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Date of Award
Restricted Thesis: Campus only access
Bachelor of Science
Dr. Suzanne O'Handley
YZGD from B. thiaminolyticus is a pyridoxal-5-phosphate specific acid phosphatase,. YZGD contains two motifs; one contains the highly conserved Nudix hydrolase signature sequence, GX5EX7REUXEEXGU (U = I, L, or V), and the other contains homology to two yeast pNppases (hydrolyze p-nitrophenyl phosphate). No Nudix substrate has been discovered for YZGD and the phosphatase activity is believed to originate from the pNppase motif; YZGD's optimal activity is observed at an acidic pH (~pH 5) whereas Nudix hydrolases all catalyze hydrolysis at an alkaline pH (~pH 9) and YZGD does not require Mg+2 , whereas Nudix hydrolases do. To determine if we have uncovered a novel phosphatase motif, NAGD from E. coli, which also contains homology to this "pNppase" motif, has been cloned and will be studied for phosphatase activity. The pNppase from S. cerevisiae was also determined to be a protein18 , but YZGD does not have protein phosphatase activity, therefore, this motif does not appear to be a new protein phosphatase motif.
Wall, Jennifer L., "YZGD from B. thiaminolyticus is a pyridoxal-5-phosphate specific acid phosphatase and an unknown nudix hydrolase" (2000). Honors Theses. 493.