Enzymes Involved in the Metabolism of Plant Allelochemicals

Ahmad, Sami; Brattsten, L. B.; Mullin, Christopher A.; Yu, Simon J.

doi:10.1007/978-1-4613-1865-1_3

Cited by 88 publications

(60 citation statements)

References 306 publications

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“…Host-plant adaptation also can be viewed in terms of physiological, biochemical, and evolutionary adaptations to host-plant allelochemicals (Caprio & Tabashnik 1992;Ahmad et al 1986;Slansky 1992;Sorensen & Dearing 2006). Several authors report the importance of allelochemicals as deterrents, repellents, and stimulants present in plants (Berenbaum & Neal 1985;Vendramim & Guzzo 2009), which may explain the results of our study and should be considered further in future research.…”

Section: Discussionsupporting

confidence: 53%

Resistance of Some Cultivated Brassicaceae to Infestations by Plutella xylostella (Lepidoptera: Plutellidae)

Sarfraz¹,

Dosdall²,

Keddie³

2007

Journal of Economic Entomology

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Section: Discussionsupporting

confidence: 53%

Resistance of Some Cultivated Brassicaceae to Infestations by Plutella xylostella (Lepidoptera: Plutellidae)

Sarfraz¹,

Dosdall²,

Keddie³

2007

Journal of Economic Entomology

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“…A better understanding of the diversity of insect responses to these allelochemicals in their local ecological context represents a key challenge in developing durable pest control management (Després et al, 2007). Consequently, host-plant adaptation could be viewed in terms of physiological, biochemical, and evolutional adaptation to host-plant allelochemicals (Caprio and Tabashnik, 1992;Ahmad et al, 1986;Slansky, 1992;Sorensen and Dearing, 2006). The adaption mechanisms might include contact and ingestion avoidance of the plant containing the allelochemicals; excretion of the toxic food, sequestration or degradation of the toxins and target site mutation (Gould, 1984;Raffa, 1987;Sorensen and Dearing, 2006;Wouters et al, 2014).…”

Section: Discussionmentioning

confidence: 99%

Biology and nutrition of Spodoptera frugiperda (Lepidoptera: Noctuidae) fed on different food sources

Silva

Bueno

Andrade

et al. 2017

Sci. agric. (Piracicaba, Braz.)

145

102

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We studied Spodoptera frugiperda development using different food sources in the laboratory and field. Newly hatched larvae were fed soybean, cotton, maize, wheat, and oat leaves. An artificial diet was used as the control. Duration of pre-pupal, pupal, and larva-adult period, pupal weight, sex ratio, survival, larva feeding preferences, oviposition preferences, and nutritional quality of different hosts were evaluated. Insects fed on wheat showed the shortest larva-adult period. The insects fed on cotton and soybean had longer larval development cycles and pupae of lower weight. Feeding preference was evident for third instar larvae and did not differ between wheat, oat, maize, and soybean, which were the preferred hosts. Moths oviposited to a greater extent on the upper canopy of wheat than that of other plants in both the no-choice and free-choice tests. Treatments influenced insect growth, food consumption, and digestion when nutritional variables were analyzed. Thus, grasses were better hosts for S. frugiperda development. Cotton was the least preferred food, followed by soybean. The present study can improve our understanding of S. frugiperda in these different crops and help in developing management strategies. Even though S. frugiperda is considered to be polyphagous, this pest is closely associated with grasses (maize, wheat, oat) and has lower potential as a soybean or cotton feeder. Howerver, S. frugiperda food intake regulation appears to be triggered by a complex of different mechanisms. Thus, S. frugiperda can also damage soybean and cotton and adapt to them in the absence of preferred hosts.

