A class of enzymes that catalyze the hydrolysis of one of the three ester bonds in a phosphotriester-containing compound.
Any member of the class of enzymes that catalyze the cleavage of the substrate and the addition of water to the resulting molecules, e.g., ESTERASES, glycosidases (GLYCOSIDE HYDROLASES), lipases, NUCLEOTIDASES, peptidases (PEPTIDE HYDROLASES), and phosphatases (PHOSPHORIC MONOESTER HYDROLASES). EC 3.
"Esters are organic compounds that result from the reaction between an alcohol and a carboxylic acid, playing significant roles in various biological processes and often used in pharmaceutical synthesis."
Compounds containing carbon-phosphorus bonds in which the phosphorus component is also bonded to one or more sulfur atoms. Many of these compounds function as CHOLINERGIC AGENTS and as INSECTICIDES.
Substances used for the detection, identification, analysis, etc. of chemical, biological, or pathologic processes or conditions. Indicators are substances that change in physical appearance, e.g., color, at or approaching the endpoint of a chemical titration, e.g., on the passage between acidity and alkalinity. Reagents are substances used for the detection or determination of another substance by chemical or microscopical means, especially analysis. Types of reagents are precipitants, solvents, oxidizers, reducers, fluxes, and colorimetric reagents. (From Grant & Hackh's Chemical Dictionary, 5th ed, p301, p499)

Role of calcium ions in the structure and function of the di-isopropylfluorophosphatase from Loligo vulgaris. (1/47)

Di-isopropylfluorophosphatase (DFPase) is shown to contain two high-affinity Ca(2+)-binding sites, which are required for catalytic activity and stability. Incubation with chelating agents results in the irreversible inactivation of DFPase. From titrations with Quin 2 [2-([2-[bis(carboxymethyl)amino]-5-methylphenoxy]-methyl)-6-methoxy-8-[bis(carbox ymethyl)-amino]quinoline], a lower-affinity site with dissociation constants of 21 and 840 nM in the absence and the presence of 150 mM KCl respectively was calculated. The higher-affinity site was not accessible, indicating a dissociation constant of less than 5.3 nM. Stopped-flow experiments have shown that the dissociation of bound Ca(2+) occurs in two phases, with rates of approx. 1.1 and 0.026 s(-1) corresponding to the dissociation from the low-affinity and high-affinity sites respectively. Dissociation rates depend strongly on temperature but not on ionic strength, indicating that Ca(2+) dissociation is connected with conformational changes. Limited proteolysis, CD spectroscopy, dynamic light scattering and the binding of 8-anilino-1-naphthalenesulphonic acid have been combined to give a detailed picture of the conformational changes induced on the removal of Ca(2+) from DFPase. The Ca(2+) dissociation is shown to result in a primary, at least partly reversible, step characterized by a large decrease in DFPase activity and some changes in enzyme structure and shape. This step is followed by an irreversible denaturation and aggregation of the apo-enzyme. From the temperature dependence of Ca(2+) dissociation and the denaturation results we conclude that the higher-affinity Ca(2+) site is required for stabilizing DFPase's structure, whereas the lower-affinity site is likely to fulfil a catalytic function.  (+info)

Insights into the reaction mechanism of the diisopropyl fluorophosphatase from Loligo vulgaris by means of kinetic studies, chemical modification and site-directed mutagenesis. (2/47)

Kinetic measurements, chemical modification and site-directed mutagenesis have been employed to gain deeper insights into the reaction mechanism of the diisopropyl fluorophosphatase (DFPase) from Loligo vulgaris. Analysis of the kinetics of diisopropyl fluorophosphate hydrolysis reveals optimal enzyme activity at pH >/=8, 35 degrees C and an ionic strength of 500 mM NaCl, where k(cat) reaches a limiting value of 526 s(-1). The pH rate profile shows that full catalytic activity requires the deprotonation of an ionizable group with an apparent pK(a) of 6.82, DeltaH(ion) of 42 kJ/mol and DeltaS(ion) of 9.8 J/mol K at 25 degrees C. Chemical modification of aspartate, glutamate, cysteine, arginine, lysine and tyrosine residues indicates that these amino acids are not critical for catalysis. None of the six histidine residues present in DFPase reacts with diethyl pyrocarbonate (DEPC), suggesting that DEPC has no accessibility to the histidines. Therefore, all six histidine residues have been individually replaced by asparagine in order to identify residues participating in catalysis. Only substitution of H287 renders the enzyme catalytically almost inactive with a residual activity of approx. 4% compared to wild-type DFPase. The other histidine residues do not significantly influence the enzymatic activity, but H181 and H274 seem to have a stabilizing function. These results are indicative of a catalytic mechanism in which H287 acts as a general base catalyst activating a nucleophilic water molecule by the abstraction of a proton.  (+info)

