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

Biochimica et Biophysica Acta - Proteins and Proteomics

Volumn 1784, Issue 12, 2008, Pages 2038-2044

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

^a DEPARTAMENTO DE QUÍMICA   (Argentina)

Author keywords

Choline; Metal activation; Phosphorylcholine phosphatase; Pseudomonas aeruginosa

Indexed keywords

4 NITROPHENYLPHOSPHATASE; BACTERIAL PROTEIN; CHOLINE; COPPER; DIVALENT CATION; MAGNESIUM; PHOSPHATE; PHOSPHATIDYLCHOLINE; PHOSPHOLIPASE C; PHOSPHORYLCHOLINE; PHOSPHORYLCHOLINE PHOSPHATASE; SPHINGOMYELIN; UNCLASSIFIED DRUG; ZINC;

ARTICLE; CATALYSIS; ENZYME KINETICS; HYDROLYSIS; MOLECULAR MODEL; NONHUMAN; PATHOGENESIS; PRIORITY JOURNAL; PROTEIN MOTIF; PSEUDOMONAS AERUGINOSA; SITE DIRECTED MUTAGENESIS;

AMINO ACID MOTIFS; CATALYSIS; CATALYTIC DOMAIN; HYDROLYSIS; METALS; MODELS, MOLECULAR; MUTAGENESIS, SITE-DIRECTED; MUTATION, MISSENSE; PHOSPHORIC MONOESTER HYDROLASES; PHOSPHORYLCHOLINE; PSEUDOMONAS AERUGINOSA; TRANSFERASES (OTHER SUBSTITUTED PHOSPHATE GROUPS);

PSEUDOMONAS AERUGINOSA;

EID: 54549099009     PISSN: 15709639     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbapap.2008.08.014     Document Type: Article

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