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Related Experiment Videos

Different segment similarities in long-chain dehydrogenases.

B Persson1, J Jeffery, H Jörnvall

  • 1Department of Chemistry I, Karolinska Institutet, Stockholm, Sweden.

Biochemical and Biophysical Research Communications
|May 31, 1991
PubMed
Summary

Long-chain dehydrogenases lack overall molecular similarity, but conserved coenzyme-binding segments exist. Glucose-6-phosphate dehydrogenase variants show conserved residues crucial for coenzyme binding and catalysis.

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Area of Science:

  • Biochemistry
  • Enzymology
  • Molecular Biology

Background:

  • Long-chain dehydrogenases (LCDs) are a diverse enzyme class.
  • Unlike short- and medium-chain dehydrogenases, LCDs generally lack discernible overall molecular similarities.
  • Understanding conserved regions is key to elucidating enzyme function.

Purpose of the Study:

  • To identify common patterns and conserved segments within long-chain dehydrogenases.
  • To investigate the coenzyme-binding sites and catalytic residues in glucose-6-phosphate dehydrogenase (G6PD).
  • To explore potential evolutionary relationships between different dehydrogenase enzymes.

Main Methods:

  • Comparative sequence analysis of various long-chain dehydrogenase enzymes.
  • Identification and characterization of conserved amino acid residues and segments.

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  • Analysis of enzyme variants, specifically species variants of glucose-6-phosphate dehydrogenase.
  • Examination of the pentose phosphate pathway enzymes, glucose-6-phosphate dehydrogenase and 6-phosphogluconate dehydrogenase.

    • Main Results:

    • No overall molecular similarities were found among long-chain dehydrogenases.
    • Discernible coenzyme-binding segments were identified across LCDs.
    • Approximately 20% of strictly conserved residues were found in glucose-6-phosphate dehydrogenase variants, forming three distinct segments.
    • These conserved segments in G6PD support assignments for coenzyme-binding and catalytic sites.
    • Glycine was found to be overrepresented among conserved residues, a common feature in distantly related proteins.
    • A distant similarity was noted between a C-terminal segment of G6PD and the N-terminal part of 6-phosphogluconate dehydrogenase.

    Conclusions:

    • Long-chain dehydrogenases exhibit conserved coenzyme-binding segments despite a lack of overall sequence similarity.
    • Specific conserved regions in glucose-6-phosphate dehydrogenase are critical for its catalytic function.
    • The identified distant similarity between G6PD and 6-phosphogluconate dehydrogenase warrants further investigation into their evolutionary connections.