An analysis of the structurally and catalytically diverse serine hydrolase protein family in the Saccharomyces cerevisiae proteome was undertaken using two independent but complementary, large-scale approaches. The first approach is based on computational analysis of the structure of serine hydrolase active sites; the second utilizes the chemical reactivity of the serine hydrolase active site in complex mixtures. These proteomics approaches share the ability to fractionate the complex proteome into functional subsets. Each method identified a significant number of sequences, but fifteen proteins were identified by both methods. Eight of these were unannotated in the Saccharomyces Genome Database (SGD) at the time of this study and three of these are members of a newly-recognized eukaryotic serine hydrolase family. The results demonstrate the precision derived from combining complementary, function and structure-based approaches to extract biological information from complex proteomes.
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