Plant α-glucan phosphatases SEX4 and LSF2 display different affinity for amylopectin and amylose

Research output: Contribution to journalJournal article – Annual report year: 2015Researchpeer-review


View graph of relations

The plant glucan phosphatases Starch EXcess 4 (SEX4) and Like Sex Four2 (LSF2) apply different starch binding mechanisms. SEX4 contains a carbohydrate binding module, and LSF2 has two surface binding sites (SBSs). We determined KDapp for amylopectin and amylose, and KD for β-cyclodextrin and validated binding site mutants deploying affinity gel electrophoresis (AGE) and surface plasmon resonance. SEX4 has a higher affinity for amylopectin; LSF2 prefers amylose and β-cyclodextrin. SEX4 has 50-fold lower KDapp for amylopectin compared to LSF2. Molecular dynamics simulations and AGE data both support long-distance mutual effects of binding at SBSs and the active site in LSF2.
Original languageEnglish
JournalFEBS Letters
Issue number1
Pages (from-to)118-128
Number of pages11
Publication statusPublished - 2016
CitationsWeb of Science® Times Cited: No match on DOI

    Research areas

  • Affinity gel electrophoresis, Carbohydrate binding domain, Like Sex Four2, Starch Excess 4, Surface binding sites, Surface plasmon resonance

ID: 119555645