What Are the Effects of Depressants?
An inhibitor (also known as a retarder) is a substance used to retard or reduce the speed of a chemical reaction, and acts like a negative catalyst. It cannot stop the polymerization reaction, it just slows the polymerization reaction. A substance by which chemical reactions are inhibited or mitigated. There are many types and they are widely used.
- Also known as
- Commonly used inhibitors are [1]
- Float
- Psychotropic drugs, common include
- Any substance that can reduce the catalytic activity of the enzyme without causing the enzyme protein to degenerate is collectively referred to as an inhibitor of the enzyme [5] . Inhibitors are often combined with essential groups inside and outside the enzyme active center, thereby inhibiting the catalytic activity of the enzyme. Enzyme activity was restored upon removal of the inhibitor. According to the tightness of the binding between the inhibitor and the enzyme, the inhibitory effect of the enzyme is divided into irreversible inhibition and reversible inhibition.
- 1. Irreversible inhibitors are mainly covalently bound to enzymes
- Inhibitors of irreversible inhibition (irreversible inhibition) are usually covalently bonded to essential groups on the active center of the enzyme to inactivate the enzyme. Such inhibitors cannot be removed by dialysis, ultrafiltration, etc.
- 2. Non-covalent binding of reversible inhibitors to enzymes and / or enzyme-substrate complexes
- Reversible inhibition inhibitors reversibly combine with enzymes and / or enzyme-substrate complexes through non-covalent bonds to reduce or eliminate enzyme activity. The inhibitor can be removed by dialysis or ultrafiltration. Here are three common reversible inhibitory effects.
- 1) Competitive inhibition
- Inhibitors are similar to substrates in that they compete with the substrate for the active center of the enzyme, which prevents the enzyme and substrate from binding to form an intermediate.
- 2) Non-competitive inhibition
- Some inhibitors bind to essential groups outside the active center of the enzyme and do not affect the binding of the enzyme to the substrate. There is no competitive relationship between substrate and inhibitor. However, the enzyme-substrate-inhibitor complex (ESI) cannot further release the product [6] .
- 3) uncompetitive inhibition
- Such inhibitors only bind to intermediates (ES) formed by enzymes and substrates, and the amount of intermediates decreases. In this way, both the amount of conversion from the intermediate product to the product is reduced, and at the same time the amount of free enzyme and substrate dissociated from the intermediate product is also reduced.