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

Product binding modulates the thermodynamic properties of a Megasphaera elsdenii short-chain acyl-CoA dehydrogenase active-site mutant.

Biochemistry - 14 Jun 1994

Becker D F, Fuchs J A, Stankovich M T

Abstract excerpt

Previous work has shown that the redox properties of Megasphaera elsdenii short-chain acyl-CoA dehydrogenase (SCAD) are specifically modulated upon the binding of the substrate/product couple, allowing the reaction to proceed thermodynamically [Stankovich, M.T., & Soltysik, S. (1987) Biochemistry 26, 2627-2632]. The focus of this study on the Glu367Gln SCAD mutant protein is to gain an understanding of this...

Read the complete abstract on PubMed

Topics

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

Share to Acyl-CoA Dehydrogenase
Share to Acyl-CoA Dehydrogenases

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

Share to Binding Sites

Share to Electrochemistry

Share to Mutation

Share to Oxidation-Reduction

Share to Protein Binding

Share to Thermodynamics

Source

Identifiers

PMID: 8003473
DOI: 10.1021/bi00189a010

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 · 8 closest

Product binding modulates the thermodynamic properties of a Megasphaera elsdenii short-chain acyl-CoA dehydrogenase active-site mutant.PMID 8003473Read ↗

Identification of a long-range protein network that modulates active site dynamics in extremophilic alcohol dehydrogenases.Semantic proximity Read ↗

Purification and characterization of two polymorphic variants of short chain acyl-CoA dehydrogenase reveal reduction of catalytic activity and stability of the Gly185Ser enzyme.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 ↗

Structure and Substrate Specificity of Human Short-Chain Acyl-CoA Dehydrogenase and Insights into Pathogenicity of Disease-Associated Mutations.Semantic proximity Read ↗

Cytochrome c/cytochrome c peroxidase complex: effect of binding-site mutations on the thermodynamics of complex formation.Semantic proximity Read ↗

Short circuiting a sulfite oxidising enzyme with direct electrochemistry: active site substitutions and their effect on catalysis and electron transfer.Semantic proximity Read ↗

Structural and biochemical characterization of an atypical short-chain dehydrogenase/reductase reveals an unusual cofactor preference.Semantic proximity Read ↗

Functional analysis of acyl-CoA dehydrogenase catalytic residue mutants using surface plasmon resonance and circular dichroism.Semantic proximity Read ↗

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