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Related Experiment Videos

Coenzyme binding in alcohol dehydrogenase.

H Eklund1

  • 1Department of Molecular Biology, Swedish University of Agricultural Sciences, Uppsala.

Biochemical Society Transactions
|April 1, 1989
PubMed
Summary

Nicotinamide adenine dinucleotide (NAD) is an active enzyme activator, not a passive participant, in alcohol dehydrogenase reactions. NAD binding induces a conformational change, creating a dehydrated active site and facilitating substrate binding.

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Area of Science:

  • Biochemistry
  • Structural Biology
  • Enzymology

Background:

  • Alcohol dehydrogenase (ADH) is a key enzyme in alcohol metabolism.
  • The role of nicotinamide adenine dinucleotide (NAD) in ADH catalysis has been investigated.
  • Understanding enzyme-cofactor interactions is crucial for elucidating metabolic pathways.

Purpose of the Study:

  • To investigate the role of NAD in the catalytic mechanism of horse liver alcohol dehydrogenase.
  • To elucidate the structural basis of NAD-induced enzyme activation.
  • To compare human ADH isoenzymes in relation to sequence differences and substrate specificities.

Main Methods:

  • Crystallographic investigations of horse liver alcohol dehydrogenase.
  • Analysis of enzyme structure and active site conformation.
  • Comparative sequence analysis of human ADH isoenzymes.

Main Results:

  • NAD is not a passive participant but an active activator of alcohol dehydrogenase.
  • NAD binding induces a significant conformational change, leading to a dehydrated active site.
  • NAD contributes to the formation of the substrate-binding cleft.
  • The catalytic events, substrate/inhibitor binding, and the role of the zinc ion are influenced by NAD.
  • Sequence differences in human ADH isoenzymes correlate with their distinct substrate specificities.

Conclusions:

  • NAD plays a critical role in activating alcohol dehydrogenase through conformational changes.
  • The structural insights into NAD binding provide a molecular understanding of ADH catalysis.
  • Sequence variations in human ADH isoenzymes explain their differing substrate preferences, highlighting evolutionary adaptations.

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