ArticleThe Journal of biological chemistry2016
Enzymatic and Structural Characterization of the Major Endopeptidase in the Venus Flytrap Digestion Fluid.
Article in The Journal of biological chemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 22 citations in OpenAlex.
- Jasmonate signaling and prey nutrient availability trigger distinct biochemical responses in the Drosera capensis feeding cycle.Plant physiology · 2026Article
- Expression and function of an S1-type nuclease in the digestive fluid of a sundew, Drosera adelae.Annals of botany · 2023Article
- The Droserasin 1 PSI: A Membrane-Interacting Antimicrobial Peptide from the Carnivorous PlantBiomolecules · 2020Article
- Anaesthesia with diethyl ether impairs jasmonate signalling in the carnivorous plant Venus flytrap (Dionaea muscipula).Annals of botany · 2020Article
- A Commensal Dipeptidyl Aminopeptidase with Specificity for N-Terminal Glycine Degrades Human-Produced Antimicrobial Peptides in Vitro.ACS chemical biology · 2018Article
- Article
- Long-read sequencing uncovers the adaptive topography of a carnivorous plant genome.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Structure prediction and network analysis of chitinases from the Cape sundew, Drosera capensis.Biochimica et biophysica acta. General subjects · 2017Article
- Novel proteases from the genome of the carnivorous plant Drosera capensis: Structural prediction and comparative analysis.Proteins · 2016Article
- Sequence comparison, molecular modeling, and network analysis predict structural diversity in cysteine proteases from the Cape sundew, Drosera capensis.Computational and structural biotechnology journal · 2016Article
- The Computer-Assisted Sequence Annotation (CASA) workflow for enzyme discovery.Applications in plant sciencesArticle
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Authors and funding
13 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Carnivorous plants primarily use aspartic proteases during digestion of captured prey. In contrast, the major endopeptidases in the digestive fluid of the Venus flytrap (Dionaea muscipula) are cysteine proteases (dionain-1 to -4). Here, we present the crystal structure of mature dionain-1 in covalent complex with inhibitor E-64 at 1.5 Å resolution. The enzyme exhibits an overall protein fold reminiscent of other plant cysteine proteases. The inactive glycosylated pro-form undergoes autoprocessing and self-activation, optimally at the physiologically relevant pH value of 3.6, at which the protective effect of the pro-domain is lost. The mature enzyme was able to efficiently degrade a Drosophila fly protein extract at pH 4 showing high activity against the abundant Lys- and Arg-rich protein, myosin. The substrate specificity of dionain-1 was largely similar to that of papain with a preference for hydrophobic and aliphatic residues in subsite S2 and for positively charged residues in S1. A tentative structure of the pro-domain was obtained by homology modeling and suggested that a pro-peptide Lys residue intrudes into the S2 pocket, which is more spacious than in papain. This study provides the first analysis of a cysteine protease from the digestive fluid of a carnivorous plant and confirms the close relationship between carnivorous action and plant defense mechanisms.
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