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

Toward a blueprint for UDP-glucose pyrophosphorylase structure/function properties: homology-modeling analyses.

Plant molecular biology - 1 Nov 2004

Geisler Matt, Wilczynska Malgorzata, Karpinski Stanislaw, Kleczkowski Leszek A

Abstract excerpt

UDP-glucose pyrophosphorylase (UGPase) is an important enzyme of synthesis of sucrose, cellulose, and several other polysaccharides in all plants. The protein is evolutionarily conserved among eukaryotes, but has little relation, aside from its catalytic reaction, to UGPases of prokaryotic origin. Using protein homology modeling strategy, 3D structures for barley, poplar, and Arabidopsis UGPases have been...

Read the complete abstract on PubMed

Topics

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

Share to Alternative Splicing
Share to Eukaryotic Cells

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Isoenzymes

Share to Plants

Share to Populus

Share to Prokaryotic Cells

Share to Protein Conformation

Share to Sequence Homology, Amino Acid

Source

Identifiers

PMID: 15803415
DOI: 10.1007/s11103-004-4953-x

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Toward a blueprint for UDP-glucose pyrophosphorylase structure/function properties: homology-modeling analyses.PMID 15803415Read ↗

UDP-glucose pyrophosphorylase. An old protein with new tricks.Semantic proximity Read ↗

Octamerization is essential for enzymatic function of human UDP-glucose pyrophosphorylase.Semantic proximity Read ↗

Open and Closed Structures of the UDP-glucose Pyrophosphorylase from Leishmania majorSemantic proximity Read ↗

A quaternary mechanism enables the complex biological functions of octameric human UDP-glucose pyrophosphorylase, a key enzyme in cell metabolism.Semantic proximity Read ↗

Mutation of UDP-glucose binding motif residues lead to increased affinity for ADP-glucose in sugarcane sucrose phosphate synthase.Semantic proximity Read ↗

Structural basis for the reaction mechanism of UDP-glucose pyrophosphorylase.Semantic proximity Read ↗

Biology, Mechanism, and Structure of Enzymes in the α-d-Phosphohexomutase Superfamily.Semantic proximity Read ↗

Sequence-structure relationships, expression profiles, and disease-associated mutations in the paralogs of phosphoglucomutase 1.Semantic proximity Read ↗

Cloning of a human liver UDP-glucose pyrophosphorylase cDNA by complementation of the bacterial galU mutation.Semantic proximity Read ↗

Structure-function relationships in NDP-sugar active SDR enzymes: Fingerprints for functional annotation and enzyme engineeringSemantic proximity Read ↗

Prediction and validation of the three-dimensional structure of glucokinase-1 from <i>Phytophthora infestans</i>Semantic proximity Read ↗

Proposed carrier lipid-binding site of undecaprenyl pyrophosphate phosphatase from Escherichia coli.Semantic proximity Read ↗

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