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

Subunit interactions specify the allosteric regulatory properties of the potato tuber ADP-glucose pyrophosphorylase.

Biochemical and biophysical research communications - 19 Oct 2007

Kim Dongwook, Hwang Seon-Kap, Okita Thomas W

Abstract excerpt

ADP-glucose pyrophosphorylase (AGPase) catalyzes the first committed step of starch synthesis in plants. The potato tuber enzyme contains a pair of catalytic small subunits (SSs) and a pair of non-catalytic large subunits (LSs). We have previously identified a LS mutant containing a P52L replacem...

Read the complete abstract on PubMed

Topics

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

Share to Adenosine Triphosphate
Share to Allosteric Regulation
Share to Catalysis

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Glucose-1-Phosphate Adenylyltransferase

Share to Mutant Proteins

Share to Plant Tubers

Share to Protein Subunits

Share to Solanum tuberosum

Source

Identifiers

PMID: 17707339
DOI: 10.1016/j.bbrc.2007.07.162

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 4 Sept 2026. Prepared record publication-17707339-2026-09-04.2. Manifest publication-graph-cohort-2026-09-04.2.

Source receipt: PubMed via Helena Literature Corpus, retrieved 4 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Subunit interactions specify the allosteric regulatory properties of the potato tuber ADP-glucose pyrophosphorylase.PMID 17707339Read ↗

Analysis of allosteric effector binding sites of potato ADP-glucose pyrophosphorylase through reverse genetics.Semantic proximity Read ↗

Unraveling the activation mechanism of the potato tuber ADP-glucose pyrophosphorylase.Semantic proximity Read ↗

Direct appraisal of the potato tuber ADP-glucose pyrophosphorylase large subunit in enzyme function by study of a novel mutant form.Semantic proximity Read ↗

Modulation of allosteric regulation by E38K and G101N mutations in the potato tuber ADP-glucose pyrophosphorylase.Semantic proximity Read ↗

Enhanced heterotetrameric assembly of potato ADP-glucose pyrophosphorylase using reverse genetics.Semantic proximity Read ↗

Allosteric regulation of the higher plant ADP-glucose pyrophosphorylase is a product of synergy between the two subunits.Semantic proximity Read ↗

Generation of up-regulated allosteric variants of potato ADP-glucose pyrophosphorylase by reversion genetics.Semantic proximity Read ↗

ADP-glucose pyrophosphorylase from potato tuber: site-directed mutagenesis of homologous aspartic acid residues in the small and large subunits.Semantic proximity Read ↗

Directed molecular evolution of ADP-glucose pyrophosphorylase.Semantic proximity Read ↗

Probing allosteric binding sites of the maize endosperm ADP-glucose pyrophosphorylase.Semantic proximity Read ↗

Two Arabidopsis ADP-glucose pyrophosphorylase large subunits (APL1 and APL2) are catalytic.Semantic proximity Read ↗

ADP-Glucose pyrophosphorylase from potato tubers. Site-directed mutagenesis studies of the regulatory sites.Semantic proximity Read ↗

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