Crystal structure of diisopropylfluorophosphatase from Loligo vulgaris. (3/47)

BACKGROUND: Phosphotriesterases (PTE) are enzymes capable of detoxifying organophosphate-based chemical warfare agents by hydrolysis. One subclass of these enzymes comprises the family of diisopropylfluorophosphatases (DFPases). The DFPase reported here was originally isolated from squid head ganglion of Loligo vulgaris and can be characterized as squid-type DFPase. It is capable of hydrolyzing the organophosphates diisopropylfluorophosphate, soman, sarin, tabun, and cyclosarin. RESULTS: Crystals were grown of both the native and the selenomethionine-labeled enzyme. The X-ray crystal structure of the DFPase from Loligo vulgaris has been solved by MAD phasing and refined to a crystallographic R value of 17.6% at a final resolution of 1.8 A. Using site-directed mutagenesis, we have structurally and functionally characterized essential residues in the active site of the enzyme. CONCLUSIONS: The crystal structure of the DFPase from Loligo vulgaris is the first example of a structural characterization of a squid-type DFPase and the second crystal structure of a PTE determined to date. Therefore, it may serve as a structural model for squid-type DFPases in general. The overall structure of this protein represents a six-fold beta propeller with two calcium ions bound in a central water-filled tunnel. The consensus motif found in the blades of this beta propeller has not yet been observed in other beta propeller structures. Based on the results obtained from mutants of active-site residues, a mechanistic model for the DFP hydrolysis has been developed.  (+info)

Evolution of an organophosphate-degrading enzyme: a comparison of natural and directed evolution. (4/47)

Organophosphate-degrading enzyme from Agrobacterium radiobacter P230 (OPDA) is a recently discovered enzyme that degrades a broad range of organophosphates. It is very similar to OPH first isolated from Pseudomonas diminuta MG. Despite a high level of sequence identity, OPH and OPDA exhibit different substrate specificities. We report here the structure of OPDA and identify regions of the protein that are likely to give it a preference for substrates that have shorter alkyl substituents. Directed evolution was used to evolve a series of OPH mutants that had activities similar to those of OPDA. Mutants were selected for on the basis of their ability to degrade a number of substrates. The mutations tended to cluster in particular regions of the protein and in most cases, these regions were where OPH and OPDA had significant differences in their sequences.  (+info)

Trypsin revisited: crystallography AT (SUB) atomic resolution and quantum chemistry revealing details of catalysis. (5/47)

A series of crystal structures of trypsin, containing either an autoproteolytic cleaved peptide fragment or a covalently bound inhibitor, were determined at atomic and ultra-high resolution and subjected to ab initio quantum chemical calculations and multipole refinement. Quantum chemical calculations reproduced the observed active site crystal structure with severe deviations from standard stereochemistry and indicated the protonation state of the catalytic residues. Multipole refinement directly revealed the charge distribution in the active site and proved the validity of the ab initio calculations. The combined results confirmed the catalytic function of the active site residues and the two water molecules acting as the nucleophile and the proton donor. The crystal structures represent snapshots from the reaction pathway, close to a tetrahedral intermediate. The de-acylation of trypsin then occurs in true SN2 fashion.  (+info)

Growth of Escherichia coli coexpressing phosphotriesterase and glycerophosphodiester phosphodiesterase, using paraoxon as the sole phosphorus source. (6/47)

