Publications by authors named "Paola Rita Beassoni"
Article Synopsis
- * Hemolytic phospholipase C and phosphorylcholine phosphatase (PchP) work sequentially to convert phosphatidylcholine into choline and inorganic phosphate, and PchP's structure includes three domains crucial for its function and regulation.
- * The crystal structure of PchP reveals two binding sites for phosphocholine, and experiments confirm how these sites interact, enhancing our understanding of PchP's role and how it recognizes various substrates in the haloacid dehalogenase family.
Pseudomonas aeruginosa synthesizes phosphorylcholine phosphatase (PchP) when grown on choline, betaine, dimethylglycine or carnitine. In the presence of Mg(2+) or Zn(2+), PchP catalyzes the hydrolysis of p-nitrophenylphosphate (p-NPP) or phosphorylcholine (Pcho). The regulation of pchP gene expression is under the control of GbdR and NtrC; dimethylglycine is likely the metabolite directly involved in the induction of PchP.
View Article and Find Full Text PDFPseudomonas aeruginosa phosphorylcholine phosphatase (PchP) catalyzes the hydrolysis of phosphorylcholine (Pcho), is activated by Mg(2+) or Zn(2+), and is inhibited by high concentrations of substrate. This study has shown that PchP contains two sites for alkylammonium compounds (AACs): one in the catalytic site near the metal ion-phosphoester pocket, and the other in an inhibitory site responsible for the binding of the alkylammonium moiety. The catalytic mechanism for the entry of Pcho in both sites and Zn(2+) or Mg(2+) follows a random sequential mechanism.
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