Inhibitory specificity and insecticidal selectivity of ?-amylase inhibitor from

Kluh, I.; Horn, Martin; Hýblová, Jana; Hubert, Jan; Dolečková-Marešová, Lucie; Vobůrka, Zdeněk; Kudlı́ková, Iva; Kocourek, F.; Mareš, Michael

doi:10.1016/j.phytochem.2004.11.001

Cited by 50 publications

(57 citation statements)

References 29 publications

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“…ences have been reported in other insect, either toward more acidic (pH 4.5-5 for the weevil Sitophilus oryzae, Kluh et al, 2005) or more basic α-amylases (pH 9.2-10 for the silkworm Bombyx mori or the noctuid Ephestia kuehniella, Pytelkova et al, 2009).…”

Section: Resultsmentioning

confidence: 96%

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

et al. 2013

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We performed a comparative study on the enzymological features of purified recombinant α-amylase of three species belonging to the Drosophila melanogaster species subgroup: D. melanogaster, D. erecta and D. sechellia. D. erecta and D. sechellia are specialist species, with host plant Pandanus candelabrum (Pandanaceae) and Morinda citrifolia (Rubiaceae), respectively. The temperature optima were around 57-60°C for the three species. The pH optima were 7.2 for D. melanogaster, 8.2 for D. erecta and 8.5 for D. sechellia. The k cat and K m were also estimated for each species with different substrates. The specialist species D. erecta and D. sechellia display a higher affinity for starch than D. melanogaster. α-Amylase activity is higher on starch than on glycogen in all species. α-Amylases of D. erecta and D. sechellia have a higher activity on maltooligosaccharides (G6 and G7) than on starch, contrary to D. melanogaster. Such differences in the enzymological features between the species might reflect adaptation to different ecological niches and feeding habits.

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Section: Resultsmentioning

confidence: 96%

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

et al. 2013

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“…In Table 1 inhibitory activity of AIs from different sources are reviewed. -AIs are naturally used by plants as a defense mechanism against insect pests (Ishimoto et al, 1989;Kluh et al, 2005). Moreover, there is a great interest to use -AIs for control of insect pest and also to use them for production of transgenic plants that are resistant against insect pest (Gatehouse et al, 1998;Chrispeels et al, 1998;Gatehouse and Gatehouse, 1998;Valencia et al, 2000;Yamada et al, 2001).…”

Section: Proteinaceous α-Amylase Inhibitors From Plantsmentioning

confidence: 99%

“…The expression of -amylase inhibitors has been showed to be effective in transgenic plants. The expression of the cDNA encoding Al-I into some plants such as pea (Pisum sativum L.) and azuki bean (Vigna anguralis L.) against bruchid beetle pests (Coleoptera: Bruchidae) has been well documented for showing ability of these inhibitors to be used as plant resistance factors against some species of insect pests (Ishimoto et al, 1989;Yamada et al, 2001;Kluh et al, 2005). Pea and azuki transgenic plants expressing α-amylase inhibitors from common beans ( -AI) were completely resistant to the Bruchus pisorum and Callosobruchus chinensis weevils (Morton et al 2000).…”

Section: Proteinaceous α-Amylase Inhibitors From Plantsmentioning

confidence: 99%

“…There have been particular attentions on lectin-like inhibitors and they are toxic against several insect pests (Ishimoto and Kitamura, 1989;Huesing et al, 1991a;Ishimoto and Chrispeels, 1996;Grossi-de-Sa et al, 1997, Kluh et al,., 2005Karbache et al, 2011). AI-1 and AI-2, Two lectin-like inhibitors, were identified in common white, red and black kidney beans (Ishimoto and Chrispeels, 1996;).…”

Section: Lectin-like Inhibitorsmentioning

confidence: 99%

“…AI-1 inhibits mammalian -amylases and several insect amylases, but it is not active against Mexican bean weevil (Zabrotes subfasciatus). On the other hand, AI-2 does not inhibit the -amylases recognized by AI-1 but inhibits the -amylase of Z. subfasciatus (Ishimoto an d Chrispeels, 1996;Kluh et al, 2005).…”

Section: Lectin-like Inhibitorsmentioning

confidence: 99%

See 2 more Smart Citations

Plant Proteinaceous α-Amylase and Proteinase Inhibitors and Their Use in Insect Pest Control

Mehrabadi¹,

Franco²,

Bandani³

2012

New Perspectives in Plant Protection

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The importance of starch and sucrose digestion in nutritive biology of synanthropic acaridid mites: α‐Amylases and α‐glucosidases are suitable targets for inhibitor‐based strategies of mite control

Erban

Erbanova

Nešvorná

et al. 2009

Arch Insect Biochem Physiol

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The adaptation of nine species of mites that infest stored products for starch utilization was tested by (1) enzymatic analysis using feces and whole mite extracts, (2) biotests, and (3) inhibition experiments. Acarus siro, Aleuroglyphus ovatus, and Tyroborus lini were associated with the starch-type substrates and maltose, with higher enzymatic activities observed in whole mite extracts. Lepidoglyphus destructor was associated with the same substrates but had higher activities in feces. Dermatophagoides farinae, Chortoglyphus arcuatus, and Caloglyphus redickorzevi were associated with sucrose. Tyrophagus putrescentiae and Carpoglyphus lactis had low or intermediate enzymatic activity on the tested substrates. Biotests on starch additive diets showed accelerated growth of species associated with the starch-type substrates. The inhibitor acarbose suppressed starch hydrolysis and growth of the mites. We suggest that the species with higher starch hydrolytic activity in feces were more tolerant to acarbose, and alpha-amylase and alpha-glucosidase of synanthropic mites are suitable targets for inhibitor-based strategies of mite control.

show abstract

Inhibitory specificity and insecticidal selectivity of ?-amylase inhibitor from

Cited by 50 publications

References 29 publications

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

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

Plant Proteinaceous α-Amylase and Proteinase Inhibitors and Their Use in Insect Pest Control

The importance of starch and sucrose digestion in nutritive biology of synanthropic acaridid mites: α‐Amylases and α‐glucosidases are suitable targets for inhibitor‐based strategies of mite control

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