Phosphotriesterases catalyze the hydrolytic detoxification of phosphotriester pesticides and chemical warfare nerve agents with various efficiencies. The directed evolution of phosphotriesterases to enhance the breakdown of poor substrates is desirable for the purposes of bioremediation. A limiting factor in the identification of phosphotriesterase mutants with increased activity is the ability to effectively screen large mutant libraries. To this end, we have investigated the possibility of coupling phosphotriesterase activity to cell growth by using methyl paraoxon as the sole phosphorus source. The catabolism of paraoxon to phosphate would occur via the stepwise enzymatic hydrolysis of paraoxon to dimethyl phosphate, methyl phosphate, and then phosphate. The Escherichia coli strain DH10B expressing the phosphotriesterase from Agrobacterium radiobacter P230 (OpdA) is unable to grow when paraoxon is used as the sole phosphorus source. Enterobacter aerogenes is an organism capable of growing when dimethyl phosphate is the sole phosphorus source. The enzyme responsible for hydrolyzing dimethyl phosphate has been previously characterized as a nonspecific phosphohydrolase. We isolated and characterized the genes encoding the phosphohydrolase operon. The operon was identified from a shotgun clone that enabled E. coli to grow when dimethyl phosphate is the sole phosphorus source. E. coli coexpressing the phosphohydrolase and OpdA grew when paraoxon was the sole phosphorus source. By constructing a short degradative pathway, we have enabled E. coli to use phosphotriesters as a sole source of phosphorus.  (+info)

Contribution of the active-site metal cation to the catalytic activity and to the conformational stability of phosphotriesterase: temperature- and pH-dependence. (7/47)

Phosphotriesterase (PTE) detoxifies nerve agents and organophosphate pesticides. The two zinc cations of the PTE active centre can be substituted by other transition metal cations without loss of activity. Furthermore, metal-substituted PTEs display differences in catalytic properties. A prerequisite for engineering highly efficient mutants of PTE is to improve their thermostability. Isoelectric focusing, capillary electrophoresis and steady-state kinetics analysis were used to determine the contribution of the active-site cations Zn2+, Co2+ or Cd2+ to both the catalytic activity and the conformational stability of the corresponding PTE isoforms. The three isoforms have different pI values (7.2, 7.5 and 7.1) and showed non-superimposable electrophoretic titration curves. The overall structural alterations, causing changes in functional properties, were found to be related to the nature of the bound cation: ionic radius and ion electronegativity correlate with Km and kcat respectively. In addition, the pH-dependent activity profiles of isoforms were different. The temperature-dependent profiles of activity showed maximum activity at T < or =35 degrees C, followed by an activation phase near 45-48 degrees C and then inactivation which was completed at 60 degrees C. Analysis of thermal denaturation of the PTEs provided evidence that the activation phase resulted from a transient intermediate. Finally, at the optimum activity between pH 8 and 9.4, the thermostability of the different PTEs increased as the pH decreased, and the metal cation modulated stability (Zn2+-, Co2+- and Cd2+-PTE showed different T (m) values of 60.5-67 degrees C, 58-64 degrees C and 53-64 degrees C respectively). Requirements for optimum activity of PTE (displayed by Co2+-PTE) and maximum stability (displayed by Zn2+-PTE) were demonstrated.  (+info)

Structure/function analyses of human serum paraoxonase (HuPON1) mutants designed from a DFPase-like homology model. (8/47)

Human serum paraoxonase (HuPON1) is a calcium-dependent enzyme that hydrolyzes esters, including organophosphates and lactones, and exhibits anti-atherogenic properties. A few amino acids have been shown to be essential for the enzyme's arylesterase and organophosphatase activities. Until very recently, a three-dimensional model was not available for HuPON1, so functional roles have not been assigned to those residues. Based on sequence-structure alignment studies, we have folded the amino acid sequence of HuPON1 onto the sixfold beta-propeller structure of squid diisopropylfluorophosphatase (DFPase). We tested the validity of this homology model by circular dichroism (CD) spectroscopy and site-directed mutagenesis. Consistent with predictions from the homology model, CD data indicated that the structural composition of purified HuPON1 consists mainly of beta-sheets. Mutants of HuPON1 were assayed for enzymatic activity against phenyl acetate and paraoxon. Substitution of residues predicted to be important for substrate binding (L69, H134, F222, and C284), calcium ion coordination (D54, N168, N224, and D269), and catalytic mechanism of HuPON1 (H285) led to enzyme inactivation. Mutants F222Y and H115W exhibited substrate-binding selectivity towards phenyl acetate and paraoxon, respectively. The homology model presented here is very similar to the recently obtained PON1 crystal structure, and has allowed identification of several residues within the enzyme active site.  (+info)

Phosphoric triester hydrolases are a class of enzymes that catalyze the hydrolysis of phosphoric triesters into corresponding alcohols and phosphates. These enzymes play a crucial role in the detoxification of organophosphate pesticides and nerve agents, as well as in the metabolism of various endogenous compounds.

