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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Beassoni, Paola R. Otero, Lisandro H. Lisa, Angela T. Boetsch, Cristhian Domenech, Carlos E. González-nilo, Fernado D. |
| Description | Author Affiliation: Beassoni PR ( Departamento de Biología Molecular, Universidad Nacional de Río Cuarto, X5800BYA Río Cuarto, Córdoba, Argentina. pbeassoni@exa.unrc.edu.ar) |
| Abstract | Pseudomonas aeruginosa phosphorylcholine phosphatase (PchP) catalyzes the hydrolysis of phosphorylcholine (Pcho) to produce choline and inorganic phosphate. PchP belongs to the haloacid dehalogenase superfamily (HAD) and possesses the three characteristic motifs of this family: motif I ( $^{31}$ D and $^{33}$ D), motif II ( $^{166}$ S), and motif III ( $^{242}$ K, $^{261}$ G, $^{262}$ D and $^{267}$ D), which fold to form the catalytic site that binds the metal ion and the phosphate moiety of Pcho. Based on comparisons to the PHOSPHO1 and PHOSPHO2 human enzymes and the choline-binding proteins of Gram-(+) bacteria, we selected residues $^{42}$ E and $^{43}$ E and the aromatic triplet $^{82}$ YYY $^{84}$ for site-directed mutagenesis to study the interactions with Pcho and p -nitrophenylphosphate as substrates of PchP. Because mutations in $^{42}$ E, $^{43}$ E and the three tyrosine residues affect both the substrate affinity and the inhibitory effect produced by high Pcho concentrations, we postulate that two sites, one catalytic and one inhibitory, are present in PchP and that they are adjacent and share residues. |
| ISSN | 00063002 |
| Journal | Biochimica et Biophysica Acta (BBA) - Reviews on Cancer |
| Issue Number | 7 |
| Volume Number | 1814 |
| Language | English |
| Publisher | Elsevier |
| Publisher Date | 2011-07-01 |
| Publisher Place | Netherlands |
| Access Restriction | Open |
| Subject Keyword | Bacterial Proteins Metabolism Mutation Phosphoric Monoester Hydrolases Phosphorylcholine Pseudomonas Aeruginosa Enzymology Quaternary Ammonium Compounds Alkanes Chemistry Amino Acid Sequence Genetics Binding Sites Biocatalysis Catalytic Domain Kinetics Models, Molecular Molecular Sequence Data Mutagenesis, Site-Directed Protein Binding Protein Structure, Tertiary Sequence Homology, Amino Acid Substrate Specificity Research Support, Non-U.S. Gov't Biochemistry |
| Content Type | Text |
| Resource Type | Article |
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