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

Class III alcohol dehydrogenase: consistent pattern complemented with the mushroom enzyme.

Annika Norin1, Jawed Shafqat, Mustafa El-Ahmad

  • 1Department of Medical Biochemistry and Biophysics, Karolinska Institutet, SE-171 77 Stockholm, Sweden.

FEBS Letters
|February 13, 2004
PubMed
Summary

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

Mass Spectrometry and Machine Learning Reveal Determinants of Client Recognition by Antiamyloid Chaperones.

Molecular & cellular proteomics : MCP·2022
Same author

Biological activity versus physiological function of proinsulin C-peptide.

Cellular and molecular life sciences : CMLS·2020
Same author

High intracellular stability of the spidroin N-terminal domain in spite of abundant amyloidogenic segments revealed by in-cell hydrogen/deuterium exchange mass spectrometry.

The FEBS journal·2019
Same author

60 years with BBRC.

Biochemical and biophysical research communications·2019
Same author

Novel long-chain neurotoxins from <i>Bungarus candidus</i> distinguish the two binding sites in muscle-type nicotinic acetylcholine receptors.

The Biochemical journal·2019
Same author

Systemic AA amyloidosis in the red fox (Vulpes vulpes).

Protein science : a publication of the Protein Society·2017

Researchers purified mushroom alcohol dehydrogenase (ADH) from Agaricus bisporus, revealing class III ADH active sites. This finding aids in recognizing these enzymes across different organisms.

Area of Science:

  • Biochemistry
  • Enzymology
  • Molecular Biology

Background:

  • Alcohol dehydrogenase (ADH) enzymes are crucial in metabolic pathways across organisms.
  • The common mushroom, Agaricus bisporus, possesses ADH enzymes whose structural and functional characteristics are not fully elucidated.
  • Understanding ADH diversity is important for metabolic engineering and drug development.

Purpose of the Study:

  • To purify and characterize alcohol dehydrogenase (ADH) from the common mushroom, Agaricus bisporus.
  • To determine the primary structure and active site characteristics of mushroom ADH.
  • To compare mushroom ADH with human ADHs and identify conserved residues for enzyme recognition.

Main Methods:

  • Purification of mushroom ADH to homogeneity.

Related Experiment Videos

  • Analysis of ADH isozymes and subunit composition.
  • Determination of primary structure using chemical, mass spectrometry, and cDNA sequencing.
  • Molecular modeling to compare with human ADHs.

    • Main Results:

    • Purification of a single set of ADH isozymes with specificity against formaldehyde/glutathione.
    • Identification of two highly similar subunits forming a three-member isozyme set of dimers.
    • Determination that active site residues are of the class III ADH type.
    • Subunit differences were found to affect residues outside the active site.
    • Conserved substrate-binding residues for class I (three) and class III (eight) ADHs were identified.

    Conclusions:

    • Mushroom ADH from Agaricus bisporus shares characteristics with class III ADHs.
    • The identified conserved residues are valuable for recognizing ADH enzymes across diverse species.
    • This study provides insights into the structural basis of ADH function and evolution.