Journal of Molecular Evolution

, Volume 44 , Issue 5 , pp 552 –572

Molecular Evolutionary Analysis of the Thiamine-Diphosphate-Dependent Enzyme, Transketolase

  • Gerhard  Schenk
  • Roy  Layfield
  • Judith M.  Candy
  • Ronald G.  Duggleby
  • Peter F.  Nixon

DOI: 10.1007/PL00006179

Cite this article as:
Schenk, G., Layfield, R., Candy, J. et al. J Mol Evol (1997) 44: 552. doi:10.1007/PL00006179
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Abstract.

Members of the transketolase group of thiamine-diphosphate-dependent enzymes from 17 different organisms including mammals, yeast, bacteria, and plants have been used for phylogenetic reconstruction. Alignment of the amino acid and DNA sequences for 21 transketolase enzymes and one putative transketolase reveals a number of highly conserved regions and invariant residues that are of predicted importance for enzyme activity, based on the crystal structure of yeast transketolase. One particular sequence of 36 residues has some similarities to the nucleotide-binding motif and we designate it as the transketolase motif. We report further evidence that the recP protein from Streptococcus pneumoniae might be a transketolase and we list a number of invariant residues which might be involved in substrate binding. Phylogenies derived from the nucleotide and the amino acid sequences by various methods show a conventional clustering for mammalian, plant, and gram-negative bacterial transketolases. The branching order of the gram-positive bacteria could not be inferred reliably. The formaldehyde transketolase (sometimes known as dihydroxyacetone synthase) of the yeast Hansenula polymorpha appears to be orthologous to the mammalian enzymes but paralogous to the other yeast transketolases. The occurrence of more than one transketolase gene in some organisms is consistent with several gene duplications. The high degree of similarity in functionally important residues and the fact that the same kinetic mechanism is applicable to all characterized transketolase enzymes is consistent with the proposition that they are all derived from one common ancestral gene. Transketolase appears to be an ancient enzyme that has evolved slowly and might serve as a model for a molecular clock, at least within the mammalian clade.

Key words: Transketolase — Thiamine diphosphate — Transketolase motif — Evolution — Phylogenetic trees — Molecular clock 

Copyright information

© Springer-Verlag New York Inc. 1997

Authors and Affiliations

  • Gerhard  Schenk
    • 1
  • Roy  Layfield
    • 2
  • Judith M.  Candy
    • 3
  • Ronald G.  Duggleby
    • 1
  • Peter F.  Nixon
    • 1
  1. 1.Department of Biochemistry, Centre for Protein Structure, Function and Engineering, The University of Queensland,St. Lucia, QLD 4072, AustraliaAU
  2. 2.Centre for Molecular and Cellular Biology, The University of Queensland, St. Lucia, QLD 4072, AustraliaAU
  3. 3.Centre for Molecular Biotechnology, School of Life Sciences, Queensland University of Technology, Gardens Point,Brisbane, QLD 4001, AustraliaAU

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