Abstract
The nitrophenyl phosphatase family of the Haloacid Dehalogenase superfamily consists of a number of phosphatases. The homolog in S. cerevisiae was only known to hydrolyze p‐nitrophenyl phosphate. BLAST searches and alignments indicated that PHO13 from S. cerevisiae was most similar to an algae PGPase. We cloned and overexpressed PHO13 and determined that PHO13 is a PGPase. In photosynthetic organisms, phosphoglycolate is generated in the Calvin cycle; how it is produced in nonphotosynthetic organisms is less clear. Since it a strong inhibitor of triose phosphate isomerase, it must be degraded, regardless of its origin. The PGPase from S. aureus is a virulence factor, indicating its importance. To better understand the role of PGPase in the cell, we are using yeast as a model organism, studying a pho13 knockout mutant and doing complementation studies. Enzymatic characterization, including substrate specificity, pH optimum, divalent metal ion requirements, and kinetics, has been completed, and crystal growth for structural determination is in progress. This research has been supported by an NIH AREA grant, an ASM summer undergraduate research fellowship, and a RIT honors summer research fellowship.
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