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dc.contributorClack, Beatrice A.en_US
dc.creatorEl Bouhssini, Mustaphaen_US
dc.date2014-10-22en_US
dc.date.accessioned2017-11-29T13:15:36Z
dc.date.available2017-11-29T13:15:36Z
dc.identifierhttps://mel.cgiar.org/reporting/download/hash/Tye7nEi4en_US
dc.identifier.citationMustapha El Bouhssini, Beatrice A. Clack. (22/10/2014). Cloning, Expression, Sequence Analysis and Homology Modeling of the Prolyl Endoprotease from Eurygaster integriceps Puton. Insects, 5, pp. 762-782.en_US
dc.identifier.urihttps://hdl.handle.net/20.500.11766/7549
dc.description.abstractEurygaster integriceps Puton, commonly known as sunn pest, is a major pest of wheat in Northern Africa, the Middle East and Eastern Europe. This insect injects a prolyl endoprotease into the wheat, destroying the gluten. The purpose of this study was to clone the full length cDNA of the sunn pest prolyl endoprotease (spPEP) for expression in E. coli and to compare the amino acid sequence of the enzyme to other known PEPs in both phylogeny and potential tertiary structure. Sequence analysis shows that the 5ꞌ UTR contains several putative transcription factor binding sites for transcription factors known to be expressed in Drosophila that might be useful targets for inhibition of the enzyme. The spPEP was first identified as a prolyl endoprotease by Darkoh et al., 2010. The enzyme is a unique serine protease of the S9A family by way of its substrate recognition of the gluten proteins, which are greater than 30 kD in size. At 51% maximum identity to known PEPs, homology modeling using SWISS-MODEL, the porcine brain PEP (PDB: 2XWD) was selected in the database of known PEP structures, resulting in a predicted tertiary structure 99% identical to the porcine brain PEP structure. A Km for the recombinant spPEP was determined to be 210 ± 53 µM for the zGly-Pro-pNA substrate in 0.025 M ethanolamine, pH 8.5, containing 0.1 M NaCl at 37 °C with a turnover rate of 172 ± 47 µM Gly-Pro-pNA/s/µM of enzyme.en_US
dc.formatPDFen_US
dc.languageenen_US
dc.publisherMDPIen_US
dc.rightsCC-BY-NC-4.0en_US
dc.sourceInsects;5,(2014) Pagination 762,782en_US
dc.subjectscutelleridaeen_US
dc.subjectprolyl endoproteaseen_US
dc.subjectserine proteaseen_US
dc.subjectcdnaen_US
dc.subjecthomology modelingen_US
dc.subjectinserten_US
dc.titleCloning, Expression, Sequence Analysis and Homology Modeling of the Prolyl Endoprotease from Eurygaster integriceps Putonen_US
dc.typeJournal Articleen_US
cg.creator.ID0000-0001-8945-3126en_US
cg.creator.ID-typeORCIDen_US
cg.subject.agrovocwheaten_US
cg.subject.agrovochemipteraen_US
cg.subject.agrovocglutenen_US
cg.contributor.centerInternational Center for Agricultural Research in the Dry Areas - ICARDAen_US
cg.contributor.centerStephen F. Austin State University - SFASUen_US
cg.contributor.crpCRP on Dryland Systems - DSen_US
cg.contributor.crpCRP on Grain Legumes - GLen_US
cg.contributor.crpCRP on Wheat - WHEATen_US
cg.contributor.funderNot Applicableen_US
cg.contributor.project-lead-instituteInternational Center for Agricultural Research in the Dry Areas - ICARDAen_US
cg.coverage.regionGlobalen_US
cg.contactblack@sfasu.eduen_US
dc.identifier.statusOpen accessen_US


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