Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Experiment Videos

Fundamental molecular differences between alcohol dehydrogenase classes

O Danielsson1, S Atrian, T Luque

  • 1Department of Medical Biochemistry and Biophysics, Karolinska Institutet, Stockholm, Sweden.

Proceedings of the National Academy of Sciences of the United States of America
|May 24, 1994
PubMed
Summary
This summary is machine-generated.

Related Concept Videos

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

Binding of amyloid beta-peptide to mitochondrial hydroxyacyl-CoA dehydrogenase (ERAB): regulation of an SDR enzyme activity with implications for apoptosis in Alzheimer's disease.

FEBS letters·1999
Same author

Structure and function of betaine aldehyde dehydrogenase. An enzyme within the multienzyme aldehyde dehydrogenase system.

Advances in experimental medicine and biology·1999
Same author

Studies on variants of alcohol dehydrogenases and its domains.

Advances in experimental medicine and biology·1999
Same author

Zinc binding characteristics of the synthetic peptide corresponding to the structural zinc site of horse liver alcohol dehydrogenase.

Advances in experimental medicine and biology·1999
Same author

Multiplicity and complexity of SDR and MDR enzymes.

Advances in experimental medicine and biology·1999
Same author

Regulatory factors and motifs in SDR enzymes.

Advances in experimental medicine and biology·1999
Same journal

Chemotactic self-organization captures the dynamics of mammalian hair follicle patterning.

Proceedings of the National Academy of Sciences of the United States of America·2026
Same journal

Tomographic imaging of superconducting order using particle-hole interference.

Proceedings of the National Academy of Sciences of the United States of America·2026
Same journal

Inhibitory potential of autologous neutralizing antibodies sets quantitative limits on the rebound-competent HIV-1 reservoir.

Proceedings of the National Academy of Sciences of the United States of America·2026
Same journal

Inferring epidemiological parameters under an infectious phylogeography model with visitor dynamics.

Proceedings of the National Academy of Sciences of the United States of America·2026
Same journal

Analytical modeling for suction cup designs for skin-interfaced wearable devices.

Proceedings of the National Academy of Sciences of the United States of America·2026
Same journal

Improving cell-free metabolism through direct integration of artificial respiratory chains.

Proceedings of the National Academy of Sciences of the United States of America·2026
See all related articles

Researchers identified a medium-chain alcohol dehydrogenase in Drosophila, bridging a gap in enzyme distribution. This conserved class III enzyme plays a crucial role in cellular metabolism.

Area of Science:

  • Biochemistry
  • Enzymology
  • Molecular Biology

Background:

  • Alcohol dehydrogenases (ADHs) exist in two main families: medium-chain (zinc enzymes) and short-chain.
  • Medium-chain ADHs are found in various organisms, but were thought to be absent in insects.
  • Insects were believed to possess only short-chain ADHs.

Purpose of the Study:

  • To characterize a medium-chain alcohol dehydrogenase in Drosophila.
  • To investigate the evolutionary distribution and functional conservation of medium-chain ADHs.
  • To compare the properties of Drosophila medium-chain ADH with other known ADH classes.

Main Methods:

  • Biochemical characterization of the identified Drosophila enzyme.
  • Sequence and structural comparison with human medium-chain ADH.

Related Experiment Videos

  • Analysis of enzymatic properties, including substrate specificity and kinetic parameters.
  • Gene expression analysis across different developmental stages.
  • Main Results:

    • A medium-chain alcohol dehydrogenase (class III ADH) was identified in Drosophila, identical to insect octanol dehydrogenase.
    • The Drosophila enzyme shows high residue identity (70%) to human class III ADH, with conserved substrate/coenzyme interaction sites.
    • Key differences, such as Phe-51 and extra residues near position 250, influence coenzyme binding and activity.
    • The enzyme exhibits low activity toward ethanol but high selectivity for formaldehyde/glutathione.
    • mRNA expression is constitutive across all developmental stages.

    Conclusions:

    • The discovery bridges the gap in the known distribution of medium-chain alcohol dehydrogenases.
    • Establishes the class III enzyme as strictly conserved across diverse species, including insects.
    • Highlights the fundamental molecular differences between class III and class I ADHs.
    • Suggests a significant role for this conserved enzyme in cellular metabolism.