In crystallo capture of a Michaelis complex and product-binding modes of a bacterial phosphotriesterase*
Date
2008
Authors
Jackson, Colin
Foo, Jee
Kim, Hye-Kyung
Carr, Paul D
Liu, Jian-Wei
Salem, Geoffrey
Ollis, David
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Volume Title
Publisher
Elsevier
Abstract
The mechanism by which the binuclear metallophosphotriesterases (PTEs, E.C. 3.1.8.1) catalyse substrate hydrolysis has been extensively studied. The μ-hydroxo bridge between the metal ions has been proposed to be the initiating nucleophile in the hydroly
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Keywords
Keywords: bacterial enzyme; metal ion; phosphotriesterase; article; catalysis; crystallography; enzyme activity; enzyme binding; hydrolysis; Michaelis constant; molecular dynamics; nonhuman; priority journal; proteomics; Amino Acid Sequence; Amino Acids, Aromatic; µ-hydroxo bridge; binuclear metal centre; general base; Michaelis complex; phosphotriesterase
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Source
Journal of Molecular Biology
Type
Journal article
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2037-12-31
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