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-Reference-Cited by-同舟云学术

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

Published:2008-12 Issue:12 Volume:1784 Page:2038-2044
ISSN:1570-9639
Container-title:Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics
language:en
Short-container-title:Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics

Author:

Beassoni Paola R.,Otero Lisandro H.,Lisa Angela T.,Domenech Carlos E.

Publisher

Elsevier BV

Subject

Molecular Biology,Biochemistry,Biophysics,Analytical Chemistry

Reference28 articles.

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3. Critical active-site residues identified by site-directed mutagenesis in Pseudomonas aeruginosa phosphorylcholine phosphatase, a new member of the haloacid dehalogenases hydrolase superfamily;Beassoni;Curr. Microbiol.,2006

4. Identification, cloning, and expression of Pseudomonas aeruginosa phosphorylcholine phosphatase gene;Massimelli;Curr. Microbiol.,2005

5. Crystal structure of phosphoserine phosphatase from Methanococcus jannaschii, a hyperthermophile, at 1.8Å resolution;Wang;Structure,2001

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