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

Differences between alcohol dehydrogenases. Structural properties and evolutionary aspects.

H Jörnvall

    European Journal of Biochemistry
    |February 1, 1977
    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

    Comparison of expression patterns and cell adhesion properties of the mouse biliary glycoproteins Bgp1 and Bgp2.

    European journal of biochemistry·2020
    Same journal

    AB 3.1.1.1 (or EC 3.1.1.?).

    European journal of biochemistry·2020
    Same journal

    Cdk5.

    European journal of biochemistry·2018
    Same journal

    Structure of the core oligosaccharide of a rough-type lipopolysaccharide of Pseudomonas syringae pv. phaseolicola.

    European journal of biochemistry·2004
    Same journal

    Monitoring ligand-mediated nuclear receptor-coregulator interactions by noncovalent mass spectrometry.

    European journal of biochemistry·2004
    Same journal

    Solution structure of long neurotoxin NTX-1 from the venom of Naja naja oxiana by 2D-NMR spectroscopy.

    European journal of biochemistry·2004
    See all related articles

    Yeast and horse liver alcohol dehydrogenases are distantly related homologous enzymes. Differences in subunit size and structure are explained by internal variations, suggesting evolutionary divergence and a common ancestor.

    Area of Science:

    • Biochemistry
    • Enzymology
    • Molecular Evolution

    Background:

    • Alcohol dehydrogenases (ADHs) are crucial enzymes in alcohol metabolism.
    • Comparing ADH structures provides insights into enzyme evolution and function.
    • Previous studies established the tertiary structure of horse liver ADH.

    Purpose of the Study:

    • To compare the primary structures of yeast and horse liver alcohol dehydrogenases.
    • To understand the structural basis for differences in subunit size and function.
    • To explore evolutionary relationships between different ADH enzymes.

    Main Methods:

    • Primary structure comparison of yeast and horse liver ADHs.
    • Analysis of sequence identity and differences.
    • Correlation of structural similarities/dissimilarities with functional regions.

    Related Experiment Videos

    Main Results:

    • Yeast and horse liver ADHs are homologous but distantly related, with 25% positional identity in common regions.
    • Subunit size differences are attributed to internal deletions/insertions.
    • Most similar regions involve active sites; dissimilar regions relate to loops and subunit interactions, potentially affecting zinc-binding and quaternary structure.
    • Evidence suggests internal sequence coincidences and superficial similarities with other dehydrogenases.

    Conclusions:

    • Structural variations in ADHs are linked to functional requirements and evolutionary adaptations.
    • Dissimilarities may reflect changes in zinc-binding and quaternary structure.
    • A model proposing a common ancestor for these and associated dehydrogenases is supported by observations.