The term "phosphoric triester hydrolases" is often used interchangeably with "phosphotriesterases" or "organophosphorus hydrolases." These enzymes are characterized by their ability to cleave the P-O-C bond in phosphoric triesters, releasing a free alcohol and a diethyl phosphate moiety.

Phosphoric triester hydrolases have attracted significant interest due to their potential applications in bioremediation, biosensors, and therapeutics. However, it is important to note that the specificity and efficiency of these enzymes can vary widely depending on the structure and properties of the target compounds.

Hydrolases are a class of enzymes that help facilitate the breakdown of various types of chemical bonds through a process called hydrolysis, which involves the addition of water. These enzymes catalyze the cleavage of bonds in substrates by adding a molecule of water, leading to the formation of two or more smaller molecules.

Hydrolases play a crucial role in many biological processes, including digestion, metabolism, and detoxification. They can act on a wide range of substrates, such as proteins, lipids, carbohydrates, and nucleic acids, breaking them down into smaller units that can be more easily absorbed or utilized by the body.

Examples of hydrolases include:

1. Proteases: enzymes that break down proteins into smaller peptides or amino acids.
2. Lipases: enzymes that hydrolyze lipids, such as triglycerides, into fatty acids and glycerol.
3. Amylases: enzymes that break down complex carbohydrates, like starches, into simpler sugars, such as glucose.
4. Nucleases: enzymes that cleave nucleic acids, such as DNA or RNA, into smaller nucleotides or oligonucleotides.
5. Phosphatases: enzymes that remove phosphate groups from various substrates, including proteins and lipids.
6. Esterases: enzymes that hydrolyze ester bonds in a variety of substrates, such as those found in some drugs or neurotransmitters.

Hydrolases are essential for maintaining proper cellular function and homeostasis, and their dysregulation can contribute to various diseases and disorders.

Esters are organic compounds that are formed by the reaction between an alcohol and a carboxylic acid. They are widely found in nature and are used in various industries, including the production of perfumes, flavors, and pharmaceuticals. In the context of medical definitions, esters may be mentioned in relation to their use as excipients in medications or in discussions of organic chemistry and biochemistry. Esters can also be found in various natural substances such as fats and oils, which are triesters of glycerol and fatty acids.

Organothiophosphorus compounds are a class of chemical compounds that contain carbon (organo-) and thiophosphorus bonds. Thiophosphorus refers to a phosphorus atom bonded to one or more sulfur atoms. These compounds have various applications, including use as plasticizers, flame retardants, insecticides (such as malathion and parathion), and nerve agents (such as sarin and VX). They can be synthesized through the reaction of organolithium or Grignard reagents with thiophosphoryl chloride. The general structure of these compounds is R-P(=S)Y, where R is an organic group, P is phosphorus, and Y is a group that determines the properties and reactivity of the compound.

Indicators and reagents are terms commonly used in the field of clinical chemistry and laboratory medicine. Here are their definitions:

1. Indicator: An indicator is a substance that changes its color or other physical properties in response to a chemical change, such as a change in pH, oxidation-reduction potential, or the presence of a particular ion or molecule. Indicators are often used in laboratory tests to monitor or signal the progress of a reaction or to indicate the end point of a titration. A familiar example is the use of phenolphthalein as a pH indicator in acid-base titrations, which turns pink in basic solutions and colorless in acidic solutions.

2. Reagent: A reagent is a substance that is added to a system (such as a sample or a reaction mixture) to bring about a chemical reaction, test for the presence or absence of a particular component, or measure the concentration of a specific analyte. Reagents are typically chemicals with well-defined and consistent properties, allowing them to be used reliably in analytical procedures. Examples of reagents include enzymes, antibodies, dyes, metal ions, and organic compounds. In laboratory settings, reagents are often prepared and standardized according to strict protocols to ensure their quality and performance in diagnostic tests and research applications.