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“…Carboxylesterases and cholinesterases aTe inhibited stoichiometrically by organophosphorolls or sulfhydryl reagents without concurrent hydrolysis (Aldridge 1953, Krisch 1971. The arylcsterases are resistant to inhibition by OP and SH compounds (Ahmad et al 1986). Cholinesterase is inhibited by the methylcarbamate, physostigmine (eserine) (Beranek 1974).…”

mentioning

confidence: 99%

Characterization of General Esterases in Workers of the Eastern Subterranean Termite (Isoptera: Rhinotermitidae)

Davis

Kamble

Prabhakaran

1995

Journal of Economic Entomology

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General esterases from eastern subterranean termite, Reticulitcnncs flmJipl'S (Kollar), workers were examined for activity and were characterized by electrophoretic and biochemical methods. Greater acti\~ty was observed toward a-naphthyl substrates when compared \vith p-nitrophenyl substrates. Tbe specific activity of the esterases increased with a corresponding increase in a-naphthyl acetate concentration. Maximal activities were observed \vith a buffer pH of 7.6 and an incubation temperature of 45°C. The calculated MichaelisMenten constant (Kill)was 72.53 J.LMand the Villa'was 33.77 J.LM/minlmgof protein. Nondenaturing polyacrylamide gel electrophoresis revealed the presence of seven esterase bands, which were named EI-E7. Bands EI-E4 (slowest gel mobility) were determined to be choIinesterases based on physostigmine inhibition. The remaining three bands were identificd as carbox)'lesterases based on inhibition by paraoxon. The molecular weights of the seven bands ranged from 71.5 to 97.2 kD.KEY WORDS Retil-1.tlitennesflavipes, esterase, termites SUBTEHHANEANTEHMITES CAUSE considerable damage to structures and wood products. An estimated $1.17 billion was spent in 1982 on termite prevention and control measures in the United States (Granovsky 1983). The eastern subterranean termite, Reticulitennes flavipes (Kollar), is one of the most economically important species in the United States (Mampe 1982). Karnble et al. (1984) estimated that a minimum of $1 million is spent annually in Nebraska as a result of damage caused by Reticulitemu~s spp.Despite the economic importance of subterranean termites, little is known about the metabolic and xenobiotie detoxifying systems of these insects. Esterases are important in the metabolism and physiology of animals and plants (Sivakumaran & Mayo 1991). These enzymes may hydrolyze endogenous substances, assume a part in intermedimy metabolism, or promote xenobiotic detoxification (Shen & Dowd 1991). Esterases are proteins that are defined by their ability to catalyze the hydrolysis of ester bonds within lipophilic compounds (Pantelouris & Amason 1966). They are primarily phase I enzymes which, in the presence of water, cleave the target compound into an alcohol and an acid. The ability of esterases to hydrolyze synthetic amides and esters is well documented (Eto 1974, Dauterman 1976, Junge 1984, Junge & Kless 1984, Wilkinson 1985.The hydrolases include the following esterases: arylesterases (A esterases, EC 3.1.1.2), carboxylesterases (B esterases, EC 3.1.1.1), and cholinesterases (B esterases, EC 3.1.1.8) (Augustinson 19.59, 1961). Carboxylesterases and cholinesterases aTe inhibited stoichiometrically by organophosphorolls or sulfhydryl reagents without concurrent hydrolysis (Aldridge 1953, Krisch 1971. The arylcsterases are resistant to inhibition by OP and SH compounds (Ahmad et al. 1986). Cholinesterase is inhibited by the methylcarbamate, physostigmine (eserine) (Beranek 1974).Because of the importance of esterases in physiology, metabolism, and xenobiotic det...

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Enzymes Involved in the Metabolism of Plant Allelochemicals

Cited by 88 publications

References 306 publications

Resistance of Some Cultivated Brassicaceae to Infestations by Plutella xylostella (Lepidoptera: Plutellidae)

Resistance of Some Cultivated Brassicaceae to Infestations by Plutella xylostella (Lepidoptera: Plutellidae)

Biology and nutrition of Spodoptera frugiperda (Lepidoptera: Noctuidae) fed on different food sources

Characterization of General Esterases in Workers of the Eastern Subterranean Termite (Isoptera: Rhinotermitidae)

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