ArticleThe FEBS journal2006
Characterization of a membrane-bound aminopeptidase purified from Acyrthosiphon pisum midgut cells. A major binding site for toxic mannose lectins.
Article in The FEBS journal, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 80 citations in OpenAlex.
- Drug targeting of aminopeptidases: importance of deploying a right metal cofactor.Biophysical reviews · 2024Review
- Urbanization-driven environmental shifts cause reduction in aminopeptidase N activity in the honeybee.Conservation physiology · 2024Article
- Streamlined phage display library protocols for identification of insect gut binding peptides highlight peptide specificity.Current research in insect science · 2021Article
- Remusatia vivipara lectin and Sclerotium rolfsii lectin interfere with the development and gall formation activity of Meloidogyne incognita in transgenic tomato.Transgenic research · 2019Article
- Overview of the Structure⁻Function Relationships of Mannose-Specific Lectins from Plants, Algae and Fungi.International journal of molecular sciences · 2019Review
- The Principal Salivary Gland Is the Primary Source of Digestive Enzymes in the Saliva of the Brown Marmorated Stink Bug,Frontiers in physiology · 2019Article
- Distribution of Glycan Motifs at the Surface of Midgut Cells in the Cotton Leafworm (Frontiers in physiology · 2017Article
- Article
- Virulent Diuraphis noxia Aphids Over-Express Calcium Signaling Proteins to Overcome Defenses of Aphid-Resistant Wheat Plants.PloS one · 2016Article
- Functional Evaluation of Proteins in Watery and Gel Saliva of Aphids.Frontiers in plant science · 2016Review
- In Vitro Evidence Supports Membrane Alanyl Aminopeptidase N as a Receptor for a Plant Virus in the Pea Aphid Vector.Journal of virology · 2015Article
- Insecticidal activity of plant lectins and potential application in crop protection.Molecules (Basel, Switzerland) · 2015Review
- Recognition and binding of the PF2 lectin to α-amylase from Zabrotes subfasciatus (Coleoptera:Bruchidae) larval midgut.Journal of insect science (Online) · 2014Article
- How phloem-feeding insects face the challenge of phloem-located defenses.Frontiers in plant science · 2013Review
- Review
- Circulating virus load determines the size of bottlenecks in viral populations progressing within a host.PLoS pathogens · 2012Article
- Article
- A barley cysteine-proteinase inhibitor reduces the performance of two aphid species in artificial diets and transgenic Arabidopsis plants.Transgenic research · 2011Article
- Diversity in protein glycosylation among insect species.PloS one · 2011Article
- Symbiotic bacteria enable insect to use a nutritionally inadequate diet.Proceedings. Biological sciences · 2009Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
A single membrane-bound aminopeptidase N (APN) occurs in the pea aphid (Acyrthosiphon pisum Harris) midgut, with a pH optimum of 7.0, pI of 8.1 and molecular mass of 130 kDa. This enzyme accounts for more than 15.6% of the total gut proteins. After being solubilized in detergent, APN was purified to homogeneity. The enzyme is a glycoprotein rich in mannose residues, which binds the entomotoxic lectins of the concanavalin family. The internal sequence of APN is homologous with a conservative domain in APNs, and degenerated primers of highly conserved APN motifs were used to screen a gut cDNA library. The complete sequence of APN has standard residues involved in zinc co-ordination and catalysis and a glycosyl-phosphatidylinositol anchor, as in APNs from Lepidoptera. APN has a broad specificity towards N-terminal amino acids, but does not hydrolyze acidic aminoacyl-peptides, thus resembling the mammalian enzyme (EC 3.4.11.2). The kcat/Km ratios for different di-, tri-, tetra-, and penta-peptides suggest a preference for tripeptides, and that subsites S1, S2' and S3' are pockets able to bind bulky aminoacyl residues. Bestatin and amastatin bound APN in a rapidly reversible mode, with Ki values of 1.8 microM and 0.6 microM, respectively. EDTA inactivates this APN (k(obs) 0.14 M(-1) x s(-1), reaction order of 0.44) at a rate that is reduced by competitive inhibitors. In addition to oligopeptide digestion, APN is proposed to be associated with amino-acid-absorption processes which, in contrast with aminopeptidase activity, may be hampered on lectin binding.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.