Structural basis for natural lactonase and promiscuous phosphotriesterase activities - Wikidata - wikimedia - TriplyDB

Structural basis for natural lactonase and promiscuous phosphotriesterase activities

Structural basis for natural lactonase and promiscuous phosphotriesterase activities

http://www.wikidata.org/entity/Q27650637

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Quorum quenching revisited--from signal decays to signalling confusion Functional Annotation and Three-Dimensional Structure of Dr0930 from Deinococcus radiodurans , a Close Relative of Phosphotriesterase in the Amidohydrolase Superfamily † ‡Structural basis for thermostability revealed through the identification and characterization of a highly thermostable phosphotriesterase-like lactonase from Geobacillus stearothermophilus Crystal Structures of Wzb of Escherichia coli and CpsB of Streptococcus pneumoniae, Representatives of Two Families of Tyrosine Phosphatases that Regulate Capsule Assembly Directed Evolution of a Thermostable Quorum-quenching Lactonase from the Amidohydrolase Superfamily Structural and Enzymatic characterization of the lactonase SisLac from Sulfolobus islandicus Characterisation of the organophosphate hydrolase catalytic activity of SsoPox Structural Evidence of a Productive Active Site Architecture for an Evolved Quorum-Quenching GKL Lactonase Molecular Engineering of Organophosphate Hydrolysis Activity from a Weak Promiscuous Lactonase Template Hydrogen atoms in protein structures: high-resolution X-ray diffraction structure of the DFPase Differential active site loop conformations mediate promiscuous activities in the lactonase SsoPox Structural and Enzymatic Characterization of the Phosphotriesterase OPHC2 from Pseudomonas pseudoalcaligenes Switching a newly discovered lactonase into an efficient and thermostable phosphotriesterase by simple double mutations His250Ile/Ile263Trp Harnessing hyperthermostable lactonase from Sulfolobus solfataricus for biotechnological applications Crystallization and preliminary X-ray diffraction analysis of the lactonaseVmoLac fromVulcanisaeta moutnovskia Functional annotation and structural characterization of a novel lactonase hydrolyzing D-xylono-1,4-lactone-5-phosphate and L-arabino-1,4-lactone-5-phosphate.Hyperthermophilic phosphotriesterases/lactonases for the environment and human health.Quorum quenching agents: resources for antivirulence therapy Isolation and characterization of N-acylhomoserine lactonase from the thermophilic bacterium, Geobacillus caldoxylosilyticus YS-8.Isolation of the opdE gene that encodes for a new hydrolase of Enterobacter sp. capable of degrading organophosphorus pesticides.Quorum quenching enzymes and their application in degrading signal molecules to block quorum sensing-dependent infection Crystallization and preliminary X-ray diffraction analysis of the hyperthermophilic Sulfolobus islandicus lactonase.Active site loop conformation regulates promiscuous activity in a lactonase from Geobacillus kaustophilus HTA426 Evolutionary expansion of the amidohydrolase superfamily in bacteria in response to the synthetic compounds molinate and diuron.SacPox from the thermoacidophilic crenarchaeon Sulfolobus acidocaldarius is a proficient lactonase.Catalytic bioscavengers against toxic esters, an alternative approach for prophylaxis and treatments of poisonings.Promiscuity in the Enzymatic Catalysis of Phosphate and Sulfate Transfer.Enhancing the promiscuous phosphotriesterase activity of a thermostable lactonase (GkaP) for the efficient degradation of organophosphate pesticides Overexpression, crystallization and preliminary X-ray crystallographic analysis of the phosphotriesterase from Mycobacterium tuberculosis Carboxylic ester hydrolases from hyperthermophiles.Active Site Hydrophobicity and the Convergent Evolution of Paraoxonase Activity in Structurally Divergent Enzymes: The Case of Serum Paraoxonase 1.Divergence and convergence in enzyme evolution: parallel evolution of paraoxonases from quorum-quenching lactonases Catalytic mechanisms for phosphotriesterases Cometabolic degradation of organic wastewater micropollutants by activated sludge and sludge-inherent microorganisms.Quorum quenching mediated approaches for control of membrane biofouling.Quorum quenching: role in nature and applied developments.Gulosibacter molinativorax ON4T molinate hydrolase, a novel cobalt-dependent amidohydrolase.Current and emerging strategies for organophosphate decontamination: special focus on hyperstable enzymes.The quorum-quenching lactonase from Geobacillus caldoxylosilyticus: purification, characterization, crystallization and crystallographic analysis.Crystallization and preliminary crystallographic analysis of the phosphotriesterase-like lactonase from Geobacillus kaustophilus.

P2860

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P2860

Structural basis for natural lactonase and promiscuous phosphotriesterase activities

http://www.wikidata.org/entity/Q27650637

description

2008 nî lūn-bûn

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2008 թուականի Յունիսին հրատարակուած գիտական յօդուած

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2008 թվականի հունիսին հրատարակված գիտական հոդված

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2008年の論文

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Structural basis for natural lactonase and promiscuous phosphotriesterase activities

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Structural basis for natural lactonase and promiscuous phosphotriesterase activities

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Structural basis for natural lactonase and promiscuous phosphotriesterase activities

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Structural basis for natural lactonase and promiscuous phosphotriesterase activities

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Structural basis for natural lactonase and promiscuous phosphotriesterase activities

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Structural basis for natural lactonase and promiscuous phosphotriesterase activities

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Structural basis for natural lactonase and promiscuous phosphotriesterase activities

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J.JMB.2008.04.022

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Journal of Molecular Biology

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Structural basis for natural lactonase and promiscuous phosphotriesterase activities

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Claude Lecomte

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Daniel Rochu

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Eric Chabriere

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Luigia Merone

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Mosè Rossi

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Sébastien Moniot

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