about
Characterisation of the organophosphate hydrolase catalytic activity of SsoPoxMolecular Engineering of Organophosphate Hydrolysis Activity from a Weak Promiscuous Lactonase TemplateDirected evolution of an extremely fast phosphotriesterase by in vitro compartmentalization.The role of nonbonded interactions in the conformational dynamics of organophosphorous hydrolase adsorbed onto functionalized mesoporous silica surfaces.Hyperthermophilic phosphotriesterases/lactonases for the environment and human health.Structural determinants for the stereoselective hydrolysis of chiral substrates by phosphotriesteraseCatalytic mechanism and three-dimensional structure of adenine deaminase.Structural basis of α-catenin recognition by EspB from enterohaemorrhagic E. coli based on hybrid strategy using low-resolution structural and protein dissection.Enhancing the promiscuous phosphotriesterase activity of a thermostable lactonase (GkaP) for the efficient degradation of organophosphate pesticidesOverexpression, crystallization and preliminary X-ray crystallographic analysis of the phosphotriesterase from Mycobacterium tuberculosisConformational variability of organophosphorus hydrolase upon soman and paraoxon binding.Molecular dynamics simulations of the detoxification of paraoxon catalyzed by phosphotriesterase.Bacterial cell surface display of organophosphorus hydrolase for selective screening of improved hydrolysis of organophosphate nerve agents.Haloalkylphosphorus hydrolases purified from Sphingomonas sp. strain TDK1 and Sphingobium sp. strain TCM1.Cloning of a novel aldo-keto reductase gene from Klebsiella sp. strain F51-1-2 and its functional expression in Escherichia coli.Monitoring enzyme catalysis in the multimeric state: direct observation of Arthrobacter 4-hydroxybenzoyl-coenzyme A thioesterase catalytic complexes using time-resolved electrospray ionization mass spectrometry.Characterization of the zinc-binding site of the histidine-proline-rich glycoprotein associated with rabbit skeletal muscle AMP deaminase.An isofenphos-methyl hydrolase (Imh) capable of hydrolyzing the P-O-Z moiety of organophosphorus pesticides containing an aryl or heterocyclic group.Symmetrical and unsymmetrical dizinc complexes as models for the active sites of hydrolytic enzymes.Stereoselectivity of phosphotriesterase with paraoxon derivatives: a computational study.
P2860
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P2860
description
2000 nî lūn-bûn
@nan
2000 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած
@hyw
2000 թվականի սեպտեմբերին հրատարակված գիտական հոդված
@hy
2000年の論文
@ja
2000年論文
@yue
2000年論文
@zh-hant
2000年論文
@zh-hk
2000年論文
@zh-mo
2000年論文
@zh-tw
2000年论文
@wuu
name
The binding of substrate analogs to phosphotriesterase
@ast
The binding of substrate analogs to phosphotriesterase
@en
The binding of substrate analogs to phosphotriesterase
@nl
type
label
The binding of substrate analogs to phosphotriesterase
@ast
The binding of substrate analogs to phosphotriesterase
@en
The binding of substrate analogs to phosphotriesterase
@nl
prefLabel
The binding of substrate analogs to phosphotriesterase
@ast
The binding of substrate analogs to phosphotriesterase
@en
The binding of substrate analogs to phosphotriesterase
@nl
P2093
P2860
P356
P1476
The binding of substrate analogs to phosphotriesterase
@en
P2093
F M Raushel
H M Holden
M M Benning
P2860
P304
P356
10.1074/JBC.M003852200
P407
P577
2000-09-29T00:00:00Z