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

Substrate and inhibitor specificities of the thermostable alcohol dehydrogenase allozymes ADH-71k and ADH-FCh.D. of Drosophila melanogaster.

Biochemical genetics - 1 Apr 1994

Eisses K T, Davies S L, Chambers G K

Abstract excerpt

Purified thermostable alcohol dehydrogenase allozymes ADH-71k and ADH-FCh.D. of Drosophila melanogaster have been compared with the two common enzyme forms ADH-F and ADH-S. Enzyme kinetic parameters for various primary and secondary alcohols were determined under standard conditions used previously. Both ADH-71k and ADH-FCh.D. show ADH-S-like reaction kinetics and Km values, due to retrograde evolution at site...

Read the complete abstract on PubMed

Topics

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

Share to Alcohol Dehydrogenase
Share to Alleles
Share to Drosophila melanogaster

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

Share to Kinetics

Share to Substrate Specificity

Source

Identifiers

PMID: 7980388
DOI: 10.1007/BF00554418

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

Substrate and inhibitor specificities of the thermostable alcohol dehydrogenase allozymes ADH-71k and ADH-FCh.D. of Drosophila melanogaster.PMID 7980388Read ↗

Analysis of the gene encoding the multifunctional alcohol dehydrogenase allozyme ADH-71k of Drosophila melanogaster.Semantic proximity Read ↗

Isolation of protease-free alcohol dehydrogenase (ADH) from Drosophila simulans and several homozygous and heterozygous Drosophila melanogaster variants.Semantic proximity Read ↗

Molecular similarity of Drosophila melanogaster alcohol dehydrogenase thermostable alleles from populations on different continents.Semantic proximity Read ↗

The alcohol dehydrogenase polymorphism in natural populations of Drosophila melanogaster: ADH activity variation restriction site polymorphism and the Adh cline.Semantic proximity Read ↗

ADH enzyme activity and Adh gene expression in Drosophila melanogaster lines differentially selected for increased alcohol tolerance.Semantic proximity Read ↗

A worldwide polymorphism in aldehyde dehydrogenase in Drosophila melanogaster: evidence for selection mediated by dietary ethanol.Semantic proximity Read ↗

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

Evolutionary genetics of the Drosophila alcohol dehydrogenase gene-enzyme system.Semantic proximity Read ↗

Drosophila melanogaster, a genetic model system for alcohol research.Semantic proximity Read ↗

Strains of Drosophila melanogaster differ in alcohol tolerance.Semantic proximity Read ↗

[Alcohol dehydrogenase and adaptation to ethanol in Drosophila].Semantic proximity Read ↗

[The ADH gene-enzyme system and the fitness of Drosophila melanogaster mutants].Semantic proximity Read ↗

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