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

Enhanced heat stability and kinetic parameters of maize endosperm ADPglucose pyrophosphorylase by alteration of phylogenetically identified amino acids.

Archives of biochemistry and biophysics - 1 Feb 2014

Boehlein Susan K, Shaw Janine R, Georgelis Nikolaos, Hannah L Curtis

Abstract excerpt

ADP-glucose pyrophosphorylase (AGPase) controls the rate-limiting step in starch biosynthesis and is regulated at various levels. Cereal endosperm enzymes, in contrast to other plant AGPases, are particularly heat labile and transgenic studies highlight the importance of temperature for cereal yi...

Read the complete abstract on PubMed

Topics

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

Share to Biocatalysis
Share to Endosperm
Share to Enzyme Stability

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Glucose-1-Phosphate Adenylyltransferase

Share to Hot Temperature

Share to Phosphates

Share to Protein Denaturation

Share to Protein Engineering

Source

Identifiers

PMID: 24378757
DOI: 10.1016/j.abb.2013.12.018

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 4 Sept 2026. Prepared record publication-24378757-2026-09-04.2. 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

Enhanced heat stability and kinetic parameters of maize endosperm ADPglucose pyrophosphorylase by alteration of phylogenetically identified amino acids.PMID 24378757Read ↗

Phylogenetic analysis of ADP-glucose pyrophosphorylase subunits reveals a role of subunit interfaces in the allosteric properties of the enzyme.Semantic proximity Read ↗

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

The two AGPase subunits evolve at different rates in angiosperms, yet they are equally sensitive to activity-altering amino acid changes when expressed in bacteria.Semantic proximity Read ↗

Starch phosphorylation: insights and perspectives.Semantic proximity Read ↗

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

The rice endosperm ADP-glucose pyrophosphorylase large subunit is essential for optimal catalysis and allosteric regulation of the heterotetrameric enzyme.Semantic proximity Read ↗

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

Functional characterization of alpha-glucan,water dikinase, the starch phosphorylating enzyme.Semantic proximity Read ↗

A single mutation that increases maize seed weight.Semantic proximity Read ↗

Multiple glycogen-binding sites in eukaryotic glycogen synthase are required for high catalytic efficiency toward glycogen.Semantic proximity Read ↗

OsPKpα1 encodes a plastidic pyruvate kinase that affects starch biosynthesis in the rice endosperm.Semantic proximity Read ↗

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

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