Why don t proteases hydrolyze proteases? What method should be used to hydrolase enzymes?

Some proteases can digest themselves. For example, vacuolar processing enzyme (VPE). But protease hydrolyzed substrates are not hydrolyzed randomly.

They need to recognize a specific sequence of amino acids. If a protease itself does not have a site recognized by its own active region, then it should not be hydrolyzed by itself. The degree of protease activation is regulated by the pH, inhibitory domain.

When no other protein substrate is present or not in the proper spatial location, these proteases are not activated, protecting themselves from hydrolysis.

Protease is a general term for a class of enzymes that hydrolyze protein peptide chains. According to the way in which polypeptides are degraded, they are divided into two categories: endopeptidase and tepeptidase. The former can cut off the large molecular weight polypeptide chain from the middle to form prion and peptone with small molecular weight; The latter can be further divided into carboxypeptidases and aminopeptidases, which hydrolyze peptide chains from the free carboxyl terminus or free amino terminus of polypeptides one by one to produce amino acids.

Enzymes are very specific drops, you say protease, protease, you have learned these three words now, and when you are in college, you will understand that there are many definite words in front of proteases! A variety of different proteases that hydrolyze different proteins! Basically, an enzyme can only hydrolyze one or a class of substances

Most enzymes belong to proteins, and the protein itself is formed by the dehydration and condensation of amino acids, and it can lose water in the state of water, of course, it cannot be hydrolyzed by itself If the protein can be hydrolyzed by itself, then may I ask, can people still live?

Enzymes have binding centers, which can bind to substrates, and then rely on catalytic centers for catalysis, pepsin cannot bind to its own binding centers, so it cannot decompose itself.

The process of zymogen activation is usually accompanied by changes in the primary structure of enzyme proteins. The change in the primary structure of the zymogen molecule leads to a change in the spatial structure of the zymogen molecule, which allows the formation of the catalytic active center, thus transforming it from an inactive form of zymogen to an active enzyme. The physiological significance of zymogen activation is as follows:

Protects tissue cells from being digested by enzymatic hydrolysis.

Hydrolases are enzymes that catalyze the hydrolysis of substrates. For example, amylase, protease, lipase, phosphatase, etc.

For hydrolases, as long as the name of the substrate is sufficient, such as sucrase, cholinesterase, protease, etc.

As we all know, in our lives, many things cannot be solved, and at the same time, we will be left with certain questions, to know about proteases.

First of all, we must know that enzyme is a protein with catalytic activity, and protease is because protein catalyzes enzyme, so there is a protease, and protease is a class that can catalyze protein hydrolysis.

The reaction of proteins, this enzyme has a relatively large impact on us, and it is also an indispensable substance in our lives, but we must know that many substances cannot hydrolyze themselves, and the same is true for proteases, you must know that enzymes are specific, so not all proteases can be hydrolyzed, so there is a saying that proteases do not hydrolyze proteases. It can be seen that proteases are not only proteins, but also contain some lipids.

and polysaccharides, which is a complex, plus there is no specificity in itself, at this time, if you want to be able to decompose yourself, then there is no protease in our lives.

It can be seen that in life, we must pay attention to our own body, protease is an essential nutrient for our body, if once the lack of protease, then the impact on us is relatively large, so in life we must exercise more, eat more fresh vegetables and fruits, can synthesize protease, but also pay attention to their own health, many people do not pay attention to their own health, so it will lead to some other symptoms in the body.

And you should also know that protease can not hydrolyze all proteins, only some proteins, you must know that enzymes have a high degree of specificity, if there is a protease that can hydrolyze all proteins, then the whole person is hydrolyzed by this substance.

Because proteases do not have the ability to hydrolyze, and proteases are affected by other factors during their breakdown, this does not happen.

Because protease lacks basic factors, the mediation temperature is not high enough, and there are no bacteria, so it cannot decompose hydrolyzed protein.

Because an enzyme is a catalytically active protein with a certain specificity, it cannot be hydrolyzed protease.

The protease itself is a protein in its own right, and the two chemicals have the same structure, so they do not react.

Chinese name: protease English name: protease; Proteinase Other Names:

Proteolytic enzyme Definition: An enzyme that catalyzes the hydrolysis of peptide bonds in proteins. According to the properties of the group in which the active center of the enzyme plays a catalytic role, it can be divided into:

Serine Threonine protease (number: EC mercaptoprotease) (number: EC metalloproteinases (number:

EC and aspartic acid proteases (number: EC, etc.) Applied Disciplines:

Biochemistry and Molecular Biology (first-level discipline); Enzymes (secondary discipline).

A general term for a class of enzymes that hydrolyze protein peptide bonds. According to the way it hydrolyzes polypeptides, it can be divided into two categories: endopeptidase and exopeptidase. Endopeptidases cut off the inside of protein molecules to form crescents and peptones with a smaller molecular weight.

Exopeptidases hydrolyze peptide bonds one by one from the ends of the free amino or carboxyl groups of protein molecules, and free amino acids, the former being aminopeptidase and the latter being carboxypeptidase. According to its active center and optimal pH value, proteases can be divided into serine proteases, thiol proteases, metalloproteinases and aspartic proteases. According to the optimal pH value of its reaction, it is divided into acid protease, neutral protease and alkaline protease.

Proteases used in industrial production are mainly endopeptidases.

Proteases are widely found in animal offal, plant stems and leaves, fruits, and microorganisms. Microbial proteases are mainly produced by molds, bacteria, and secondarily yeasts and actinomycetes.

Enzymes that catalyze protein hydrolysis. There are many types, the important ones are pepsin, trypsin, cathepsin, papain and subtilisin. Proteases have strict selectivity for the substrates they act on, and one protease can only act on certain peptide bonds in protein molecules, such as peptide bonds formed by trypsin-catalyzed hydrolysis of basic amino acids.

Proteases are widely distributed, mainly found in the digestive tract of humans and animals, and are abundant in plants and microorganisms. Due to the limited animal and plant resources, the industrial production of protease preparations is mainly prepared by fermentation of microorganisms such as Bacillus subtilis and Aspergillus perchonica.

Proteolytic enzymes are the ones that hydrolyze proteins.

Proteoenzymes refer to enzymes in which the components of the enzyme are proteins, which correspond to nucleases. Protease is a general term for a class of enzymes that hydrolyze protein peptide bonds, which are enzymes that can hydrolyze proteins.

According to the nature of the active sites of various proteases, they can be divided into four categories: serine proteases, thiol proteases, aspartic acid proteases, and metalloproteinases.

Serine protease: its active center includes histidine and aspartic acid residues in addition to serine, such as various endocyptiptidase secreted by the pancreas and various proteases related to coagulation, hemolytic fiber, and complement system.

Aspartate proteases: their active centers are composed of two aspartate residues, such as pepsin secreted by the gastric membrane, angiotensin-releasing enzyme in the kidneys, and some cathepsin in cytolysosomes.

Metalloproteinase: its active center needs to be involved in other amino acid residues in addition to metal ions, such as pancreatic carboxypeptidase The active center includes zinc ions, glutamic acid, and tyrosine residues.