Kinetic Properties of Purified Pseudomonas aeruginosa Phosphorylcholine Phosphatase Indicated That This Enzyme May Be Utilized by the Bacteria to Colonize in Different Environments

1999 ◽  
Vol 39 (1) ◽  
pp. 1-8 ◽  
Author(s):  
Mario A. Salvano ◽  
Carlos E. Domenech
Keyword(s):  
Pseudomonas Aeruginosa ◽  
Kinetic Properties ◽  
Phosphorylcholine Phosphatase

scholarly journals Phosphorylcholine Phosphatase: A Peculiar Enzyme of Pseudomonas aeruginosa

2011 ◽  
Vol 2011 ◽  
pp. 1-12 ◽  
Author(s):  
Carlos Eduardo Domenech ◽  
Lisandro Horacio Otero ◽  
Paola Rita Beassoni ◽  
Angela Teresita Lisa
Keyword(s):  
Gene Expression ◽  
Pseudomonas Aeruginosa ◽  
Adaptive Response ◽  
Metal Ion ◽  
Coordination Geometry ◽  
Choline Metabolism ◽  
Inhibitory Site ◽  
Closed Structure ◽  
Phosphorylcholine Phosphatase ◽  
Hydrolysis Of

Pseudomonas aeruginosa synthesizes phosphorylcholine phosphatase (PchP) when grown on choline, betaine, dimethylglycine or carnitine. In the presence of Mg2+ or Zn2+, 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. Therefore, the regulation of choline metabolism and consequently PchP synthesis may reflect an adaptive response of P. aeruginosa to environmental conditions. Bioinformatic and biochemistry studies shown that PchP contains two sites for alkylammonium compounds (AACs): one in the catalytic site near the metal ion-phosphoester pocket, and another in an inhibitory site responsible for the binding of the alkylammonium moiety. Both sites could be close to each other and interact through the residues 42E, 43E and 82YYY84. Zn2+ is better activator than Mg2+ at pH 5.0 and it is more effective at alleviating the inhibition produced by the entry of Pcho or different AACs in the inhibitory site. We postulate that Zn2+ induces at pH 5.0 a conformational change in the active center that is communicated to the inhibitory site, producing a compact or closed structure. However, at pH 7.4, this effect is not observed because to the hydrolysis of the [Zn2+L2−1L20(H2O)2] complex, which causes a change from octahedral to tetrahedral in the metal coordination geometry. This enzyme is also present in P. fluorescens, P. putida, P. syringae, and other organisms. We have recently crystallized PchP and solved its structure.

Identification, Cloning, and Expression of Pseudomonas aeruginosa Phosphorylcholine Phosphatase Gene

2005 ◽  
Vol 50 (5) ◽  
pp. 251-256 ◽  
Author(s):  
María J. Massimelli ◽  
Paola R. Beassoni ◽  
Marina A. Forrellad ◽  
José L. Barra ◽  
Mónica N. Garrido ◽  
...  
Keyword(s):  
Pseudomonas Aeruginosa ◽  
Cloning And Expression ◽  
Phosphorylcholine Phosphatase

Preparation and biophysical characterization of recombinant Pseudomonas aeruginosa phosphorylcholine phosphatase

2010 ◽  
Vol 71 (2) ◽  
pp. 153-159 ◽  
Author(s):  
Paola R. Beassoni ◽  
Federico Pérez de Berti ◽  
Lisandro H. Otero ◽  
Valeria A. Risso ◽  
Raul G. Ferreyra ◽  
...  
Keyword(s):  
Pseudomonas Aeruginosa ◽  
Biophysical Characterization ◽  
Phosphorylcholine Phosphatase

scholarly journals BEL-2, an Extended-Spectrum β-Lactamase with Increased Activity toward Expanded-Spectrum Cephalosporins in Pseudomonas aeruginosa

2009 ◽  
Vol 54 (1) ◽  
pp. 533-535 ◽  
Author(s):  
Laurent Poirel ◽  
Jean-Denis Docquier ◽  
Filomena De Luca ◽  
Annemie Verlinde ◽  
Louis Ide ◽  
...  
Keyword(s):  
Pseudomonas Aeruginosa ◽  
Kinetic Properties ◽  
Extended Spectrum ◽  
Positive Isolate ◽  
Increased Activity

ABSTRACT A Pseudomonas aeruginosa isolate recovered in Belgium produced a novel extended-spectrum ß-lactamase, BEL-2, differing from BEL-1 by a single Leu162Phe substitution. That modification significantly altered the kinetic properties of the enzyme, increasing its affinity for expanded-spectrum cephalosporins. The bla BEL-2 gene was identified from a P. aeruginosa isolate clonally related to another bla BEL-1-positive isolate.

scholarly journals Choline catabolism, σ54 factor and NtrC are required for the full expression of the Pseudomonas aeruginosa phosphorylcholine phosphatase gene

2011 ◽  
Vol 166 (5) ◽  
pp. 380-390 ◽  
Author(s):  
Maria J. Massimelli ◽  
Diego G. Sánchez ◽  
Maria V. Buchieri ◽  
Leticia Olvera ◽  
Paola R. Beassoni ◽  
...  
Keyword(s):  
Pseudomonas Aeruginosa ◽  
Full Expression ◽  
Phosphorylcholine Phosphatase
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