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Article

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

Scientific reports - 10 Apr 2015

Führing Jana Indra, Cramer Johannes Thomas, Schneider Julia, Baruch Petra, Gerardy-Schahn Rita, Fedorov Roman

Abstract excerpt

In mammals, UDP-glucose pyrophosphorylase (UGP) is the only enzyme capable of activating glucose-1-phosphate (Glc-1-P) to UDP-glucose (UDP-Glc), a metabolite located at the intersection of virtually all metabolic pathways in the mammalian cell. Despite the essential role of its product, the molecular basis of UGP function is poorly understood. Here we report the crystal structure of human UGP in complex with its...

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Identifiers

PMID: 25860585
DOI: 10.1038/srep09618
PMCID: PMC5381698

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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.

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