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

Reengineering of the human pyruvate dehydrogenase complex: from disintegration to highly active agglomerates.

The Biochemical journal - 20 Feb 2017

Guo Jin, Hezaveh Samira, Tatur Jana, Zeng An-Ping, Jandt Uwe

Abstract excerpt

The pyruvate dehydrogenase complex (PDC) plays a central role in cellular metabolism and regulation. As a metabolite-channeling multi-enzyme complex it acts as a complete nanomachine due to its unique geometry and by coupling a cascade of catalytic reactions using 'swinging arms'. Mammalian and specifically human PDC (hPDC) is assembled from multiple copies of E1 and E3 bound to a large E2/E3BP 60-meric core. A...

Read the complete abstract on PubMed

Topics

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

Share to Acetyl Coenzyme A
Share to Catalytic Domain
Share to Dihydrolipoamide Dehydrogenase

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Protein Engineering

Share to Protein Multimerization

Share to Pyruvate Dehydrogenase Complex

Share to Pyruvate Dehydrogenase (Lipoamide)

Share to Pyruvic Acid

Source

Identifiers

PMID: 27986918
DOI: 10.1042/BCJ20160916

Genes

PDC

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 3 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Reengineering of the human pyruvate dehydrogenase complex: from disintegration to highly active agglomerates.PMID 27986918Read ↗

Structural insight into interactions between dihydrolipoamide dehydrogenase (E3) and E3 binding protein of human pyruvate dehydrogenase complex.Semantic proximity Read ↗

Structural basis of the dysfunctioning of human 2-oxo acid dehydrogenase complexes.Semantic proximity Read ↗

Simulations of Pathogenic E1α Variants: Allostery and Impact on Pyruvate Dehydrogenase Complex-E1 Structure and FunctionSemantic proximity Read ↗

Pyruvate dehydrogenase complex deficiency is linked to regulatory loop disorder in the αV138M variant of human pyruvate dehydrogenase.Semantic proximity Read ↗

Snapshots of catalysis in the E1 subunit of the pyruvate dehydrogenase multienzyme complex.Semantic proximity Read ↗

Exploring Structural Perturbations Caused by Cancer-Related Mutations in Pyruvate Kinase M2: A Comparison with the Wild-Type Enzyme.Semantic proximity Read ↗

Simulations of Pathogenic E1α Variants: Allostery and Impact on Pyruvate Dehydrogenase Complex-E1 Structure and Function.Semantic proximity Read ↗

Swiveling domain mechanism in pyruvate phosphate dikinase.Semantic proximity Read ↗

Crystal structure and interaction studies of human DHTKD1 provide insight into a mitochondrial megacomplex in lysine catabolismSemantic proximity Read ↗

A surface loop directs conformational switching of a lipoyl domain between a folded and a novel misfolded structure.Semantic proximity Read ↗

Structural insight into mechanisms for dynamic regulation of PKM2.Semantic proximity Read ↗

The two active sites in human branched-chain alpha-keto acid dehydrogenase operate independently without an obligatory alternating-site mechanism.Semantic proximity Read ↗

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