The Experts below are selected from a list of 24 Experts worldwide ranked by ideXlab platform
Douglas D Anspaugh - One of the best experts on this subject based on the ideXlab platform.
-
assays for the classification of two types of esterases carboxylic ester hydrolases and phosphoric triester hydrolases
Current protocols in immunology, 2002Co-Authors: Douglas D AnspaughAbstract:Assays for the Classification of Two Types of Esterases: Carboxylic Ester Hydrolase and Phosphoric Triester Hydrolase (Douglas D. Anspaugh and Michael Roe, North Carolina State University, Raleigh, North Carolina). This unit describes assays that quantitate two types of esterase the carboxylic ester hydrolases and the phosphoric triester hydrolases. Carboxylic ester hydrolases include the B-esterases, which are inhibited by organophosphorus compounds. Among the phosphoric triester hydrolases is Aryldialkylphosphatase, which has been called A-esterase or paraoxonase due to its ability to oxidize paraoxon and other organophosphates. These assays are colorimetric and miniaturized for rapid simultaneous testing of multiple, small-volume samples in a microtiter plate format. There is also a discussion of the history of esterase nomenclature and the reasons why this large group of enzymes is so difficult to classify.
Chris Sander - One of the best experts on this subject based on the ideXlab platform.
-
an evolutionary treasure unification of a broad set of amidohydrolases related to urease
Proteins, 1997Co-Authors: Liisa Holm, Chris SanderAbstract:The recent determination of the three-dimensional structure of urease revealed striking similarities of enzyme architecture to adenosine deaminase and phosphotriesterase, evidence of a distant evolutionary relationship that had gone undetected by one-dimensional sequence comparisons. Here, based on an analysis of conservation patterns in three dimensions, we report the discovery of the same active-site architecture in an even larger set of enzymes involved primarily in nucleotide metabolism. As a consequence, we predict the three-dimensional fold and details of the active site architecture for dihydroorotases, allantoinases, hydantoinases, AMP-, adenine and cytosine deaminases, imidazolonepropionase, Aryldialkylphosphatase, chlorohydrolases, formylmethanofuran dehydrogenases, and proteins involved in animal neuronal development. Two member families are common to archaea, eubacteria, and eukaryota. Thirteen other functions supported by the same structural motif and conserved chemical mechanism apparently represent later adaptations for different substrate specificities in different cellular contexts. © 1997 Wiley-Liss Inc.
-
an evolutionary treasure unification of a broad set of amidohydrolases related to urease
Chemtracts, 1997Co-Authors: Liisa Holm, Chris Sander, Thomas TrautAbstract:The recent determination of the three-dimensional structure of urease re- vealed striking similarities of enzyme architec- ture to adenosine deaminase and phosphotries- terase, evidence of a distant evolutionary relationship that had gone undetected by one- dimensional sequence comparisons. Here, based on an analysis of conservation patterns in three dimensions, we report the discovery of the same active-site architecture in an even larger set of enzymes involved primarily in nucleotide metabolism. As a consequence, we predict the three-dimensional fold and details of the active site architecture for dihy- droorotases, allantoinases, hydantoinases, AMP-, adenine and cytosine deaminases, imid- azolonepropionase, Aryldialkylphosphatase, chlorohydrolases, formylmethanofuran dehy- drogenases, and proteins involved in animal neuronal development. Two member families are common to archaea, eubacteria, and eu- karyota. Thirteen other functions supported by the same structural motif and conserved chemi- cal mechanism apparently represent later adap- tations for different substrate specificities in different cellular contexts. Proteins 28:72-82, 1997 r1997 Wiley-Liss, Inc.
Liisa Holm - One of the best experts on this subject based on the ideXlab platform.
-
an evolutionary treasure unification of a broad set of amidohydrolases related to urease
Proteins, 1997Co-Authors: Liisa Holm, Chris SanderAbstract:The recent determination of the three-dimensional structure of urease revealed striking similarities of enzyme architecture to adenosine deaminase and phosphotriesterase, evidence of a distant evolutionary relationship that had gone undetected by one-dimensional sequence comparisons. Here, based on an analysis of conservation patterns in three dimensions, we report the discovery of the same active-site architecture in an even larger set of enzymes involved primarily in nucleotide metabolism. As a consequence, we predict the three-dimensional fold and details of the active site architecture for dihydroorotases, allantoinases, hydantoinases, AMP-, adenine and cytosine deaminases, imidazolonepropionase, Aryldialkylphosphatase, chlorohydrolases, formylmethanofuran dehydrogenases, and proteins involved in animal neuronal development. Two member families are common to archaea, eubacteria, and eukaryota. Thirteen other functions supported by the same structural motif and conserved chemical mechanism apparently represent later adaptations for different substrate specificities in different cellular contexts. © 1997 Wiley-Liss Inc.
