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

Dimerization interface of 3-hydroxyacyl-CoA dehydrogenase tunes the formation of its catalytic intermediate.

PloS one - 1 Jan 2014

Xu Yingzhi, Li He, Jin Ying-Hua, Fan Jun, Sun Fei

Abstract excerpt

3-Hydroxyacyl-CoA dehydrogenase (HAD, EC 1.1.1.35) is a homodimeric enzyme localized in the mitochondrial matrix, which catalyzes the third step in fatty acid β-oxidation. The crystal structures of human HAD and subsequent complexes with cofactor/substrate enabled better understanding of HAD catalytic mechanism. However, numerous human diseases were found related to mutations at HAD dimerization interface that is...

Read the complete abstract on PubMed

Topics

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

Share to 3-Hydroxyacyl CoA Dehydrogenases
Share to Biocatalysis
Share to Caenorhabditis elegans Proteins

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Molecular Dynamics Simulation

Share to Mutation

Share to Protein Multimerization

Source

Open in PubMed Open full text

Identifiers

PMID: 24763278
DOI: 10.1371/journal.pone.0095965
PMCID: PMC3999109

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

Dimerization interface of 3-hydroxyacyl-CoA dehydrogenase tunes the formation of its catalytic intermediate.PMID 24763278Read ↗

Molecular insights into mutation-induced conformational changes in Acetyl CoA Carboxylase for improved activity.Semantic proximity Read ↗

Structures of a constitutively active mutant of human IDH3 reveal new insights into the mechanisms of allosteric activation and the catalytic reaction.Semantic proximity Read ↗

Exploring Deleterious Nonsynonymous SNPs in the ACADM Gene: Insights Into Medium-Chain Acyl-CoA Dehydrogenase Deficiency (MCADD) via In Silico Analysis.Semantic proximity Read ↗

E487K-Induced Disorder in Functionally Relevant Dynamics of Mitochondrial Aldehyde Dehydrogenase 2.Semantic proximity Read ↗

Structural basis for channelling mechanism of a fatty acid beta-oxidation multienzyme complex.Semantic proximity Read ↗

Bivalent recognition of fatty acyl-CoA by a human integral membrane palmitoyltransferase.Semantic proximity Read ↗

A hydrogen-bonding network in mammalian sorbitol dehydrogenase stabilizes the tetrameric state and is essential for the catalytic power.Semantic proximity Read ↗

Insight into the molecular mechanism of yeast acetyl-coenzyme A carboxylase mutants F510I, N485G, I69E, E477R, and K73R resistant to soraphen A.Semantic proximity Read ↗

Functional and structural impact of 10 ACADM missense mutations on human medium chain acyl-Coa dehydrogenase.Semantic proximity Read ↗

A gatekeeper helix determines the substrate specificity of Sjögren-Larsson Syndrome enzyme fatty aldehyde dehydrogenase.Semantic proximity Read ↗

Structural basis for catalysis and substrate specificity of human ACAT1Semantic proximity Read ↗

The impacts of the mitochondrial myopathy-associated G58R mutation on the dynamic structural properties of CHCHD10.Semantic proximity Read ↗

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