Jump to main content
Jump to site search

Issue 1, 2009
Previous Article Next Article

Cross-species analysis of the glycolytic pathway by comparison of molecular interaction fields

Author affiliations

Abstract

The electrostatic potential of an enzyme is a key determinant of its substrate interactions and catalytic turnover. Here we invoke comparative analysis of protein electrostatic potentials, along with sequence and structural analysis, to classify and characterize all the enzymes in an entire pathway across a set of different organisms. The electrostatic potentials of the enzymes from the glycolytic pathway of 11 eukaryotes were analyzed by qPIPSA (quantitative protein interaction property similarity analysis). The comparison allows the functional assignment of neuron-specific isoforms of triosephosphate isomerase from zebrafish, the identification of unusual protein surface interaction properties of the mosquito glucose-6-phosphate isomerase and the functional annotation of ATP-dependent phosphofructokinasesand cofactor-dependent phosphoglycerate mutases from plants. We here show that plants possess two parallel pathways to convert glucose. One is similar to glycolysis in humans, the other is specialized to let plants adapt to their environmental conditions. We use differences in electrostatic potentials to estimate kinetic parameters for the triosephosphate isomerases from nine species for which published parameters are not available. Along the core glycolytic pathway, phosphoglycerate mutase displays the most conserved electrostatic potential. The largest cross-species variations are found for glucose-6-phosphate isomerase, enolase and fructose-1,6-bisphosphate aldolase. The extent of conservation of electrostatic potentials along the pathway is consistent with the absence of a single rate-limiting step in glycolysis.

Graphical abstract: Cross-species analysis of the glycolytic pathway by comparison of molecular interaction fields

Back to tab navigation

Supplementary files

Publication details

The article was received on 24 Jun 2009, accepted on 27 Jul 2009 and first published on 07 Sep 2009


Article type: Paper
DOI: 10.1039/B912398A
Citation: Mol. BioSyst., 2009,6, 162-174
  •   Request permissions

    Cross-species analysis of the glycolytic pathway by comparison of molecular interaction fields

    M. Stein, R. R. Gabdoulline and R. C. Wade, Mol. BioSyst., 2009, 6, 162
    DOI: 10.1039/B912398A

Search articles by author

Spotlight

Advertisements