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Hyperthermophilic dehydrogenase enzymes.

J A Littlechild1, J E Guy, M N Isupov

  • 1School of Biological Science and Chemistry, Exeter Biocatalysis Centre, Stocker Road, Exeter EX4 4QD, U.K. J.A.Littlechild@exeter.ac.uk

Biochemical Society Transactions
|March 30, 2004
PubMed
Summary

This study reveals that archaeal dehydrogenases, despite low sequence identity, share similar protein folds with bacterial and eukaryotic enzymes. Their high thermostability is linked to increased salt bridges, hydrophobic interactions, and disulfide bonds.

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Area of Science:

  • Biochemistry
  • Structural Biology
  • Enzymology

Background:

  • Archaeal dehydrogenases exhibit low sequence identity compared to bacterial and eukaryotic counterparts.
  • Hyperthermophilic enzymes present unique structural and stability characteristics.

Purpose of the Study:

  • To elucidate the structural basis of thermostability in archaeal dehydrogenases.
  • To compare the structures of archaeal dehydrogenases with their counterparts in other domains of life.

Main Methods:

  • Cloning and over-expression of archaeal dehydrogenases in Escherichia coli.
  • High-resolution crystallographic structure determination of apo- and holo-forms of GAPDH and ADH.
  • Analysis of protein fold, active site, and stabilizing interactions.

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Main Results:

  • Archaeal GAPDH and ADH structures were solved, revealing conserved protein folds despite low sequence identity.
  • A relocation of the active site in archaeal GAPDH enzymes was observed, indicating evolutionary significance.
  • High thermostability is attributed to increased salt bridges, hydrophobic interactions, secondary structure content, and disulfide bonds.

Conclusions:

  • Archaeal dehydrogenases maintain functional folds and exhibit unique structural adaptations for thermostability.
  • The findings provide insights into the evolution of enzymes and their adaptation to extreme environments.