| Autor: |
Lisandro Horacio, Otero, Paola Rita, Beassoni, Cristhian, Boetsch, Angela Teresita, Lisa, Carlos Eduardo, Domenech |
| Rok vydání: |
2011 |
| Předmět: |
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| Zdroj: |
Enzyme Research |
| ISSN: |
2090-0414 |
| Popis: |
Pseudomonas 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. However, Zn(2+) is more effective than Mg(2+) at alleviating the inhibition produced by the entry of Pcho or different AACs in the inhibitory site. We postulate that Zn(2+) induces a conformational change in the active center that is communicated to the inhibitory site, producing a compact or closed structure. In contrast, Mg(2+) produces a relaxed or open conformation. |
| Databáze: |
OpenAIRE |
| Externí odkaz: |
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