Non-nucleoside inhibitors of reverse transcriptase enzyme:
- efavirenz (EFV or EFZ)
- nevirapine (NVP)
Protease inhibitors:
- indinavir (IDV)
- lopinavir
- nelfinavir (NFV)
- ritonavir
- (saquinavir (SQV).
Enzyme inhibitors are molecules that bind to enzymes and reduce their activity temporarily or permanently.
The inhibitor link can stop the substrate material from entering the active enzyme site and / or preventing the enzyme from stimulating its reaction. There are two types of inhibitors, either reflective or non-reflective. Non-reflective inhibitors typically interact with the enzyme and change it chemically (by forming covalent bonds).
These inhibitors are found to modify the residues of essential amino acids necessary for enzymatic activity. In contrast, there are reflective inhibitors that are linked to non-covalent bonds and different types of inhibitors are produced depending on whether these inhibitors bind to the enzyme, or synthesized enzyme and substrate material, or both. Many drug molecules are inhibitory to the enzyme, so their detection and improvement is a very active area in Research in biochemistry and pharmacy.
The enzyme inhibitor is often judged by its class (lack of binding to other proteins) and its efficacy (its dissociation constant, indicating the concentration needed to inhibit the enzyme).
When the variety is high, we ensure that the drug will have few side effects and therefore low toxicity.
The enzyme inhibitors also occur naturally and are involved in the regulation of metabolism.
For example, enzymes in the metabolic pathway can be inhibited by products produced during the chain reaction and discouraged.
This type of negative feedback slows down the production line when products begin to build and is an important way to maintain balance in the cell.
Other cellular enzyme inhibitors are proteins that are specifically linked to the enzyme and inhibit its action.
This can help control the enzymes that may be harmful to the cell, such as proteases or nucleases. Natural enzyme inhibitors can be used as a protection against any foreign or harmful body.
The most common uses of enzyme inhibitors are drugs to treat diseases.
Many of these inhibitors target an enzyme in the human body and aim to correct its pathological condition.
However, not all drugs are enzyme inhibitors.
Some, such as antiepileptic drugs, alter the activity of the enzyme by causing an increase in its productivity or reduction, which are unrelated to the above types.
An example of a medical enzyme inhibitor is Viagra, a common treatment for males with erectile dysfunction.
This molecule works to increase body signals, which relax the smooth muscles in the body and increase the flow of blood and expansion of the arteries, causing erection.
Since the drugs reduce the activity of the enzyme that stops these signals, it makes these signals last longer than the time.
Another example of the structural similarity of some enzyme inhibitors that are targeted is similar to the form that compares methotrexate and folic acid.
Folic acid is the substrate of dehydrolyte reduction, an enzyme involved in the manufacture of nucleotides that are strongly inhibited by methotrexate. Methotrexate performs the same action as the enzyme dehydrolyte reductase, thus stopping the production of nucleotides.
This biomass of nucleotide is more toxic to cells of rapid growth than non-dividing cells, because the fast-growing cell has the ability to replicate nucleic acids, so methotrexate is often used in chemotherapy for cancer.
Drugs are also used to inhibit enzymes needed to survive pathogens.
For example, bacteria surround a thick cell wall made of polymer such as peptidoglycans.
Many antibiotics such as penicillin and vancomycin inhibit the enzymes that then produce and bind the polymer filaments together.
This causes to decrease the cell wall strength and the bursting of bacteria.
The design of antibiotics is facilitated when the enzyme necessary to survive the disease is absent or very different in humans.
In the example above, humans do not produce peptidoglycans, hence the inhibitors of this process are toxic to bacteria.
It also produces toxicity in antibiotics by exploiting differences in the structure of ribosomes in bacteria, or how they are made for fatty acids.
Enzyme inhibitors are also important in controlling metabolic processes.
Many metabolic pathways in the cell are inhibited by metabolites that control enzyme activity through the tibial ligaments or inhibition of substrate material.
A good example is the diaphragmatic controls of diabetic biodegradation. This pathway consumes glucose and produces energy.
A major step to the regulation of diabetic glycolysis is an early reaction in the pathway stimulated by phosphofructokinase.
When energy levels rise, the energy molecule connects the alosteric site in PFK1 to reduce the rate of enzyme reaction.
Sugar dissolving is inhibited and production of ATP decreases.
This control helps the negative feedback maintain a constant concentration of the epithelium in the cell. However, metabolic pathways are not only regulated by inhibition since activation of the enzyme is equally important.
With respect to PFK1, 2,6-bisphosphate and literature are examples of metabolism that are arostric doping.
Inhibitory physiological enzymes can also be inhibited by specific protein inhibitors.
This process occurs in the pancreas, which inhibits many enzymes that activate enzymes of the digestive system known as Zemogens.
Many of these inhibitors are activated by the terpsin protein, so it is important to block the activity of trypsin propane in the pancreas to prevent the organ from digesting itself.
One way to control trypsin activity is to produce a protein that inhibits trypsin and is specific and strong in the pancreas.
This inhibitor is tightly bound with trypsin, inhibits its activity and protects the pancreas.
Although trypsin inhibitor is a protein, it avoids degradation as a substrate of protease by excluding water from the active site of the toxin and disrupting the transition state.
Many pesticides are enzyme inhibitors. Acetylcholinesterase (ASH) is an enzyme found in animals from insects to humans.
It is essential that the function of neurons through its mechanism to break down acetylcholine nervous in their components, acetate and choline.
This is fairly unusual among neurotransmitters as most are absorbed, including serotonin, dopamine, and noradrenaline, from the synaptic cleft rather than cleft. A large number of ASH inhibitors are used in both medicine and agriculture.
Adverse competitive inhibitors, such as erydomonium, fisostigmine, and neostigmine, are used in the treatment of myasthenia gravis and anesthesia.
Carbamide pesticides are also examples of reversible AS inhibitors.
Organic phosphate pesticides such as malathion, parathion, and chlorpyrifos irreversibly inhibit acetylcholinesterase. Many pesticides are inhibitory enzymes.
Such as sulfonyl urea inhibiting acetolactate synthase. All of these enzymes are required for plants to make amino acids branching chain.
Many other enzymes are inhibited by herbicides, including enzymes needed for the bio-synthesis of lipids, carotenoids, oxidative photosynthesis and phosphorus processes.