... phosphoric triester hydrolases MeSH D08.811.277.352.660.500 - aryldialkylphosphatase MeSH D08.811.277.352.700 - ribonucleases ... phosphoric diester hydrolases MeSH D08.811.277.352.640.050 - annexin A3 MeSH D08.811.277.352.640.125 - 3',5'-cyclic-GMP ... phosphoric monoester hydrolases MeSH D08.811.277.352.650.025 - acid phosphatase MeSH D08.811.277.352.650.035 - alkaline ... thiolester hydrolases MeSH D08.811.277.352.897.075 - acetyl-CoA hydrolase MeSH D08.811.277.352.897.700 - palmitoyl-coa ...
... fluoride This enzyme belongs to the family of hydrolases, specifically those acting on ester bonds phosphoric-triester ... diisopropyl phosphorofluoridate hydrolase, isopropylphosphorofluoridase, and diisopropylfluorophosphonate dehalogenase. It ... hydrolases. The systematic name is diisopropyl-fluorophosphate fluorohydrolase. Other names in common use include DFPase, ...
... (EC 3.1.8.1, also known as phosphotriesterase, organophosphate hydrolase, parathion hydrolase, ... The products of the reaction are diethyl phosphoric acid and p-nitrophenol. The latter product is further degraded by an enzyme ... It acts specifically on synthetic organophosphate triesters and phosphorofluoridates. It does not seem to have a natural ... This enzyme is homologous to hydrolases in Pseudomonas putida, Pseudomonas azelaica, Rhodococcus sp., and P. fluorescens. ...
Sulfuric ester hydrolases (sulfatases) EC 3.1.7: Diphosphoric monoester hydrolases EC 3.1.8: Phosphoric triester hydrolases ... Thiolester hydrolases Thioesterase Ubiquitin carboxy-terminal hydrolase L1 EC 3.1.3: Phosphoric monoester hydrolases ... Phosphoric diester hydrolases EC 3.1.5: Triphosphoric monoester hydrolases EC 3.1.6: ... An esterase is a hydrolase enzyme that splits esters into an acid and an alcohol in a chemical reaction with water called ...
... phosphoric triester hydrolases MeSH D08.811.277.352.660.500 - aryldialkylphosphatase MeSH D08.811.277.352.700 - ribonucleases ... phosphoric diester hydrolases MeSH D08.811.277.352.640.050 - annexin A3 MeSH D08.811.277.352.640.125 - 3,5-cyclic-GMP ... phosphoric monoester hydrolases MeSH D08.811.277.352.650.025 - acid phosphatase MeSH D08.811.277.352.650.035 - alkaline ... thiolester hydrolases MeSH D08.811.277.352.897.075 - acetyl-CoA hydrolase MeSH D08.811.277.352.897.700 - palmitoyl-coa ...
phosphoric triester hydrolase activity GO:0016795 * calcium-transporting ATPase activity GO:0005388 ...
trans-permethrin hydrolase activity GO:0102209 * phosphoric triester hydrolase activity GO:0016795 ...
Hidrolases de Triester Fosfórico. Phosphoric Triester Hydrolases. Hidrolasas de Triéster Fosfórico. L-Lactato Desidrogenase ( ...
Phosphoric Triester Hydrolases. Hidrolases de Triester Fosfórico. L-Lactato Deshidrogenasa (Citocromo). L-Lactate Dehydrogenase ...
Phosphoric Triester Hydrolases. Hidrolases de Triester Fosfórico. L-Lactato Deshidrogenasa (Citocromo). L-Lactate Dehydrogenase ...
Phosphoric Triester Hydrolases. Hidrolases de Triester Fosfórico. L-Lactato Deshidrogenasa (Citocromo). L-Lactate Dehydrogenase ...
Phosphoric Triester Hydrolases. Hidrolases de Triester Fosfórico. Hidrolasas de Triéster Fosfórico. Photosynthetic Reaction ...
Hidrolases de Triester Fosfórico. Phosphoric Triester Hydrolases. Hidrolasas de Triéster Fosfórico. L-Lactato Desidrogenase ( ...
Hidrolases de Triester Fosfórico. Phosphoric Triester Hydrolases. Hidrolasas de Triéster Fosfórico. L-Lactato Desidrogenase ( ...
Phosphoric Triester Hydrolases. Hidrolases de Triester Fosfórico. Hidrolasas de Triéster Fosfórico. Photosynthetic Reaction ...
