drosera capillaris/protease

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Discovery of digestive enzymes in carnivorous plants with focus on proteases.

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UNASSIGNED Carnivorous plants have been fascinating researchers with their unique characters and bioinspired applications. These include medicinal trait of some carnivorous plants with potentials for pharmaceutical industry. UNASSIGNED This review will cover recent progress based on current studies

Sequence comparison, molecular modeling, and network analysis predict structural diversity in cysteine proteases from the Cape sundew, Drosera capensis.

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Carnivorous plants represent a so far underexploited reservoir of novel proteases with potentially useful activities. Here we investigate 44 cysteine proteases from the Cape sundew, Drosera capensis, predicted from genomic DNA sequences. D. capensis has a large number of cysteine protease genes;

Novel proteases from the genome of the carnivorous plant Drosera capensis: Structural prediction and comparative analysis.

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In his 1875 monograph on insectivorous plants, Darwin described the feeding reactions of Drosera flypaper traps and predicted that their secretions contained a "ferment" similar to mammalian pepsin, an aspartic protease. Here we report a high-quality draft genome sequence for the cape sundew,

Digestive enzymes in insectivorous plants. 3. Acid proteases in the genus Nepenthes and Drosera peltata.

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Feeding on prey increases photosynthetic efficiency in the carnivorous sundew Drosera capensis.

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BACKROUND AND AIMS: It has been suggested that the rate of net photosynthesis (AN) of carnivorous plants increases in response to prey capture and nutrient uptake; however, data confirming the benefit from carnivory in terms of increased AN are scarce and unclear. The principal aim of our study was

The Droserasin 1 PSI: A Membrane-Interacting Antimicrobial Peptide from the Carnivorous Plant Drosera capensis

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The Droserasins, aspartic proteases from the carnivorous plant Drosera capensis, contain a 100-residue plant-specific insert (PSI) that is post-translationally cleaved and independently acts as an antimicrobial peptide. PSIs are of interest not only for their inhibition of microbial growth,

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