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- W2742051263 abstract "Aplantcysteineendopeptidase,designatedSH-EP,isamajorproteaseoccurring incotyledonsof Vigna mungoseedlings,andactstodegradeseedglobulinstoredin proteinbodies (proteinstoragevacuoles). SH-EP is synthesizedonmembrane boundribosomesasa43-kDaintermediatethroughthecotranslationalcleavageof asignalsequence,andtheintermediateisprocessedfurthertothe33-kDamature enzymevia39-and36-kDaintermediates.(a) N-terminalprocessing- Experiments of in vitro processingoftheSH-EPintermediates revealedthattwo processing enzymes, VmPE-l and VmPE-2 (v. mungo processing enzymes 1 and 2), are involvedintheprocessing.VmPE-lwaspurifiedfromtheday-3cotyledons. The enzymeisthesametypeofproteaseasasparaginylendopeptidasesintermsofthe primarystructureandsubstratespecificity. (b) C-terminal processing- Theamino acidsequenceofSH-EPdeducedfromthecDNAcontainsC-terminuswithLys Asp-Glu-Leu(KDEL)tail,whichisknownasaretentionsignalforendoplasmic reticulum(ER)whilematureSH-EPislocalizedinproteinbodies.Theanalysisfor C-terminalaminoacidresiduesofSH-EPindicatedthattheC-terminalpropeptide of10aminoacidresiduescontainingtheKDELtailisprocessedtoformmature SH-EP." @default.
- W2742051263 created "2017-08-08" @default.
- W2742051263 creator A5057077179 @default.
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- W2742051263 date "1997-01-01" @default.
- W2742051263 modified "2023-09-26" @default.
- W2742051263 title "62.ACysteineEndopeptidase(SH-EP)inGerminated Vigna mungoSeeds:Post-translationalProcessingand IntracellularTransport" @default.
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