Biotransformation of insecticide flonicamid by
            <i>Aminobacter</i>
            sp. CGMCC 1.17253 via nitrile hydratase catalysed hydration pathway

Yang, Wenlong; Dai, Zhi-Ling; Cheng, Xi; Fan, Zhixia; Jiang, Huoyong; Dai, Yinming

doi:10.1111/jam.14880

Cited by 8 publications

(2 citation statements)

References 31 publications

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“…According to our earlier research, the N 2 -fixing bacteria Variovorax boronicumulans CGMCC 4969, Microvirga flocculans CGMCC 1.16731, Aminobacter sp. CGMCC 1.17253, Ensifer meliloti CGMCC 7333, and E. adhaerens CGMCC 6315 efficiently convert FLO to TFNG-AM using NHases [ 16 , 17 , 18 , 19 , 20 ]. V. boronicumulans CGMCC 4969 and M. flocculans CGMCC 1.16731 hydrolyze TFNG-AM to TFNG using amidases but do not hydrolyze TFNA-AM, another intermediate of FLO.…”

Section: Introductionmentioning

confidence: 99%

Efficient Biodegradation of the Neonicotinoid Insecticide Flonicamid by Pseudaminobacter salicylatoxidans CGMCC 1.17248: Kinetics, Pathways, and Enzyme Properties

Zhao,

Yuan,

Song

et al. 2024

Microorganisms

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Nitrile-containing insecticides can be converted into their amide derivatives by Pseudaminobacter salicylatoxidans. N-(4-trifluoromethylnicotinoyl) glycinamide (TFNG-AM) is converted to 4-(trifluoromethyl) nicotinoyl glycine (TFNG) using nitrile hydratase/amidase. However, the amidase that catalyzes this bioconversion has not yet been fully elucidated. In this study, it was discovered that flonicamid (FLO) is degraded by P. salicylatoxidans into the acid metabolite TFNG via the intermediate TFNG-AM. A half-life of 18.7 h was observed for P. salicylatoxidans resting cells, which transformed 82.8% of the available FLO in 48 h. The resulting amide metabolite, TFNG-AM, was almost all converted to TFNG within 19 d. A novel amidase-encoding gene was cloned and overexpressed in Escherichia coli. The enzyme, PmsiA, hydrolyzed TFNG-AM to TFNG. Despite being categorized as a member of the amidase signature enzyme superfamily, PsmiA only shares 20–30% identity with the 14 previously identified members of this family, indicating that PsmiA represents a novel class of enzyme. Homology structural modeling and molecular docking analyses suggested that key residues Glu247 and Met242 may significantly impact the catalytic activity of PsmiA. This study contributes to our understanding of the biodegradation process of nitrile-containing insecticides and the relationship between the structure and function of metabolic enzymes.

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Section: Introductionmentioning

confidence: 99%

Efficient Biodegradation of the Neonicotinoid Insecticide Flonicamid by Pseudaminobacter salicylatoxidans CGMCC 1.17248: Kinetics, Pathways, and Enzyme Properties

Zhao,

Yuan,

Song

et al. 2024

Microorganisms

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“…Previously, Aminobacter sp. CGMCC 1.17253 (Yang et al, 2021a), Ensifer meliloti CGMCC 7333 (Yang et al, 2021b), Ensifer adhaerens CGMCC 6315 (Zhao et al, 2021b), and Microvirga flocculans CGMCC 1.16731(Zhao et al, 2020; Zhao et al, 2021a) have been reported to degrade FLO via NHase/amidase pathway. Nevertheless, FLO degradation by nitrilase (EC 3.5.5.1) has been poorly understood.…”

Section: Introductionmentioning

confidence: 99%

Characterization of nitrilases from Variovorax boronicumulans that functions in insecticide flonicamid degradation and β-cyano-L-alanine detoxification

Jiang

Wang

et al. 2022

Journal of Applied Microbiology

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Aims: To characterize the functions of nitrilases of Variovorax boronicumulans CGMCC 4969 and evaluate flonicamid (FLO) degradation and β-cyano-L-alanine (Ala(CN)) detoxification by this bacterium. Methods and Results: Variovorax boronicumulans CGMCC 4969 nitrilases (NitA and NitB) were purified, and substrate specificity assay indicated that both of them degraded insecticide FLO to N-(4-trifluoromethylnicotinoyl)glycinamide (TFNG-AM) and 4-(trifluoromethyl)nicotinol glycine (TFNG). Ala(CN), a plant detoxification intermediate, was hydrolysed by NitB. Escherichia coli overexpressing NitA and NitB degraded 41.2 and 93.8% of FLO (0.87 mmol•L −1 ) within 1 h, with half-lives of 1.30 and 0.25 h, respectively. NitB exhibited the highest nitrilase activity towards FLO. FLO was used as a substrate to compare their enzymatic properties. NitB was more tolerant to acidic conditions and organic solvents than NitA. Conversely, NitA was more tolerant to metal ions than NitB. CGMCC 4969 facilitated FLO degradation in soil and surface water and utilized Ala(CN) as a sole nitrogen source for growth. Conclusions: CGMCC 4969 efficiently degraded FLO mediated by NitA and NitB; NitB was involved in Ala(CN) detoxification. Significance and Impact of the Study: This study promotes our understanding of versatile functions of nitrilases from CGMCC 4969 that is promising for environmental remediation.

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Toxicity of nitriles/amides-based products in the environment and their enzymatic bioremediation

Peter,

Singh,

Yadav

et al. 2024

Journal of Hazardous Materials Advances

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Biotransformation of insecticide flonicamid by Aminobacter sp. CGMCC 1.17253 via nitrile hydratase catalysed hydration pathway

Cited by 8 publications

References 31 publications

Efficient Biodegradation of the Neonicotinoid Insecticide Flonicamid by Pseudaminobacter salicylatoxidans CGMCC 1.17248: Kinetics, Pathways, and Enzyme Properties

Efficient Biodegradation of the Neonicotinoid Insecticide Flonicamid by Pseudaminobacter salicylatoxidans CGMCC 1.17248: Kinetics, Pathways, and Enzyme Properties

Characterization of nitrilases from Variovorax boronicumulans that functions in insecticide flonicamid degradation and β-cyano-L-alanine detoxification

Toxicity of nitriles/amides-based products in the environment and their enzymatic bioremediation

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