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Pho13 from Saccharomyces cerevisiae, a Member of the p‐Nitrophenyl Phosphatase Family of the HAD Superfamily is a Phosphoglycolate Phosphatase
Author(s) -
O'Handley Suzanne,
Blake Kimbria,
Puts Regina,
Patron Alejandra Rizo,
Ramirez Sebastian,
Strassner Amanda,
Wahler Brandon,
Walling Megan
Publication year - 2011
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.25.1_supplement.967.4
Subject(s) - phosphatase , biochemistry , saccharomyces cerevisiae , enzyme , protein phosphatase 2 , biology , yeast
The nitrophenyl phosphatase family of the Haloacid Dehalogenase superfamily is a diverse family of proteins consisting of pyridoxal phosphatases from P. thiaminolyticus and humans, a UMPase (NAGD) from E. coli , phosphoglycolate phosphatases from S. aureus and algae, and a number of putative proteins. Homologs in the yeasts, S. cerevisiae and S. pombe , were only known to hydrolyze p‐nitrophenyl phosphate, a non‐natural substrate. Through bioinformatics analyses we noticed that the homolog in S. cerevisiae , Pho13 was most similar to the algae phosphoglycolate phosphatase. We cloned and overexpressed this enzyme and upon testing determined that Pho13 is a phosphoglycolate phosphatase as we predicted. The role of phosphoglycolate phosphatases in the Calvin cycle in photosynthetic organisms is well understood; its role in nonphotosynthetic organisms is less certain, however the phosphoglycolate phosphatase from S. aureus is a virulence factor, thus the phosphoglycolate phosphatases appear to carry out different but equally important cellular roles in nonphotosynthetic organisms as well. Enzymatic characterization and crystal growth for structural determination are in progress.