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The Baeyer–Villiger oxidation is another example of a biocatalytic reaction. In one study a specially designed mutant of Candida antarctica was found to be an effective catalyst for the Michael addition of acrolein with acetylacetone at 20 °C in absence of additional solvent. [8]
Enzyme catalysis is the increase in the rate of a process by an "enzyme", a biological molecule. Most enzymes are proteins, and most such processes are chemical reactions. Within the enzyme, generally catalysis occurs at a localized site, called the active site.
An example of an enzyme that contains a cofactor is carbonic anhydrase, which uses a zinc cofactor bound as part of its active site. [61] These tightly bound ions or molecules are usually found in the active site and are involved in catalysis. [1]: 8.1.1 For example, flavin and heme cofactors are often involved in redox reactions. [1]: 17
An illustrative example is the effect of catalysts to speed the decomposition of hydrogen peroxide into water and oxygen: . 2 H 2 O 2 → 2 H 2 O + O 2. This reaction proceeds because the reaction products are more stable than the starting compound, but this decomposition is so slow that hydrogen peroxide solutions are commercially available.
The succinate dehydrogenase complex showing several cofactors, including flavin, iron–sulfur centers, and heme.. A cofactor is a non-protein chemical compound or metallic ion that is required for an enzyme's role as a catalyst (a catalyst is a substance that increases the rate of a chemical reaction).
It is now possible to make ribozymes that will specifically cleave any RNA molecule. These RNA catalysts may have pharmaceutical applications. For example, a ribozyme has been designed to cleave the RNA of HIV. If such a ribozyme were made by a cell, all incoming virus particles would have their RNA genome cleaved by the ribozyme, which would ...
The principal hydroxylation catalyst in nature is cytochrome P-450, hundreds of variations of which are known. [3] Other hydroxylating agents include flavins, alpha-ketoglutarate-dependent hydroxylases (2-oxoglutarate-dependent dioxygenases), and some diiron hydroxylases.
Ribbon diagram of a protease (TEV protease) complexed with its peptide substrate in black with catalytic residues in red.(. A protease (also called a peptidase, proteinase, or proteolytic enzyme) [1] is an enzyme that catalyzes proteolysis, breaking down proteins into smaller polypeptides or single amino acids, and spurring the formation of new protein products. [2]