Transition from octahedral to tetrahedral geometry causes the activation or inhibition by Zn2+ of Pseudomonas aeruginosa phosphorylcholine phosphatase

BioMetals

Volumn 23, Issue 2, 2010, Pages 307-314

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

^a DEPARTAMENTO DE QUÍMICA   (Argentina)

Author keywords

Mg2+; Phosphorylcholine phosphatase; Pseudomonas aeruginosa; Zn2+

Indexed keywords

BACTERIAL ENZYME; MAGNESIUM ION; PHOSPHORYLCHOLINE; PHOSPHORYLCHOLINE PHOSPHATASE; UNCLASSIFIED DRUG; ZINC ION; BACTERIAL PROTEIN; HYDROLASE; PHOSPHORYLCHOLINE HYDROLASE; ZINC;

ARTICLE; BINDING AFFINITY; COMPLEX FORMATION; CONTROLLED STUDY; ENZYME ACTIVATION; ENZYME ACTIVE SITE; ENZYME INHIBITION; ENZYME STRUCTURE; HYDROLYSIS; MOLECULAR MODEL; NONHUMAN; PH; PSEUDOMONAS AERUGINOSA; CHEMICAL STRUCTURE; CHEMISTRY; ENZYMOLOGY; GENETICS; METABOLISM; MOLECULAR DYNAMICS;

PSEUDOMONAS AERUGINOSA;

BACTERIAL PROTEINS; CATALYTIC DOMAIN; HYDROLASES; MODELS, MOLECULAR; MOLECULAR DYNAMICS SIMULATION; PHOSPHORYLCHOLINE; PSEUDOMONAS AERUGINOSA; ZINC;

EID: 77952483738     PISSN: 09660844     EISSN: None     Source Type: Journal    
DOI: 10.1007/s10534-010-9289-1     Document Type: Article

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