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What are the specific functions of catalase (CAT)

Catalase (CAT), as the name suggests, is an enzyme that catalyzes the decomposition of hydrogen peroxide into oxygen and water. However, if you think that it can only catalyze the decomposition of hydrogen peroxide, you would be quite wrong. People also have special functions. Next, let the editor of Desheng talk about this magical enzyme in detail.

First, as a substance, catalase was first discovered in 1811 by Louis Jacques Thénard, the discoverer of hydrogen peroxide (H2O2). In 1900, Oscar Loew named this enzyme capable of degrading hydrogen peroxide "catalase", or catalase, and discovered that this enzyme exists in many plants and animals. In 1937, James B. Sumner crystallized catalase from bovine liver and obtained the molecular weight of the enzyme the following year. In 1969, the amino acid sequence of cattle catalase was solved. Then in 1981, its three-dimensional structure was resolved.

Catalase exists in almost all living organisms. It is commonly found in breathing organisms, mainly in plant chloroplasts, mitochondria, endoplasmic reticulum, animal liver and red blood cells, and its enzymatic activity provides the body with an antioxidant defense mechanism. CAT is hemease, and different sources have different structures. The level of activity is different in different tissues. Hydrogen peroxide decomposes faster in the liver than in organs such as the brain or heart because of the high level of CAT in the liver.

CAT exists in the peroxidase body of the cell. Catalase is a marker enzyme of peroxisomes, accounting for about 40% of the total amount of peroxisome enzymes. Catalase is present in various tissues of all known animals, especially in the liver in high concentrations.

Catalase is used in the food industry to remove hydrogen peroxide from milk used to make cheese. Catalase is also used in food packaging to prevent food from being oxidized. In the textile industry, catalase is used to remove hydrogen peroxide from textiles to ensure that the finished product is peroxide-free. It is also used in the cleaning of contact lenses: after the glasses are soaked in a cleaning agent containing hydrogen peroxide, the residual hydrogen peroxide is removed with catalase before use. The use of catalase in the beauty industry: Some facial treatments add this enzyme and hydrogen peroxide to increase the amount of cell oxygen in the upper layer of the epidermis. Catalase is often used in the laboratory as a tool to understand the effect of enzymes on reaction rates.

Catalase can oxidize other cytotoxic substances such as methanol, formic acid, phenol and ethanol. These oxidation processes need to use hydrogen peroxide to complete the following reactions:

H2O2 + AH2 → 2H2O + A

Yes, this is the special function of CAT. It also has peroxidase activity. It can not only catalyze the hydrogen peroxide reaction, but also oxidize other small molecules of toxic substances incidentally, and it must be in the presence of hydrogen peroxide.

Based on this feature, some companies in biochemical testing have developed test kits that utilize CAT peroxidase activity. For example, the principle of Cayman's kit is that methanol and hydrogen peroxide react under the catalysis of CAT to generate formaldehyde and water, and then use a substance that can react with formaldehyde to develop color to determine the generated formaldehyde and determine the activity of CAT. This perfectly avoids the problem of accurately measuring the concentration of hydrogen peroxide by using the catalase activity of CAT to determine CAT. Because hydrogen peroxide is not very stable, you need to determine the actual concentration of hydrogen peroxide yourself before use, and you need to measure the absorbance at 240 nm, which is troublesome.

So, this little brother is also very skeletal, right? It can not only decompose hydrogen peroxide but also kill other bad guys by the way. However, it also has rivals. Any heavy metal ion (such as copper ion in copper sulfate) can be used as a non-competitive inhibitor of catalase. In addition, highly toxic cyanide is a competitive inhibitor of catalase, which can bind tightly to the heme in the enzyme to prevent the enzyme's catalytic reaction. Since the catalytic mechanism of CAT has not been fully understood, there are still many unsolved mysteries waiting for everyone to discover.

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