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Plant α‐glucan phosphatases SEX4 and LSF2 display different affinity for amylopectin and amylose
Author(s) -
Wilkens Casper,
Auger Kyle D.,
Anderson Nolan T.,
Meekins David A.,
Raththagala Madushi,
Abou Hachem Maher,
Payne Christina M.,
Gentry Matthew S.,
Svensson Birte
Publication year - 2016
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1002/1873-3468.12027
Subject(s) - amylopectin , amylose , glucan , chemistry , cyclodextrin , surface plasmon resonance , starch , binding site , polysaccharide , biochemistry , carbohydrate binding module , affinity electrophoresis , affinity chromatography , enzyme , materials science , glycoside hydrolase , nanotechnology , nanoparticle
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 K Dapp for amylopectin and amylose, and K D 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 K Dapp 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.