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The evolution of hexokinases

T Ureta1, C Medina, A Preller

  • 1Departamento de Biología, Facultad de Ciencias, Universidad de Chile, Santiago, Chile.

Archivos De Biologia Y Medicina Experimentales
|January 1, 1987
PubMed
Summary
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Hexokinases, enzymes that phosphorylate sugars using ATP, exhibit diverse specificities and molecular masses across organisms. Gene duplication events likely shaped hexokinase evolution, leading to distinct regulatory mechanisms and conserved sequences.

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Enzymology

Background:

  • Hexokinases catalyze essential sugar phosphorylation reactions using ATP.
  • Enzymes range from sugar-specific kinases to less specific hexokinases.
  • Diversity in hexokinase structure, function, and evolutionary origins is observed.

Purpose of the Study:

  • To review recent advances in the structural and functional understanding of hexokinases.
  • To explore the evolutionary development of hexokinases, particularly in vertebrates.
  • To investigate the role of gene duplication in hexokinase evolution and regulation.

Main Methods:

  • Comparative analysis of hexokinase molecular masses (25 kDa, 50 kDa, 100 kDa) across different taxa.
  • Examination of hexokinase specificity, including sugar-specific, hexose-specific, and intermediate types.

Related Experiment Videos

  • Sequence comparisons of peptides from vertebrate hexokinase C and yeast hexokinases.
  • Main Results:

    • Hexokinases exhibit varied molecular masses (25, 50, 100 kDa) and specificities (e.g., glucokinase, fructokinase, mannokinasess).
    • Larger hexokinases (100 kDa) are found in vertebrates, while smaller ones are in microorganisms and invertebrates.
    • Product inhibition (glucose 6-P) in 100 kDa hexokinases suggests evolution of regulatory sites from duplicated active sites.
    • Sequence similarities between vertebrate and yeast hexokinases indicate conserved evolutionary pathways.

    Conclusions:

    • Gene duplication is a significant factor in the evolution of hexokinases.
    • The allosteric inhibition of vertebrate hexokinases points to functional divergence after gene duplication.
    • Conserved amino acid sequences suggest a slow evolutionary rate for homologous hexokinase genes.