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Background  Selection on proteins is typically measured with the assumption that each protein acts independently. However, selection more likely acts at higher levels of biological organization, requiring an integrative view of protein function. Here, we built a kinetic model for  de novo  pyrimidine biosynthesis in the yeast  Saccharomyces cerevisiae  to relate pathway function to selective pressures on individual protein-encoding genes.    Results  Gene families across yeast were constructed for each member of the pathway and the ratio of nonsynonymous to synonymous nucleotide substitution rates (dN/dS) was estimated for each enzyme from  S. cerevisiae  and closely related species. We found a positive relationship between the influence that each enzyme has on pathway function and its selective constraint.    Conclusions  We expect this trend to be locally present for enzymes that have pathway control, but over longer evolutionary timescales we expect that mutation-selection balance may change the enzymes that have pathway control.    Electronic supplementary material  The online version of this article (doi:10.1186/s12862-015-0515-x) contains supplementary material, which is available to authorized users.

Characterizing selective pressures on the pathway for de novo biosynthesis of pyrimidines in yeast