.…”

Section: Advances In Catalytic Reactions To Pyridine Substratesmentioning

confidence: 99%

Sources, Components, Structure, Catalytic Mechanism and Applications: a Critical Review on Nicotinate Dehydrogenase

Chen

et al. 2023

J. Microbiol. Biotechnol.

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Plant-derived insecticide-neonicotinoid insecticides (NIs) played a crucial role in the development of agriculture and food industry in recent years. Nevertheless, synthesis of these nitrogen-containing heterocyclic compounds with an effective and greener routing remains challenging especially to the notion raise of “green chemistry” and “atom economy”. While bio-catalyzed methods mediated by nicotinate dehydrogenase (NDHase) then provide an alternative. The current review mainly focuses on the introduction of sources, components, structure, catalytic mechanism and applications of NDHase. Specifically, NDHase is known as nicotinic acid hydroxylase and the sources principally derived from phylum Proteobacteria . In addition, NDHase requires the participation of the electron respiratory chain system on the cell membrane. And the most important components of the electron respiratory chain are hydrogen carrier, which is mainly composed of iron-sulfur proteins (Fe-S), flavin dehydrogenase (FAD), molybdenum binding protein and cytochromes. Heterologous expression studies were hampered by the plasmid and host with high efficiency and currently only Pseudomonas entomophila L48 as well as Comamonas testosterone was successfully utilized for the expression of NDHase. Furthermore, it is speculated that the conjugate and inductive effects of the substituent group at position 3 of the substrate pyridine ring exerts a critical role in the hydroxylation reactions at position 6 concerning about the substrate molecular recognition mechanism. Finally, applications of NDHase are addressed in terms of pesticide industry and wastewater treatment. On conclusion, this critical review would not only deepen our understanding of the theory about NDHase, but also provides the guideline for future investigation of NDHase.

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Section: Advances In Catalytic Reactions To Pyridine Substratesmentioning

confidence: 99%

Sources, Components, Structure, Catalytic Mechanism and Applications: a Critical Review on Nicotinate Dehydrogenase

Chen

et al. 2023

J. Microbiol. Biotechnol.

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“…One unit of NaDH activity was defined as the enzyme amount needed to produce 1 lmol of 6-hydroxynicotinate in 1 min at the test conditions (Lu et al 2005;Yuan et al 2005).…”

Section: Nadh Activity Determinationmentioning

confidence: 99%

Cloning, heterologous expression, and functional characterization of the nicotinate dehydrogenase gene from Pseudomonas putida KT2440

et al. 2009

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6-hydroxynicotinate can be used for the production of drugs, pesticides and intermediate chemicals. Some Pseudomonas species were reported to be able to convert nicotinic acid to 6-hydroxynicotinate by nicotinate dehydrogenase. So far, previous reports on NaDH in Pseudomonas genus were confused and contradictory each other. Recently, Ashraf et al. reported an NaDH gene cloned from Eubacterium barkeri and suggested some deducted NaDH genes from other nine bacteria. But they did not demonstrate the activity of recombinant NaDH and did not mention NaDH gene in Pseudomonas. In this study we cloned the gene of NaDH, ndhSL, from Pseudomonas putida KT2440. NdhSL in P. putida KT2440 is composed of two subunits. The small subunit contains [2Fe2S] iron sulfur domain, while the large subunit contains domains of molybdenum cofactor and cytochrome c. Expression of recombinant ndhSL in P. entomophila L48, which lacks the ability to produce 6-hydroxynicotinate, enabled the resting cell and cell extract of engineering P. entomophila L48 to hydroxylate nicotinate. Gene knockout and recovery studies further confirmed the ndhSL function.

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Enhanced hydroxylation of imidacloprid by Stenotrophomonas maltophilia upon addition of sucrose

Dai

Cui

et al. 2007

Appl Microbiol Biotechnol

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Sucrose's ability to promote the hydroxylation of imidacloprid (IMI) by bacterium Stenotrophomonas maltophilia strain CGMCC 1.1788 was examined. Both growing culture and resting cells could transform IMI into 5-hydroxy IMI. Adding 2% sucrose to the growing culture transformation broth and 5% sucrose to the resting cell transformation broth resulted in biotransformation yields, respectively, 2.5 and 9 times greater than without sucrose. In the growing culture transformation, sucrose increased biomass, which led to enhance hydroxylation of IMI. In the resting cell transformation, sucrose was used not as a carbon source but as an energy source for cofactor regeneration for hydroxylation of IMI. The hydroxylation activity of IMI was promoted eightfold by adding reduced nicotinamide adenine dinucleotide (NADH) to the cell-free extract. The hydroxylation of IMI was significantly inhibited by P450 inhibitor piperonyl butoxide. It seems that the hydroxylation of IMI by S. maltophilia CGMCC 1.1788 might proceed through a system by cooperating with P450 enzyme.

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A Combined Hydroxylation of 3-Cyanopyridine to 3-Cyano-6-hydroxypyridine and 6-Hydroxynicotinic Acid by Resting Cells ofComamonas testosteroni JA1 Grown on Nicotinic Acid

Cited by 5 publications

References 15 publications

Sources, Components, Structure, Catalytic Mechanism and Applications: a Critical Review on Nicotinate Dehydrogenase

Sources, Components, Structure, Catalytic Mechanism and Applications: a Critical Review on Nicotinate Dehydrogenase

Cloning, heterologous expression, and functional characterization of the nicotinate dehydrogenase gene from Pseudomonas putida KT2440

Enhanced hydroxylation of imidacloprid by Stenotrophomonas maltophilia upon addition of sucrose

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