The Structural Domains of Pseudomonas aeruginosa Phosphorylcholine Phosphatase Cooperate in Substrate Hydrolysis: 3D Structure and Enzymatic Mechanism

2012 ◽  
Vol 423 (4) ◽  
pp. 503-514 ◽  
Author(s):  
Lourdes Infantes ◽  
Lisandro Horacio Otero ◽  
Paola Rita Beassoni ◽  
Cristhian Boetsch ◽  
Angela Teresita Lisa ◽  
...  
Keyword(s):  
Pseudomonas Aeruginosa ◽  
3D Structure ◽  
Structural Domains ◽  
Enzymatic Mechanism ◽  
Phosphorylcholine Phosphatase ◽  
Substrate Hydrolysis

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 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

scholarly journals carP, encoding a Ca2+-regulated putative phytase, is evolutionarily conserved in Pseudomonas aeruginosa and has potential as a biomarker

Microbiology ◽  
2020 ◽  
Author(s):  
Sergio E. Mares ◽  
Michelle M. King ◽  
Aya Kubo ◽  
Anna A. Khanov ◽  
Erika I. Lutter ◽  
...  
Keyword(s):  
Pseudomonas Aeruginosa ◽  
Type Species ◽  
3D Structure ◽  
Missense Mutations ◽  
Phylogenetic Groups ◽  
Single Nucleotide ◽  
Content Type ◽  
Link Type ◽  
Evolutionarily Conserved ◽  
Intracellular Ca

Pseudomonas aeruginosa infects patients with cystic fibrosis, burns, wounds and implants. Previously, our group showed that elevated Ca2+ positively regulates the production of several virulence factors in P. aeruginosa , such as biofilm formation, production of pyocyanin and secreted proteases. We have identified a Ca2+-regulated β-propeller putative phytase, CarP, which is required for Ca2+ tolerance, regulation of the intracellular Ca2+ levels, and plays a role in Ca2+ regulation of P. aeruginosa virulence. Here, we studied the conservation of carP sequence and its occurrence in diverse phylogenetic groups of bacteria. In silico analysis revealed that carP and its two paralogues PA2017 and PA0319 are primarily present in P. aeruginosa and belong to the core genome of the species. We identified 155 single nucleotide alterations within carP, 42 of which lead to missense mutations with only three that affected the predicted 3D structure of the protein. PCR analyses with carP-specific primers detected P. aeruginosa specifically in 70 clinical and environmental samples. Sequence comparison demonstrated that carP is overall highly conserved in P. aeruginosa isolated from diverse environments. Such evolutionary preservation of carP illustrates its importance for P. aeruginosa adaptations to diverse environments and demonstrates its potential as a biomarker.

scholarly journals In silico and In vitro Evaluation of Some Synthesized Quinoline Derivatives into MexB Protein of Pseudomonas aeruginosa

2020 ◽  
Vol 10 (02) ◽  
pp. 195-199
Author(s):  
Abdalkader Saeed Latif ◽  
Majida G. Magtooph ◽  
Alia Essam Mahmood Alubadi
Keyword(s):  
Pseudomonas Aeruginosa ◽  
Inhibitory Concentration ◽  
3D Structure ◽  
Diffusion Method ◽  
Quinoline Derivatives ◽  
Disc Diffusion ◽  
Disc Diffusion Method ◽  
Medical City ◽  
Agar Well Diffusion Method

Molecular docking performed to evaluate the effect of five quinoline derivatives on the MexB protein of Pseudomonas aeruginosa as a potential inhibitor by utilizing the 3D structure of each quinoline compounds (C1, C2, C3, C4, and C5), and the crystal structure of the protein, C4 showed the greatest potential with -31.4 kcal/mol binding energy, and the lowest potential was for C1 with (-18.5 kcal/mol) compared with ciprofloxacin. Fifty samples were collected from different sites from patients who are attending to the medical city of Baghdad and private Dhelal Beirut Center, Baghdad, 36 of the samples were diagnosed as P. aeruginosa by routine culture test and confirmed by VITEK2, and those isolates were subjected to the susceptibility test against carbapenems, carbenicillin, levofloxacin, and erythromycin by disc diffusion method. The isolates that showed resistance to all of four antibiotics were based to evaluate the activity of quinoline derivatives by using the agar well diffusion method, where compounds C4 and C5 showed the highest line of activity as the minimum inhibitory concentration (MIC) was 256 μg/mL, meanwhile, C1 showed the lowest activity with MIC of 1,024 μg/mL.

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