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

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 th...

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Autores principales: Chen, Zhi, Xu, Xiangjing, Ju, Xin, Yan, Lishi, Li, Liangzhi, Yang, Lin
Formato: Online Artículo Texto
Lenguaje:English
Publicado: The Korean Society for Microbiology and Biotechnology 2023
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10331938/
https://www.ncbi.nlm.nih.gov/pubmed/36959213
http://dx.doi.org/10.4014/jmb.2302.02011
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author Chen, Zhi
Xu, Xiangjing
Ju, Xin
Yan, Lishi
Li, Liangzhi
Yang, Lin
author_facet Chen, Zhi
Xu, Xiangjing
Ju, Xin
Yan, Lishi
Li, Liangzhi
Yang, Lin
author_sort Chen, Zhi
collection PubMed
description 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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spelling pubmed-103319382023-07-11 Sources, Components, Structure, Catalytic Mechanism and Applications: a Critical Review on Nicotinate Dehydrogenase Chen, Zhi Xu, Xiangjing Ju, Xin Yan, Lishi Li, Liangzhi Yang, Lin J Microbiol Biotechnol Minireview 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. The Korean Society for Microbiology and Biotechnology 2023-06-28 2023-03-06 /pmc/articles/PMC10331938/ /pubmed/36959213 http://dx.doi.org/10.4014/jmb.2302.02011 Text en Copyright © 2023 by the authors. Licensee KMB https://creativecommons.org/licenses/by/4.0/This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/)
spellingShingle Minireview
Chen, Zhi
Xu, Xiangjing
Ju, Xin
Yan, Lishi
Li, Liangzhi
Yang, Lin
Sources, Components, Structure, Catalytic Mechanism and Applications: a Critical Review on Nicotinate Dehydrogenase
title Sources, Components, Structure, Catalytic Mechanism and Applications: a Critical Review on Nicotinate Dehydrogenase
title_full Sources, Components, Structure, Catalytic Mechanism and Applications: a Critical Review on Nicotinate Dehydrogenase
title_fullStr Sources, Components, Structure, Catalytic Mechanism and Applications: a Critical Review on Nicotinate Dehydrogenase
title_full_unstemmed Sources, Components, Structure, Catalytic Mechanism and Applications: a Critical Review on Nicotinate Dehydrogenase
title_short Sources, Components, Structure, Catalytic Mechanism and Applications: a Critical Review on Nicotinate Dehydrogenase
title_sort sources, components, structure, catalytic mechanism and applications: a critical review on nicotinate dehydrogenase
topic Minireview
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10331938/
https://www.ncbi.nlm.nih.gov/pubmed/36959213
http://dx.doi.org/10.4014/jmb.2302.02011
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