二异丙基氟磷酸酶
二异丙基氟磷酸酶结构式
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常用名 | 二异丙基氟磷酸酶 | 英文名 | Diisopropylfluoro-phosphatase, lyo |
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| CAS号 | 9032-18-2 | 分子量 | N/A | |
| 密度 | N/A | 沸点 | N/A | |
| 分子式 | N/A | 熔点 | N/A | |
| MSDS | 中文版 美版 | 闪点 | N/A |
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Tyrosine-Specific Chemical Modification with in Situ Hemin-Activated Luminol Derivatives.
ACS Chem. Biol. 10 , 2633-40, (2015) Tyrosine-specific chemical modification was achieved using in situ hemin-activated luminol derivatives. Tyrosine residues in peptide and protein were modified effectively with N-methylated luminol derivatives under oxidative conditions in the presence of hemi... |
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Development of a high-throughput screening for nerve agent detoxifying materials using a fully-automated robot-assisted biological assay.
Toxicol. In Vitro 24(3) , 1026-31, (2010) Developing improved medical countermeasures against chemical warfare agents (nerve agents) is urgently needed but time-consuming and costly. Here we introduce a robot-assisted liquid handling system with warming, cooling and incubating facilities to screen th... |
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Inhibitory potency against human acetylcholinesterase and enzymatic hydrolysis of fluorogenic nerve agent mimics by human paraoxonase 1 and squid diisopropyl fluorophosphatase.
Biochemistry 47(18) , 5216-24, (2008) A wide range of toxic organophosphorus pesticides and nerve agents is effectively hydrolyzed by the structurally related phosphotriesterase enzymes paraoxonase (PON1) from human plasma and diisopropyl fluorophosphatase (DFPase) from the squid Loligo vulgaris.... |
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In vitro toxicokinetic studies of cyclosarin: molecular mechanisms of elimination.
Toxicol. Lett. 227(1) , 1-11, (2014) The toxicokinetics of in vitro elimination of highly toxic cyclosarin (GF) in biological systems revealed striking stereoselective differences in the range of 0.01μM to 1mM GF. While weak concentration dependency was detected for elimination of the toxic (-)-... |
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Quantification of hydrolysis of toxic organophosphates and organophosphonates by diisopropyl fluorophosphatase from Loligo vulgaris by in situ Fourier transform infrared spectroscopy.
Anal. Biochem. 385(2) , 187-93, (2009) The enzyme diisopropyl fluorophosphatase (DFPase) from the squid Loligo vulgaris effectively catalyzes the hydrolysis of diisopropyl fluorophosphate (DFP) and a number of organophosphorus nerve agents, including sarin, soman, cyclosarin, and tabun. Up to now,... |
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Preliminary time-of-flight neutron diffraction study on diisopropyl fluorophosphatase (DFPase) from Loligo vulgaris.
Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 63(Pt 1) , 42-5, (2007) The enzyme diisopropyl fluorophosphatase (DFPase) from Loligo vulgaris is capable of decontaminating a wide variety of toxic organophosphorus nerve agents. DFPase is structurally related to a number of enzymes, such as the medically important paraoxonase (PON... |
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Deactivating chemical agents using enzyme-coated nanofibers formed by electrospinning.
ACS Appl. Mater. Interfaces 3(12) , 4633-9, (2011) The coaxial electrospinning technique was investigated as a novel method to create stabilized, enzyme-containing fibers that have the potential to provide enhanced protection from chemical agents. Electrospinning is a versatile technique for the fabrication o... |
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X-ray structure of perdeuterated diisopropyl fluorophosphatase (DFPase): perdeuteration of proteins for neutron diffraction.
Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 66(Pt 4) , 379-85, (2010) The signal-to-noise ratio is one of the limiting factors in neutron macromolecular crystallography. Protein perdeuteration, which replaces all H atoms with deuterium, is a method of improving the signal-to-noise ratio of neutron crystallography experiments by... |
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Hydrolase stabilization via entanglement in poly(propylene sulfide) nanoparticles: stability towards reactive oxygen species.
Nanotechnology 23(29) , 294009, (2012) In the advancement of green syntheses and sustainable reactions, enzymatic biocatalysis offers extremely high reaction rates and selectivity that goes far beyond the reach of chemical catalysts; however, these enzymes suffer from typical environmental constra... |
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Mutational and structural studies of the diisopropylfluorophosphatase from Loligo vulgaris shed new light on the catalytic mechanism of the enzyme.
Biochemistry 44(25) , 9022-33, (2005) The active site, the substrate binding site, and the metal binding sites of the diisopropylfluorophosphatase (DFPase) from Loligo vulgaris have been modified by means of site-directed mutagenesis to improve our understanding of the reaction mechanism. Enzymat... |