Top 10 ArticlesLS-StudioGayRomeo Justus_Dahinden Mercedes Benz OM601 Diyanet İşleri Başkanlığı Radically 25 Ral color system RTLnow.de New concept Electromagnetic compatibility |
News: |
Peroxidases (EC number 1.11.1.x) are a large family of enzymes. A majority of peroxidase protein sequences can be found in the PeroxiBase database. Peroxidases typically catalyze a reaction of the form:
For many of these enzymes the optimal substrate is hydrogen peroxide, but others are more active with organic hydroperoxides such as lipid peroxides. Peroxidases can contain a heme cofactor in their active sites, or redox-active cysteine or selenocysteine residues.
The nature of the electron donor is very dependent on the structure of the enzyme.
While the exact mechanisms have yet to be elucidated, peroxidases are known to play a part in increasing a plant's defenses against pathogens.[1] Peroxidases are sometimes used as histological marker. Cytochrome c peroxidase is used as a soluble, easily purified model for cytochrome c oxidase.
Glutathione peroxidase is a peroxidase found in humans, which contains selenocysteine. It uses glutathione as an electron donor and is active with both hydrogen peroxide and organic hydroperoxide substrates.
Amyloid beta, when bound to heme has been shown to have peroxidase activity.[2]
Peroxidase can be used for treatment of industrial wastewaters. For example, phenols, which are important pollutans, can be remove by enzyme-catalyzed polymerization using horseradish peroxidase. Thus phenols are oxidized to phenoxy radicals which participate in reactions where are produced polymers and oligomers that are less toxic than phenols.
Furhermore, peroxidases can be an alternative option of a number of harsh chemicals, eliminating harsh reaction conditions. There are a lot of investigations about the use of peroxidase in many manufacturing processes like adhesives, computer chips, car parts, and linings of drums and cans.
|
||||||||
|
|||||
|
Custom Search
|
© Copyright 2011 WorldLingo All rights reserved.