Phosphoric Triester Hydrolases. Hidrolases de Triester Fosfórico. L-Lactato Deshidrogenasa (Citocromo). L-Lactate Dehydrogenase ...
Phosphoric Triester Hydrolases. Hidrolases de Triester Fosfórico. Hidrolasas de Triéster Fosfórico. Photosynthetic Reaction ...
Phosphoric Triester Hydrolases. Hidrolases de Triester Fosfórico. L-Lactato Deshidrogenasa (Citocromo). L-Lactate Dehydrogenase ...
Phosphoric Triester Hydrolases. Hidrolases de Triester Fosfórico. Hidrolasas de Triéster Fosfórico. Photosynthetic Reaction ...
Phosphoric Triester Hydrolases. Hidrolases de Triester Fosfórico. Hidrolasas de Triéster Fosfórico. Photosynthetic Reaction ...
Phosphoric Diester Hydrolases. *Phosphoric Monoester Hydrolases. *Phosphoric Triester Hydrolases. *Ribonucleases. *Sulfatases. ... "Phosphoric Diester Hydrolases" by people in this website by year, and whether "Phosphoric Diester Hydrolases" was a major or ... "Phosphoric Diester Hydrolases" is a descriptor in the National Library of Medicines controlled vocabulary thesaurus, MeSH ( ... Below are the most recent publications written about "Phosphoric Diester Hydrolases" by people in Profiles. ...
Phosphoric Diester Hydrolases. *Phosphoric Monoester Hydrolases. *Phosphoric Triester Hydrolases. *Ribonucleases. *Sulfatases. ... "Phosphoric Monoester Hydrolases" by people in this website by year, and whether "Phosphoric Monoester Hydrolases" was a major ... "Phosphoric Monoester Hydrolases" is a descriptor in the National Library of Medicines controlled vocabulary thesaurus, MeSH ( ... Below are the most recent publications written about "Phosphoric Monoester Hydrolases" by people in Profiles. ...
Phosphoric Diester Hydrolases. *Phosphoric Monoester Hydrolases. *Phosphoric Triester Hydrolases. *Ribonucleases. *Sulfatases. ...
Phosphoric Triester Hydrolases / pharmacology Actions. * Search in PubMed * Search in MeSH * Add to Search ...
Phosphoric Triester Hydrolases Entry term(s). Hydrolases, Phosphoric Triester Phosphotriesterase Triester Hydrolases, ... Phosphoric triester hydrolases Entry term(s):. Hydrolases, Phosphoric Triester. Phosphotriesterase. Triester Hydrolases, ... Phosphoric Triester Hydrolases - Preferred Concept UI. M0444858. Scope note. A class of enzymes that catalyze the hydrolysis of ... 2004; PHOSPHOTRIESTERASE was indexed under ESTERASES 1994-2003; PHOSPHORIC MONOESTER HYRDOLASES 1990-1993; PHOSPHOMONOESTERASES ...
Phosphoric Monoester Hydrolases [D08.811.277.352.650] * Phosphoric Triester Hydrolases [D08.811.277.352.660] * ... Phosphoric Triester Hydrolases Preferred Term Term UI T530598. Date01/21/2003. LexicalTag NON. ThesaurusID NLM (2004). ... Phosphoric Triester Hydrolases Preferred Concept UI. M0444858. Registry Number. EC 3.1.8.-. Scope Note. A class of enzymes that ... Phosphoric Triester Hydrolases. Tree Number(s). D08.811.277.352.660. Unique ID. D044345. RDF Unique Identifier. http://id.nlm. ...
Phosphoric Monoester Hydrolases [D08.811.277.352.650] * Phosphoric Triester Hydrolases [D08.811.277.352.660] * ... Phosphoric Triester Hydrolases Preferred Term Term UI T530598. Date01/21/2003. LexicalTag NON. ThesaurusID NLM (2004). ... Phosphoric Triester Hydrolases Preferred Concept UI. M0444858. Registry Number. EC 3.1.8.-. Scope Note. A class of enzymes that ... Phosphoric Triester Hydrolases. Tree Number(s). D08.811.277.352.660. Unique ID. D044345. RDF Unique Identifier. http://id.nlm. ...
