Molecular Engineering of Organophosphate Hydrolysis Activity from a Weak Promiscuous Lactonase Template - Test2 - elhamkhani - TriplyDB

Molecular Engineering of Organophosphate Hydrolysis Activity from a Weak Promiscuous Lactonase Template

Molecular Engineering of Organophosphate Hydrolysis Activity from a Weak Promiscuous Lactonase Template

http://www.wikidata.org/entity/Q27679003

about

Switching a newly discovered lactonase into an efficient and thermostable phosphotriesterase by simple double mutations His250Ile/Ile263Trp Structural characterization and function determination of a nonspecific carboxylate esterase from the amidohydrolase superfamily with a promiscuous ability to hydrolyze methylphosphonate esters Active site loop conformation regulates promiscuous activity in a lactonase from Geobacillus kaustophilus HTA426 SacPox from the thermoacidophilic crenarchaeon Sulfolobus acidocaldarius is a proficient lactonase.Expanding the enzyme universe: accessing non-natural reactions by mechanism-guided directed evolution.Function discovery and structural characterization of a methylphosphonate esterase.Functional Trade-Offs in Promiscuous Enzymes Cannot Be Explained by Intrinsic Mutational Robustness of the Native Activity Dynamics and constraints of enzyme evolution.The nature of chemical innovation: new enzymes by evolution.Organophosphate-Hydrolyzing Enzymes as First-Line of Defence Against Nerve Agent-Poisoning: Perspectives and the Road Ahead.Engineering towards nitroreductase functionality in ene-reductase scaffolds.How mutational epistasis impairs predictability in protein evolution and design Rational engineering of a native hyperthermostable lactonase into a broad spectrum phosphotriesterase.Combinatorial evolution of phosphotriesterase toward a robust malathion degrader by hierarchical iteration mutagenesis.Binding modes of phosphotriesterase-like lactonase complexed with δ-nonanoic lactone and paraoxon using molecular dynamics simulations.Stereoselectivity of phosphotriesterase with paraoxon derivatives: a computational study.Evolutionary repurposing of a sulfatase: A new Michaelis complex leads to efficient transition state charge offset Enzyme promiscuity: using the dark side of enzyme specificity in white biotechnology

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P2860

Molecular Engineering of Organophosphate Hydrolysis Activity from a Weak Promiscuous Lactonase Template

http://www.wikidata.org/entity/Q27679003

description

2013 nî lūn-bûn

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2013 թուականի Օգոստոսին հրատարակուած գիտական յօդուած

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2013 թվականի օգոստոսին հրատարակված գիտական հոդված

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2013年の論文

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2013年論文

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2013年論文

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2013年論文

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2013年論文

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2013年論文

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2013年论文

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Molecular Engineering of Organ ...... Promiscuous Lactonase Template

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Molecular Engineering of Organ ...... Promiscuous Lactonase Template

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Molecular Engineering of Organ ...... Promiscuous Lactonase Template

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Molecular Engineering of Organ ...... Promiscuous Lactonase Template

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Journal of the American Chemical Society

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Molecular Engineering of Organ ...... Promiscuous Lactonase Template

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Chengfu Xu

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Monika M Meier

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Nicholas G Fox

http://www.w3.org/2001/XMLSchema#string

Sandra Schlee

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P2860

The binding of substrate analogs to phosphotriesterase

Structural basis for natural lactonase and promiscuous phosphotriesterase activities

Functional Annotation and Three-Dimensional Structure of Dr0930 from Deinococcus radiodurans , a Close Relative of Phosphotriesterase in the Amidohydrolase Superfamily † ‡

Establishing wild-type levels of catalytic activity on natural and artificial ( )8-barrel protein scaffolds

Structure-based and random mutagenesis approaches increase the organophosphate-degrading activity of a phosphotriesterase homologue from Deinococcus radiodurans

Computational redesign of a mononuclear zinc metalloenzyme for organophosphate hydrolysis

Catalytic versatility and backups in enzyme active sites: the case of serum paraoxonase 1

Diminishing returns and tradeoffs constrain the laboratory optimization of an enzyme

Site-directed mutagenesis by overlap extension using the polymerase chain reaction

The 'evolvability' of promiscuous protein functions

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11670-7

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scholarly article

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3092527

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10.1021/JA405911H

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31

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135

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Reinhard Sterner

Chitra Rajendran

Christoph Malisi

David P Barondeau

Frank M Raushel

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2013-08-07T00:00:00Z

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23837603

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organophosphate

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3786566

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