Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

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

FEBS letters - 1 Jan 2016

Wilkens Casper, Auger Kyle D, Anderson Nolan T, Meekins David A, Raththagala Madushi, Abou Hachem Maher, Payne Christina M, Gentry Matthew S, Svensson Birte

Abstract excerpt

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...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Amylopectin
Share to Amylose

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Carbohydrate Conformation

Share to Cytoplasmic Granules

Share to Dual-Specificity Phosphatases

Share to Molecular Dynamics Simulation

Share to Substrate Specificity

Share to Surface Plasmon Resonance

Source

Identifiers

PMID: 26763114
DOI: 10.1002/1873-3468.12027

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Plant α-glucan phosphatases SEX4 and LSF2 display different affinity for amylopectin and amylose.PMID 26763114Read ↗

Structure of the Arabidopsis glucan phosphatase like sex four2 reveals a unique mechanism for starch dephosphorylation.Semantic proximity Read ↗

The phosphoglucan phosphatase like sex Four2 dephosphorylates starch at the C3-position in Arabidopsis.Semantic proximity Read ↗

Starch phosphorylation: insights and perspectives.Semantic proximity Read ↗

Starch synthases.Semantic proximity Read ↗

Surface binding sites in amylase have distinct roles in recognition of starch structure motifs and degradation.Semantic proximity Read ↗

Overlapping functions of the starch synthases SSII and SSIII in amylopectin biosynthesis in Arabidopsis.Semantic proximity Read ↗

Differential condensation of FLO6 influences grain amylose synthesis in rice.Semantic proximity Read ↗

Insight into the redox regulation of the phosphoglucan phosphatase SEX4 involved in starch degradation.Semantic proximity Read ↗

Mutations in active surface sites of NtGGPPS1 enhance carotenoid biosynthesis and drought resistance in Nicotiana tabacum.Semantic proximity Read ↗

Relationships among starch biosynthesizing protein content, fine structure and functionality in rice.Semantic proximity Read ↗

Modulation of amylose content by structure-based modification of OsGBSS1 activity in rice (Oryza sativa L.).Semantic proximity Read ↗

Natural Polymorphisms in Arabidopsis Result in Wide Variation or Loss of the Amylose Component of Starch.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.