Enzymatic characterization of recombinant α-amylase in the &lt;i&gt;Drosophila melanogaster&lt;/i&gt; species subgroup: is there an effect of specialization on digestive enzyme?

Commin, Céline; Aumont-Niçaise, Magali; Claisse, Gaëlle; Feller, Georges; Lage, Jean-Luc Da

doi:10.1266/ggs.88.251

Cited by 10 publications

(17 citation statements)

References 52 publications

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“…9,[16][17][18][19][20][21][22][23] Also, attempts were made to link some characteristics of amylases to the natural diets of their producers, eg, electric charge, 24 or catalytic activity. 25,26…”

Section: International Journal Of Insect Sciencementioning

confidence: 99%

“…For instance, optimum temperature for amylases of D melanogaster, D sechellia, and D erecta was estimated 37°C on raw extracts, 26 but rather 57°C to 60°C using purified enzymes produced in vitro. 25,120…”

Section: Da Lagementioning

confidence: 99%

“…However, model insects like drosophilids were intensively investigated as well. Using purified recombinant amylases, Commin et al 25 attempted to evidence enzymological differences between amylases of the generalist D melanogaster and two specialists, D sechellia and D erecta . But more general and accurate comparisons between the specific activities ( k cat ) of insect amylases from species differing in their diet are still wanting.…”

Section: Sequence and Enzymatic Characterization Of Insect Amylasesmentioning

confidence: 99%

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The Amylases of Insects

Lage

2018

Int J�Insect�Sci

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Alpha-amylases are major digestive enzymes that act in the first step of maltopolysaccharide digestion. In insects, these enzymes have long been studied for applied as well as purely scientific purposes. In many species, amylases are produced by multiple gene copies. Rare species are devoid of Amy gene. They are predominantly secreted in the midgut but salivary expression is also frequent, with extraoral activity. Enzymological parameters are quite variable among insects, with visible trends according to phylogeny: Coleopteran amylases have acidic optimum activity, whereas dipteran amylases have neutral preference and lepidopteran ones have clear alkaline preference. The enzyme structure shows interesting variations shaped by evolutionary convergences, such as the recurrent loss of a loop involved in substrate handling. Many works have focused on the action of plant amylase inhibitors on pest insect amylases, in the frame of crop protection by transgenesis. It appears that sensitivity or resistance to inhibitors is finely tuned and very specific and that amylases and their inhibitors have coevolved. The multicopy feature of insect amylases appears to allow tissue-specific or stage-specific regulation, but also to broaden enzymological abilities, such as pH range, and to overcome plant inhibitory defenses.

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Section: International Journal Of Insect Sciencementioning

confidence: 99%

Section: Da Lagementioning

confidence: 99%

Section: Sequence and Enzymatic Characterization Of Insect Amylasesmentioning

confidence: 99%

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The Amylases of Insects

Lage

2018

Int J�Insect�Sci

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“…A-amylases from A. oryzae and porcine pancreas were obtained from Sigma No A9857 and A3176, respectively. The α-amylase from Drosophila melanogaster was produced in the yeast Pichia pastoris (Guillierm) Phaff, as described in Commin et al (2013). The α-amylase of C. suppressalis was also produced in P. pastoris : the coding sequence of the C. suppressalis amylase gene 108827 was synthetized (Eurofins MWG), with replacement of the signal peptide by the one of D. melanogaster amylase (suppl.…”

Section: Methodsmentioning

confidence: 99%

The use of salivary α-amylase as an evolutionary solution to host selection in parasitoids

Bichang'a

Mailhan³

et al. 2017

Preprint

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Foraging parasitoids use chemical signals in host recognition and selection processes. Thereby, chemicals from the herbivore hosts play a crucial role. When different herbivores are present in the same plant or field, the perception of specific volatiles and contact compounds emitted from the host itself enable the parasitoids both to differentiate between hosts and non-hosts and to estimate the health status of its host. During the host feeding process, contact between the parasitoid and its host is very crucial, and oral secretions from the host play a key role during the first contact for such evaluation by the parasitoid. Using an integration of behavioral observations, biochemical and sensory physiological approaches we demonstrate that female parasitoids of Cotesia flavipes recognize their host and oviposit in reaction to an α-amylase, which is present in the oral secretions of the larvae of their host, Chilo partellus. This activity was also mediated by a purified α-amylase synthetized from Drosophila melanogaster. Using this synthetized enzyme, we further demonstrate that the conformation of the enzyme rather than its catalytic site is responsible for this activity. This enzyme is activating gustatory neurons of the terminal antennal sensilla chaetica of C. flavipes females. α-amylases are therefore good candidates for an evolutionary solution to host selection in parasitoids, thus opening new avenues for investigations in hosts-parasitoids interactions.

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“…Alternatively, single-injection assays can be performed with enzyme in the syringe. This variation is preferable for substrates that are poorly soluble, or those that form suspensions rather than solutions, since they can remain at working (diluted) concentration in the sample cell with constant stirring throughout the experiment (Lonhienne et al, 2001;Ali et al, 2013a,b;Commin et al, 2013;Pedroso et al, 2014;Lehoczki et al, 2016;Kaeswurm et al, 2019). Similarly, if very high substrate concentrations (100 s of mM) are needed (e.g., for enzymes with very large K m values), it can be unfeasible to inject sufficient amounts of substrate without generating large injection heat artifacts, related to the large dilutions.…”

Section: Single Injection Assaysmentioning

confidence: 99%

Enzyme Kinetics by Isothermal Titration Calorimetry: Allostery, Inhibition, and Dynamics

Wang

Moitessier

et al. 2020

Front. Mol. Biosci.

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Isothermal titration calorimetry (ITC) involves accurately measuring the heat that is released or absorbed in real time when one solution is titrated into another. This technique is usually used to measure the thermodynamics of binding reactions. However, there is mounting interest in using it to measure reaction kinetics, particularly enzymatic catalysis. This application of ITC has been steadily growing for the past two decades, and the method is proving to be sensitive, generally applicable, and capable of providing information on enzyme activity that is difficult to obtain using traditional biochemical assays. This review aims to give a broad overview of the use of ITC to measure enzyme kinetics. It describes several different classes of ITC experiment, their strengths and weaknesses, and recent methodological advancements. A summary of applications in the literature is given and several examples where ITC has been used to investigate challenging aspects of enzyme behavior are presented in more detail. These include examples of allostery, where small-molecule binding outside the active site modulates activity. We describe the use of ITC to measure the strength, mode (i.e., competitive, uncompetitive, or mixed), and association and dissociation kinetics of enzyme inhibitors. Further, we provide examples of ITC applied to complex, heterogeneous mixtures, such as insoluble substrates and live cells. These studies exemplify the wide range of problems where ITC can provide answers, and illustrate the versatility of the technique and potential for future development and applications.

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Enzymatic characterization of recombinant α-amylase in the <i>Drosophila melanogaster</i> species subgroup: is there an effect of specialization on digestive enzyme?

Cited by 10 publications

References 52 publications

The Amylases of Insects

The Amylases of Insects

The use of salivary α-amylase as an evolutionary solution to host selection in parasitoids

Enzyme Kinetics by Isothermal Titration Calorimetry: Allostery, Inhibition, and Dynamics

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