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Guest Posting enzymes as well as general catalysts have many similarities amlon group. It is not important how much is used, as long as the catalytic effect is good. In the same way as catalysts generally, enzymes change only the speed but not the equilibrium state of chemical reactions. It is because the enzyme doesn't change between before and after reactions that it can change many substrates within a short amount of time. It is possible to reduce the activated energy, however, enzymes do not influence the changes in the free energy (G3) during the chemical reaction. Thus, they can accelerate the reaction.

The catalysis enzymes exhibits unique features compared to that of general catalysts.

1. High-efficiency catalysis using enzymes

It is clear that enzymes have much more catalytic power than catalysts. The decomposition reactions of hydrogenperoxide are catalyzed by both Fe2+ catalase and the inorganic element iron. A mol (1 mol) of catalase will catalyze a decomposition reaction of 5x106 Mol of H2O2 over 1 minute. One mol Fe2+ catalyst cannot catalyze decomposition under these conditions. In comparison with Fe2+, the catalytic effectiveness of catalase can be 1010x greater.

In order to determine the catalytic efficiency of enzymes, we can use the concept of turnover numbers. The conversion number relates to the number molecule per enzyme molecule which is capable of converting the substrate in a minute at a high substrate concentration, i.e. the number of mols that catalyze substrate chemical transformation. According to data above, you can calculate the catalase conversion number as 5x106. Most enzymes are around 1,000 in number, but the highest can exceed 106.

2. The high specificity of enzyme catalysis

It is possible that an enzyme only acts on specific substances or types. Herein lies the speciality of enzymes. For example, glycosidic bonds, ester bonds, peptide bonds, etc. Although these bonds can be hydrolyzed with acid-base chemistry, the enzymes involved in this process are not identical. Each enzyme is specific. This can be done by enzymes that are found in nature.

3. Conditions of mild catalysis by enzymes

For enzymatic processes, conditions like normal temperature and pressure are needed. Also, pH should be neutral. The enzymes, which are proteins, are sensitive to environments like high temperatures and strong acids or alkalis. As enzymes are very sensitive to any changes that occur in their external environment, and they can become inactive or denatured easily, reaction conditions need to be controlled.

4. Achieve a adjustable enzyme activity

In comparison with chemical catalysts another characteristic of enzyme catalysis that can be automatic is its catalytic ability. Even though there are many chemical reactions within organisms, these are well-coordinated and organized. Changes in enzyme catalytic function can be influenced by substrate concentration, products concentration, or environmental conditions. These factors will affect the orderly and coordinated progress of biochemical reaction. An imbalance or disorder in the biochemical process will lead the organism into disease. For organisms to be able to respond to changing environmental conditions and maintain their normal daily activities, they developed an automatic system for regulating enzyme activities. Inhibitor regulation, feedback regulatory, covalent regulation, zymogen activated, and hormone regulation are all ways of regulating enzymes.

It is possible to relate the catalytic activity of an enzyme with its coenzyme (coenzyme), prosthetic group, and metal ion. Enzymes are often complex proteins. Their catalytic properties are strongly influenced by the coenzymes (small molecules), cofactors (small molecules) and metalions (small molecules). The activity of the enzyme is reduced if these molecules are removed.