Protein tyrosine phosphatase-like phytases: a new class of bacterial regulatory proteins?

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The overall objective of my research program is to increase our understanding of a newly discovered family of enzymes known as protein tyrosine phosphatase-like phytases. Phytases are widespread in nature and have been identified in prokaryotes, protists, fungi, animals, and plants. These enzymes catalyze the stepwise removal of phosphates from inositols phosphates which are an important group of signaling molecule that have been implicated in numerous important eukaryotic cellular processes including DNA repair, membrane trafficking in secretory and endocytic pathways, development, programmed cell death, and pathogenicity. In order to understand how these enzymes work in nature, I use a variety of techniques to characterize their basic biochemistry, structure, catalytic mechanism and biological function. Insights gained from these studies can also be used to develop cost effective sources of inositol phosphates, many of which have known pharmaceutical properties. This knowledge may also be used to develop solutions to a common pollution problem in intensive livestock production. Phytate is the most common inositol phosphate found in grains. Phytate is an important pollutant of surface water around intensive livestock operations because phytate is largely indigestible by swine and poultry. Feeding animals phytases is a simple approach to eliminate this problem.