Document Detail


Using a molecular model and kinetic experiments in the presence of divalent cations to study the active site and catalysis of Pseudomonas aeruginosa phosphorylcholine phosphatase.
MedLine Citation:
PMID:  18801468     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Phosphorylcholine phosphatase (PchP) of Pseudomonas aeruginosa, a product of the PA5292 gene, catalyzes the hydrolysis of phosphocholine to choline and inorganic phosphate (Pi). Phosphocholine is produced after hemolytic phospholipase C (PlcH) acts upon phosphatidylcholine or sphingomyelin. Therefore, PlcH and PchP are involved in the pathogenesis of P. aeruginosa. PchP belongs to the HAD superfamily as it contains three conserved sequences motifs. In mature PchP, the motifs I, II, and III are (31)DMDNT(35), (166)S, and (261)GDTPDSD(267), respectively. Kinetic characterization of wild-type and mutated proteins, obtained by site-directed mutagenesis, in addition to a molecular model of PchP helped us to understand the contribution of key residues in the conserved motifs I, II and III that are involved in the catalysis of p-nitrophenylphosphate processing after the addition of Mg(2+), Zn(2+) or Cu(2+) (these are activators of PchP activity). Our results are explained by invoking the concept of chemical hardness and softness introduced by Pearson in 1963 and its extension that "hard acids prefer to coordinate to hard bases and soft acids to soft bases" [Parr and Pearson, J. Am. Chem. Soc., 105, 7512-7516 (1983)].
Authors:
Paola R Beassoni; Lisandro H Otero; Angela T Lisa; Carlos E Domenech
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't     Date:  2008-08-29
Journal Detail:
Title:  Biochimica et biophysica acta     Volume:  1784     ISSN:  0006-3002     ISO Abbreviation:  Biochim. Biophys. Acta     Publication Date:  2008 Dec 
Date Detail:
Created Date:  2008-11-05     Completed Date:  2009-02-03     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  0217513     Medline TA:  Biochim Biophys Acta     Country:  Netherlands    
Other Details:
Languages:  eng     Pagination:  2038-44     Citation Subset:  IM    
Affiliation:
Departamento de Biología Molecular, Universidad Nacional de Río Cuarto, 5800 Río Cuarto, Córdoba, Argentina.
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MeSH Terms
Descriptor/Qualifier:
Amino Acid Motifs / genetics
Catalysis
Catalytic Domain / genetics
Hydrolysis
Metals / chemistry,  metabolism
Models, Molecular*
Mutagenesis, Site-Directed
Mutation, Missense
Phosphoric Monoester Hydrolases / chemistry*,  genetics,  metabolism
Phosphorylcholine / chemistry,  metabolism
Pseudomonas aeruginosa / enzymology*,  genetics,  pathogenicity
Transferases (Other Substituted Phosphate Groups) / chemistry,  genetics,  metabolism
Chemical
Reg. No./Substance:
0/Metals; 107-73-3/Phosphorylcholine; EC 2.7.8.-/Transferases (Other Substituted Phosphate Groups); EC 2.7.8.-/sphingomyelin synthase, Pseudomonas aeruginosa; EC 3.1.3.-/Phosphoric Monoester Hydrolases

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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