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

Drosophila alcohol dehydrogenase: acetate-enzyme interactions and novel insights into the effects of electrostatics on catalysis.

Journal of molecular biology - 21 Jan 2005

Benach Jordi, Winberg Jan-Olof, Svendsen John-Sigurd, Atrian Sílvia, Gonzàlez-Duarte Roser, Ladenstein Rudolf

Abstract excerpt

Drosophila alcohol dehydrogenase (DADH) is an NAD+-dependent enzyme that catalyzes the oxidation of alcohols to aldehydes/ketones and that is also able to further oxidize aldehydes to their corresponding carboxylic acids. The structure of the ternary enzyme-NADH-acetate complex of the slow alleloform of Drosophila melanogaster ADH (DmADH-S) was solved at 1.6 A resolution by X-ray crystallography. The coenzyme...

Read the complete abstract on PubMed

Topics

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

Share to Acetates
Share to Alcohol Dehydrogenase

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

Share to Catalysis

Share to Nuclear Magnetic Resonance, Biomolecular

Share to Oxidation-Reduction

Share to Static Electricity

Share to Stereoisomerism

Source

Identifiers

PMID: 15581900
DOI: 10.1016/j.jmb.2004.10.028

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 · 12 closest

Drosophila alcohol dehydrogenase: acetate-enzyme interactions and novel insights into the effects of electrostatics on catalysis.PMID 15581900Read ↗

Insights into Aldehyde Dehydrogenase Enzymes: A Structural PerspectiveSemantic proximity Read ↗

Crystal structures of mouse class II alcohol dehydrogenase reveal determinants of substrate specificity and catalytic efficiency.Semantic proximity Read ↗

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

Kinetics aspects of Gamma-hydroxybutyrate dehydrogenase.Semantic proximity Read ↗

Role of aspartic acid 38 in the cofactor specificity of Drosophila alcohol dehydrogenase.Semantic proximity Read ↗

Identification of a novel NADH-specific aldo-keto reductase using sequence and structural homologies.Semantic proximity Read ↗

Engineering the cofactor specificity of an alcohol dehydrogenase via single mutations or insertions distal to the 2'-phosphate group of NADP(H).Semantic proximity Read ↗

Allostery and Evolution: A Molecular Journey Through the Structural and Dynamical Landscape of an Enzyme Super Family.Semantic proximity Read ↗

Structural and biochemical investigations of the catalytic mechanism of an NADP-dependent aldehyde dehydrogenase from Streptococcus mutans.Semantic proximity Read ↗

The structure of the yeast NADH dehydrogenase (Ndi1) reveals overlapping binding sites for water- and lipid-soluble substrates.Semantic proximity Read ↗

Reconstructing dynamics correlation network to simultaneously improve activity and stability of 2,3-butanediol dehydrogenase by design of distal interchain disulfide bonds.Semantic proximity Read ↗

Complete reversal of coenzyme specificity by concerted mutation of three consecutive residues in alcohol dehydrogenase.Semantic proximity Read ↗

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