-
an evolutionary treasure unification of a broad set of amidohydrolases related to urease
Chemtracts, 1997Co-Authors: Liisa Holm, Chris Sander, Thomas TrautAbstract:The recent determination of the three-dimensional structure of urease re- vealed striking similarities of enzyme architec- ture to adenosine deaminase and phosphotries- terase, evidence of a distant evolutionary relationship that had gone undetected by one- dimensional sequence comparisons. Here, based on an analysis of conservation patterns in three dimensions, we report the discovery of the same active-site architecture in an even larger set of enzymes involved primarily in nucleotide metabolism. As a consequence, we predict the three-dimensional fold and details of the active site architecture for dihy- droorotases, allantoinases, hydantoinases, AMP-, adenine and cytosine deaminases, imid- azolonepropionase, Aryldialkylphosphatase, chlorohydrolases, formylmethanofuran dehy- drogenases, and proteins involved in animal neuronal development. Two member families are common to archaea, eubacteria, and eu- karyota. Thirteen other functions supported by the same structural motif and conserved chemi- cal mechanism apparently represent later adap- tations for different substrate specificities in different cellular contexts. Proteins 28:72-82, 1997 r1997 Wiley-Liss, Inc.
Thomas Traut - One of the best experts on this subject based on the ideXlab platform.
-
an evolutionary treasure unification of a broad set of amidohydrolases related to urease
Chemtracts, 1997Co-Authors: Liisa Holm, Chris Sander, Thomas TrautAbstract:The recent determination of the three-dimensional structure of urease re- vealed striking similarities of enzyme architec- ture to adenosine deaminase and phosphotries- terase, evidence of a distant evolutionary relationship that had gone undetected by one- dimensional sequence comparisons. Here, based on an analysis of conservation patterns in three dimensions, we report the discovery of the same active-site architecture in an even larger set of enzymes involved primarily in nucleotide metabolism. As a consequence, we predict the three-dimensional fold and details of the active site architecture for dihy- droorotases, allantoinases, hydantoinases, AMP-, adenine and cytosine deaminases, imid- azolonepropionase, Aryldialkylphosphatase, chlorohydrolases, formylmethanofuran dehy- drogenases, and proteins involved in animal neuronal development. Two member families are common to archaea, eubacteria, and eu- karyota. Thirteen other functions supported by the same structural motif and conserved chemi- cal mechanism apparently represent later adap- tations for different substrate specificities in different cellular contexts. Proteins 28:72-82, 1997 r1997 Wiley-Liss, Inc.
Meisam Tabatabaei - One of the best experts on this subject based on the ideXlab platform.
-
Kinetic properties of Aryldialkylphosphatase immobilised on chitosan myristic acid nanogel
Chemical Papers, 2015Co-Authors: Seyede Maryam Mesbah Namini, Afshin Mohsenifar, Rezvan Karami, Tavoos Rahmani-cherati, Taha Roodbar, Meisam TabatabaeiAbstract:Organophosphorus (OP) compounds are extensively used in agricultural practice for pest management. However, their residues have a long half-life in the ecosystem as well as in the agro-products, posing a serious threat to human and animal health. Aryldialkylphosphatase (EC 3.1.8.1) is widely used in detoxification procedures. In the present study, Aryldialkylphosphatase was immobilised on synthesised cross-linked nano-sized gel particles, also known as nanogels, in order to enhance the enzyme’s physicochemical properties. Accordingly, a new nanogel consisting of chitosan and myristic acid (CMA nanogel) was synthesised and characterised by way of Fourier transform infrared spectroscopy (FTIR), scanning electron microscopy (SEM) and transmission electron microscopy (TEM). The Aryldialkylphosphatase-CMA nanogel conjugate was then assayed by FTIR, and its physicochemical characteristics were also investigated. The data obtained from SEM and TEM showed the nanogels to be homogenous spherical particles less than 50 nm in diameter. The proper formation of the nanogel and nanobioconjugate was also confirmed by FTIR spectra. In comparison with the free enzyme, the pH and thermal stability of the Aryldialkylphosphatase were enhanced by the covalent immobilisation. Moreover, the immobilised enzyme could maintain approximately half of its activity over more than one month. The kinetic parameters of the Aryldialkylphosphatase-CMA nanogel conjugate were also shown to undergo remarkable improvements, hence the synthesised CMA-nanogel could act as a promising support for Aryldialkylphosphatase immobilisation. It is suggested that the Aryldialkylphosphatase-CMA nanogel could be used for detoxifying paraoxon; a nerve agent. Further clinical experiments are underway.