Phosphoric Triester Hydrolases. A class of enzymes that catalyze the hydrolysis of one of the three ester bonds in a ... Anhydrase IISelenomethionineCalixarenesUrate OxidaseProtonsSolventsCoordination ComplexesPhosphoric Triester HydrolasesHeme ... SpectroscopyMass SpectrometrySolventsCoordination ComplexesThermotoga maritimaCircular DichroismPhosphoric Triester Hydrolases ...
Transporting ATPases N0000170667 DNA Transposable Elements N0000010540 Tea Tree Oil N0000167660 Phosphoric Triester Hydrolases ... gamma-Glutamyl Hydrolase N0000167609 Acetyl-CoA Hydrolase N0000167611 Palmitoyl-CoA Hydrolase N0000167672 Allophanate Hydrolase ... Glycoside Hydrolases N0000167599 Epoxide Hydrolases N0000167608 Thiolester Hydrolases N0000167732 N-Glycosyl Hydrolases ... Murine-Derived N0000167640 Phosphoric Monoester Hydrolases N0000179592 Doxycycline Monohydrate N0000179661 Cephalexin ...
Hidrolases de Triester Fosfórico. Phosphoric Triester Hydrolases. Hidrolasas de Triéster Fosfórico. L-Lactato Desidrogenase ( ...
HN - 2004; use PHOSPHODIESTERASE I (NM) 1980-2003 MH - Phosphoric Triester Hydrolases UI - D044345 MN - D8.811.277.352.660 MS ... The enzyme was formerly classified as a phosphoric diester hydrolase (EC 3.1.4.10) and is often referred to as a PHOSPHOLIPASE ... A phosphoric diester hydrolase that removes 5-nucleotides from the 3-hydroxy termini of 3-hydroxy-terminated ... Agents include phosphoric or other acids (ACID ETCHING, DENTAL) and methods include LASERS. AN - coord with agent or method HN ...
Hidrolases de Triester Fosfórico. Phosphoric Triester Hydrolases. Hidrolasas de Triéster Fosfórico. L-Lactato Desidrogenase ( ...
Hidrolases de Triester Fosfórico. Phosphoric Triester Hydrolases. Hidrolasas de Triéster Fosfórico. L-Lactato Desidrogenase ( ...
Phosphoric Triester Hydrolases. Hidrolases de Triester Fosfórico. Hidrolasas de Triéster Fosfórico. Photosynthetic Reaction ...
Phosphoric Triester Hydrolases. Hidrolases de Triester Fosfórico. Hidrolasas de Triéster Fosfórico. Photosynthetic Reaction ...
Hidrolases de Triester Fosfórico. Phosphoric Triester Hydrolases. Hidrolasas de Triéster Fosfórico. L-Lactato Desidrogenase ( ...
Hidrolases de Triester Fosfórico. Phosphoric Triester Hydrolases. Hidrolasas de Triéster Fosfórico. L-Lactato Desidrogenase ( ...
Hidrolases de Triester Fosfórico. Phosphoric Triester Hydrolases. Hidrolasas de Triéster Fosfórico. L-Lactato Desidrogenase ( ...
Hidrolases de Triester Fosfórico. Phosphoric Triester Hydrolases. Hidrolasas de Triéster Fosfórico. L-Lactato Desidrogenase ( ...
Hidrolases de Triester Fosfórico. Phosphoric Triester Hydrolases. Hidrolasas de Triéster Fosfórico. L-Lactato Desidrogenase ( ...
Phosphoric Diester Hydrolases. *Phosphoric Monoester Hydrolases. *Phosphoric Triester Hydrolases. *Ribonucleases. *Sulfatases. ...
Calvo, K.C.; Moore, R.; Koser, G.F. 1998: Hydrolysis of bis-ketol phosphate alkyl triesters Hammett correlation. Abstracts of ... James, R.; Nguyen, T.; Arthur, W.; Levine, K.; Williams, D.C. 1997: Hydrolase activity in Ariolimax columbianus and Arion ater ... Hydrolysis of cellulose using mono-component enzymes shows synergy during hydrolysis of phosphoric acid swollen cellulose PASC ... Ros, M.; Pascual, J.A.; Garcia, C.; Hernandez, M.T.; Insam, H. 2000: Hydrolase activities, microbial biomass and bacterial ...
Metabolism of phosphoric acid triesters by rat liver homogenate. Bull Environ Contam Toxicol 33(3):281-288, PMID: 6478075. , ... In line with these hypotheses, a recent study showed that serum hydrolase significantly contributed to TPhP and EHDPhP ... Organophosphate triesters and diester degradation products in municipal sludge from wastewater treatment plants in China: ...
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