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Results 1 - 10 of 13 > >>
EC Number General Information Commentary Reference
Display the word mapDisplay the reaction diagram Show all sequences 3.1.8.2evolution the phosphotriesterase activity development between PON1, EC 3.1.8.1, and DFPase, EC 3.1.8.2, is investigated by using the hybrid density functional theory method B3LYP. Structure comparisons of evolutionarily related enzymes show that the mutation of Asn270 leads to the catalytic Ca2+ ion indirectly connecting the buried structural Ca2+ ion via hydrogen bonds in DFPase. It can reduce the plasticity of enzymatic structure, and possibly change the substrate preference from paraoxon (preferred substrate of PON1) to DFP (preferred substrate of DFPase), which implies an evolutionary transition from mono- to dinuclear catalytic centers, enzyme catalysis mechanism from an evolutionary perspective, overview 751626
Display the word mapDisplay the reaction diagram Show all sequences 3.1.8.2malfunction insufficient organophosphate-hydrolyzing activity of native enzyme affirms the urgent need to develop improved variant(s) having enhanced organophosphate-hydrolyzing activity. Enzyme mutants show altered substrate specificity with increased activity against paraoxon and lactone substrates, overview 749628
Display the word mapDisplay the reaction diagram Show all sequences 3.1.8.2more h-PON1 is a polymorphic enzyme. Molecular docking analysis, homology modelling, overview 749628
Display the word mapDisplay the reaction diagram Show all sequences 3.1.8.2more in detoxification of nerve gas compounds or pesticides in the human body, due to non-human origin of the enzyme, immunological reactions occur when it is injected into body. In order to using DFPase as in vivo detoxifying agent, some manipulations to augment of its efficiency and to decrease of immunogenic problems are needed. Modifications such as PEGylation is one of the possible solutions to conquer these problems 750923
Display the word mapDisplay the reaction diagram Show all sequences 3.1.8.2more organophosphorus hydrolase, OPH, contains a two-oxygen bridging mechanism in the active site suggesting subtle differences compared to organophosphorus acid anhydrolase, OPAA. OPAAs exhibit higher soman activities, whereas OPHs have higher activity against the organophosphorus pesticide paraoxon -, 713896
Display the word mapDisplay the reaction diagram Show all sequences 3.1.8.2more residue Asp229 plays a role in the coordination variation of calcium during the reaction. Quantum mechanical/molecular mechanical umbrella sampling simulations displays that the hydrolysis of diisopropyl fluorophosphate (DFP) and (S)-sarin processes by DFPase presents two different reaction pathways involving nucleophilic attack by Asp229 or an activated water on phosphorus. Modeling of active site and reaction mechanism with nucleophile Asp229 and coordinating Ca2+, detailed overview. Optimized geometries for the intermediates, transition state, and product for the hydrolysis step of DFPase 752291, 755573
Display the word mapDisplay the reaction diagram Show all sequences 3.1.8.2more the metal-substituted catalysts generates the activated water molecules that initiate nucleophilic attack on the phosphorus atom of the substrate, resulting in the cleavage of phosphoester bond and the release of leaving group 751964
Display the word mapDisplay the reaction diagram Show all sequences 3.1.8.2more the OPAA structure is composed of two domains, amino and carboxy domains, with the latter exhibiting a pita bread architecture and harboring the active site with the binuclear Mn2+ ions. The native enzyme structure reveals the presence of a well-defined nonproteinaceous density in the active site, which might be due to a bound glycolate, which is isosteric with a glycine product. All three glycolate oxygens coordinate the two Mn2+ atoms -, 707530
Display the word mapDisplay the reaction diagram Show all sequences 3.1.8.2more the phosphotriesterase diisopropyl fluorophosphatase (DFPase) is a calcium-dependent beta-propeller protein. PON1, EC 3.1.8.1, and DFPase, EC 3.1.8.2, seem to employ similar catalytic mechanisms as phosphotriesterase, due to their structural similarities of active sites. The attacking nucleophile for phosphotriester hydrolysis is identified to be an activated water molecule, with the nucleophile attacking the phosphorus center. The E53Q and D269N mutants in PON1 both possess measurable lactonase and paraoxonase activity, and mutation studies combined with related molecular dynamics simulations suggest that the water activated by Glu53 and Asp269 is the most likely attacking nucleophile. Analysis of the rate-determining reaction step of the organophosphorus compound hydrolysis catalyzed both by DFPase and PON1. Structure-function relationship, overview. Active site structure of DFPase (PDB ID 2GVW) and substrate docking 751626
Display the word mapDisplay the reaction diagram Show all sequences 3.1.8.2physiological function diisopropyl fluorophosphatase is a calcium-dependent phosphotriesterase that acts on a variety of highly toxic organophosphorus compounds, that act as inhibitors of acetylcholinesterase 713615
Results 1 - 10 of 13 > >>