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

Crystal structure of human dihydrolipoamide dehydrogenase: NAD+/NADH binding and the structural basis of disease-causing mutations.

Journal of molecular biology - 15 Jul 2005

Brautigam Chad A, Chuang Jacinta L, Tomchick Diana R, Machius Mischa, Chuang David T

Abstract excerpt

Human dihydrolipoamide dehydrogenase (hE3) is an enzymatic component common to the mitochondrial alpha-ketoacid dehydrogenase and glycine decarboxylase complexes. Mutations to this homodimeric flavoprotein cause the often-fatal human disease known as E3 deficiency. To catalyze the oxidation of dihydrolipoamide, hE3 uses two molecules: non-covalently bound FAD and a transiently bound substrate, NAD+. To address...

Read the complete abstract on PubMed

Topics

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

Share to Databases, Protein
Share to Dihydrolipoamide Dehydrogenase

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Disulfides

Share to Maple Syrup Urine Disease

Share to Niacinamide

Share to Potyvirus

Share to Pseudomonas putida

Source

Identifiers

PMID: 15946682
DOI: 10.1016/j.jmb.2005.05.014

Provenance

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.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Crystal structure of human dihydrolipoamide dehydrogenase: NAD+/NADH binding and the structural basis of disease-causing mutations.PMID 15946682Read ↗

Human dihydrolipoamide dehydrogenase (E3) deficiency: Novel insights into the structural basis and molecular pathomechanismSemantic proximity Read ↗

Crystal structures of the disease-causing D444V mutant and the relevant wild type human dihydrolipoamide dehydrogenase.Semantic proximity Read ↗

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

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

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

Identification of two missense mutations in a dihydrolipoamide dehydrogenase-deficient patient.Semantic proximity Read ↗

Activity of human dihydrolipoamide dehydrogenase is largely reduced by mutation at isoleucine-51 to alanine.Semantic proximity Read ↗

A novel mutation in the dihydrolipoamide dehydrogenase E3 subunit gene (DLD) resulting in an atypical form of alpha-ketoglutarate dehydrogenase deficiency.Semantic proximity Read ↗

Crystal structure of human 3-hydroxy-3-methylglutaryl-CoA Lyase: insights into catalysis and the molecular basis for hydroxymethylglutaric aciduria.Semantic proximity Read ↗

X-ray structure of human beta3beta3 alcohol dehydrogenase. The contribution of ionic interactions to coenzyme binding.Semantic proximity Read ↗

Molecular dynamics study of the structural basis of dysfunction and the modulation of reactive oxygen species generation by pathogenic mutants of human dihydrolipoamide dehydrogenase.Semantic proximity Read ↗

Three-dimensional structure of human electron transfer flavoprotein to 2.1-A resolution.Semantic proximity Read ↗

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