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Aldehyde dehydrogenases: widespread structural and functional diversity within a shared framework

J Hempel1, H Nicholas, R Lindahl

  • 1Department of Molecular Genetics and Biochemistry, University of Pittsburgh, Pennsylvania 15261.

Protein Science : a Publication of the Protein Society
|November 1, 1993
PubMed
Summary
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This study aligns 16 aldehyde oxidoreductases, revealing conserved residues critical for enzyme structure and function. Findings highlight evolutionary constraints and variations in coenzyme binding sites within these important metabolic enzymes.

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Enzymology

Background:

  • Aldehyde oxidoreductases are crucial enzymes in metabolic pathways, utilizing NAD and/or NADP coenzymes.
  • These enzymes exhibit diverse substrate specificities, including those for semialdehydes.
  • Understanding their evolutionary relationships and conserved features is key to elucidating their catalytic mechanisms.

Purpose of the Study:

  • To perform sequence alignment of 16 NAD and/or NADP-linked aldehyde oxidoreductases.
  • To identify conserved residues and structural motifs indicative of evolutionary constraints and functional roles.
  • To investigate variations in coenzyme-binding sites across different aldehyde dehydrogenase forms.

Main Methods:

  • Multiple sequence alignment of 16 aldehyde oxidoreductase sequences.

Related Experiment Videos

  • Analysis of invariant and highly conserved residues.
  • Identification of conserved structural motifs, including those in predicted beta-strands and NAD-binding sites.

    • Main Results:

    • Pairwise sequence identities ranged from 15% to 83%.
    • Eleven invariant residues, including glycine and proline, suggest evolutionary restraint at peptide chain-bending points.
    • A single invariant cysteine and conserved hydrophobic residues support catalytic and structural roles, respectively.
    • Variations in the NAD-binding site motif (GXGXXG) were observed, with reduced conservation of glycine and absence of threonine.

    Conclusions:

    • Conserved residues play critical roles in the structure, function, and catalytic activity of aldehyde oxidoreductases.
    • Evolutionary pressures have maintained specific structural features while allowing for variance in coenzyme-binding interactions.
    • The findings provide insights into the catalytic mechanisms and evolutionary diversification of aldehyde dehydrogenases.