Big Chemical Encyclopedia

Chemical substances, components, reactions, process design ...

Articles Figures Tables About

Classical enzyme

Veitch, N.C., Horseradish peroxidase a modern view of a classic enzyme, Phytochemistry, 65, 249-259, 2004. [Pg.686]

Veitch NC. 2004. Horseradish peroxidase a modem view of a classic enzyme. Phytochemistry 65 249—259. Wegrzyn TF, Farr JM, Hunter DC, Au J, Wohlers MW, Skinner MA, Stanley RA and Waterhouse DS. 2008. Stability of antioxidants in an apple polyphenol—milk model system. Food Chem 109 310-318. [Pg.129]

Generally, DNMT inhibitors can be divided in two big dasses. One group consists of base analogs which are incorporated into DNA and act as suidde substrates for DNMT via a covalent adduct formation. The other group acts on the free enzyme in the same way as classic enzyme inhibitors do. [Pg.170]

Classical enzyme targets (acetylcholinesterase, monoamine oxidase) Emerging targets (kinases, caspases)... [Pg.482]

The specific function of the SH3 domain is based on increased substrate specificity of tyrosine kinases in this case (Shokat, 1995). In classical enzymes, the substrate binding site and the catalytic center are close together and the substrate binding site is generally highly specific for a particular substrate. The situation is different for tyrosine kinases. Here, the substrate binding site near the catalytic center shows moderate selectivity. The specificity of the reaction is increased, however, by mediation of asso-... [Pg.307]

Our work deals with the necessity of creating kinetics laws for heterogeneous enzymology. There was a big gap between the classical enzyme kinetics in solution and highly structured biological systems. All the concepts of diffusion reaction are clear for our thick membrane but are also useful for lipid-protein membranes, even if the process of transport is not only classical diffusion. [Pg.238]

The classical enzymes of phosphorylation, the hexokinases, have broad specificity, acting as well on D-glucose, D-mannose, and D-fructose.62-63 The yeast enzyme is utilized. 6-Phosphofhictokinase and phosphoribulokinase create a second phosphate ester function on a sugar monophosphate. [Pg.208]

Veitch NC (2004) Horseradish Peroxidase A Modem View of a Classic Enzyme. Phytochemistry 65 249... [Pg.487]

In addition to this, that an interesting novel emulsion membrane reactor concept overcomes the difficulties of the large solvent volume otherwise required for the reduction of poorly soluble ketones [30]. 2-Octanone was reduced by a carbonyl reductase from Candida parapsilosis to (S)-2-octanol with > 99.5 % ee and total turnover number of 124 - the 9-fold value of that obtained in a classical enzyme reactor. [Pg.198]

Appleyard, M.E. (1992). Secreted acetylcholinesterase non-classical aspects of a classical enzyme. Trends Neurosci. 15 485-90. [Pg.708]

Economic Considerations. The most important consideration in determining whether an enzyme will be a commercial success is the economics of its use—will the cost of using the enzyme be at least equal to the value of the changes rendered through its use This principle has interesting ramifications that tend to horrify the classical enzyme chemist. [Pg.10]

The classic enzyme commission (EC) classification for GTs is on the basis of their donor and acceptor specihcity as well as the product formed. Currently, 295 entries are in this database (http //www.chem.qmul.ac.uk/iubmb/). The distinction between these enzymes is noted by their ability to catalyze the transfer of hexoses (EC 2.4.l.y, hexosyltransferases), pentoses (EC 2.4.2.y, pentosyltransferases), or other glycosyl groups (2.4.99.y, sialyltransferases). This classification is restricted to enzymes that are fully characterized, and it can be problematic for enzymes that act on several distinct acceptors but at different rates. It also does not take into account the origin of the enzyme or its three-dimensional stmcture. [Pg.658]

Alternative pathways for denitrification have been proposed that do not involve the classical enzyme systems, but their existence has only recently been confirmed or investigated in detail. In the absence of O2, a number of elements and compounds have the potential to oxidize NH , including Mn(II), Mn02, NO, NO2 and NO2. Because anaerobic oxidation of NH directly to N2 bypasses the multiple oxidation steps required for coupled nitrification-denitrification... [Pg.4223]

Classical enzyme inhibitors such as bacitracin, bes-tatin, and amastatin have been found to be effective for improving the nasal absorption of various peptide drugs such as LHRH and calcitonin. These inhibitors having peptide like structures appear to exert their inhibitory effects by a competitive mechanism. In addition, camostat mesilate and nafamostat mesilate, which are clinically used as primary ingredients for pancreatic diseases, have been found to improve the nasal absorption of vasopressin, desmopressin, and calcitonin by inhibiting aminopeptidase and trypsin activity. [Pg.2686]

By far the fastest and easiest route to finding a new enzyme is to find one that exists in a commercial library. This allows for instant access to the catalyst in sufficient quantities to take the project to the next step. For the most part there are still only a few sources. Traditional sources such as Sigma, Amano, Roche Molecular Biochemicals (formerly Boehringer-Matmheim), and Toyobo carry many of the classic enzymes that have been used in the past. [Pg.6]

For the determination of binding properties of biotinylated proteins and conjugates, use flexible 96-wells microplates (Nunc). The general design of the method is similar to classical enzyme-linked immunosorbent assay (ELISA) and RIA methods. Use the described procedure for immobilization of streptavidin, antigen, biotinylated or nonmodified antibody, or catalase. [Pg.244]

Receptor theory is based on the classical Law of Mass Action as developed by Michaelis and Menten (20) for the study of enzyme catalysis. The extrapolation of classical enzyme theory to receptors is, however, an approximation. In an enzyme-substrate (ES) interaction, the substrate S undergoes an enzyme-catalyzed conversion to a product or products. Because of the equilibrium established, product accumulation has the ability to reverse the reaction process. Alternatively, the latter can be used in other cellular pathways and is thus removed from the equilibrium situation or can act as a feedback modulator (21) to alter the ES reaction either positively or negatively (Equation 10.2). [Pg.322]

Because identification of a saturable process occurs only for low extraction ratio compounds (i.e., CL, etaboiism = /uCLint), the relationship between classical enzyme kinetics and pharmacokinetics is revealed ... [Pg.638]


See other pages where Classical enzyme is mentioned: [Pg.4]    [Pg.210]    [Pg.110]    [Pg.306]    [Pg.108]    [Pg.182]    [Pg.30]    [Pg.52]    [Pg.165]    [Pg.97]    [Pg.188]    [Pg.378]    [Pg.221]    [Pg.30]    [Pg.199]    [Pg.83]    [Pg.55]    [Pg.2700]    [Pg.108]    [Pg.259]    [Pg.199]    [Pg.101]    [Pg.107]    [Pg.107]    [Pg.138]    [Pg.333]    [Pg.265]    [Pg.214]   
See also in sourсe #XX -- [ Pg.83 ]




SEARCH



Classical enzyme inhibition

Enzyme classical inhibitor

Resolution, classical enzymic

Resolution, classical using enzymic hydrolysis

Substrate and Product Concentration in Enzymes Following Classical Michaelis-Menten Kinetics

© 2024 chempedia.info