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Please use this identifier to cite or link to this item: http://dspace.utalca.cl/handle/1950/8812

Title: Site-directed mutations and kinetic studies show key residues involved in alkylammonium interactions and reveal two sites for phosphorylcholine in Pseudomonas aeruginosa phosphorylcholine phosphatase
Authors: Beassoni, P.R.
Otero, L.H.
Boetsch, C.
Domenech, C.E.
Gonzalez-Nilo, F.D.
Lisa, A.T.
Keywords: Pseudomonas aeruginosa
Phosphorylcholine
Choline
Site-directed mutagenesis
HAD superfamily
Substrate inhibition
Issue Date: Jul-2011
Publisher: ELSEVIER SCIENCE BV, PO BOX 211
Citation: BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS Volume: 1814 Issue: 7 Pages: 858-863 DOI: 10.1016/j.bbapap.2011.04.003
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. (C) 2011 Elsevier B.V. All rights reserved.
Description: Gonzalez-Nilo, FD (Gonzalez-Nilo, Fernado D.)Univ Talca, Ctr Bioinformat & Simulac Mol, Talca, Chile
URI: http://dspace.utalca.cl/handle/1950/8812
ISSN: 1570-9639
Appears in Collections:Artículos en publicaciones ISI - Universidad de Talca

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