The Benefits Of Irreversible Enzyme Inhibitors

Chemically, enzymes are like any catalyst and are not consumed in chemical reactions, nor do they alter the equilibrium of a reaction. Enzymes differ from most other catalysts by being much more specific. Enzyme activity can be affected by other molecules: inhibitors are molecules that decrease enzyme activity, and activators are molecules that increase activity.

Most enzymes are proteins. They are catalyst that are able to speed up biological reactions by lowering the activation energy needed for the reaction to occur. (BBC, 2011) Enzymes are substrate specific and therefore each enzyme can only fit a certain substrate. They have an active site on the surface of the enzyme into which the substrate binds. Enzymes may break down a single substrate molecule into simpler substances, or join two or more substrate molecules together. As enzyme substrate bonding occurs, the substrate binds to the enzyme with weak bonds. The binding causes a change of shape in the enzyme and substrate and the bonds in the substrate become stressed allowing them to break more easily. This leads to products being formed. The products are then released and the enzyme takes its original shape.

Enzymes are proteins catalysts, in which the enzyme speeds up reactions. Enzymes speed up reactions by lowering the activation energy. The enzyme or catalyst is not consumed in the reaction; therefore, the enzyme can be reused (Areda, 2017). Activation energy is the energy needed to start a chemical reaction (Reece, 2017). In other words, the activation energy is kind of like a barrier, in which enzymes help decrease the amount of energy needed to start the chemical reactions. Enzymes have unique shapes and one part of the enzyme that has a specific shape is the active site. The active site is where the substrate (reactant) binds with the enzyme. When the enzyme and substrate attach they form what is know as the enzyme-substrate complex. This

Enzymes are proteins which acts as catalysts and an active site is an area on the exterior of the enzyme on which the substrates will bind to, and stimulates a chemical reaction. Substrate can only bind to specific enzymes because the active site has a very precise form, in which a specific substrate can bind to. This is referred to as the enzyme-substrate specificity, and can be compared to a lock & key. A substrate (key) can only bind to an enzyme (lock) if they fit. An enzyme inhibiting decreases the reaction of an enzyme catalysed. There are two types of inhibitors; competitive and noncompetitive inhibitor. Competitive inhibitors impedes the substrates from binding to the active site, because the inhibitor and the substrate is structurally

There are plenty of drugs that are targeting P-glycoprotein (p-gp), which is typically located in intestinal epithelial cells where drugs absorption occurring. The p-gp controls in and out of most of foreign substrates from the blood stream. It contributes to balancing out the concentration of drugs in the blood vain through reuptake process, especially efflux pump in this case. Therefore, this protein has been called as multidrug resistance because it is able to excrete the drugs into the lumen. Accordingly, the p-gp inhibitor has an important role for the drug bioavailability and transportation. As the p-gp inhibitor works in the vivo, the reuptake of drug will be decreasing which means decreasing the

Enzymes are soluble protein molecules that are fundamental in the maintenance of biological functioning. Their primary purpose is to take on the form of a catalyst during chemical reactions in order to lower the activation energy levels required during the reaction and therefore, change the rate at which equilibrium occurs. Each enzyme is highly selective which means they will only act on specific substrates in particular reactions to convert them to products with different molecular structures.

Enzyme inhibitors are known for hindering the action of enzymes. Many of the inhibitors simply attach to the enzymes through weak interactions resulting in reversible inhibitions. In the case of competitive inhibition, inhibitor molecules resemble and mimic the normal substrate molecules and compete with the the substrate for its attachment to the active site of the enzyme. This simply blocks the substrates from binding to the active site leading to an impeded enzymatic reaction. In contrast, a noncompetitive inhibitor does not necessarily compete with the substrate to bind to the active site. It bind to a different site on the enzyme and alters its shape in such manner that the active site becomes less

Some substances can block or distort the active site of an enzyme, reducing or stopping its catalytic activity in biochemical reactions. These chemicals are called inhibitors (Royal Society of Chemistry, 2004). Activators are compounds or factors that act on a specific enzyme to increase its activity (National Center for Biotechnology Information, 2009)

Enzymes are protein molecules that are biological catalysts in the human body, meaning that they contribute in the breaking down of certain molecules. Enzymes have a specific active site which the substrate (reactant) that is complementary to will bind with. When the substrate and enzyme bind, an enzyme-substrate complex occurs which means that a reaction takes place. The enzyme acts as a catalyst and breaks the bonds of the substrate. However different enzymes have different optimum pH &temperature values at which they can be active.

In competitive inhibition, an inhibitor that resembles the normal substrate binds to the enzyme, usually at the active site, and prevents the substrate from binding.[9] At any given moment, the enzyme may be bound to the inhibitor, the substrate, or neither, but it cannot bind both at the same time. During competitive inhibition, the inhibitor and substrate compete for the active site. The active site is a region on an enzyme which a particular protein or substrate can bind to. The active site will only allow one of the two complexes to bind to the site therefore either allowing for a reaction to occur or yielding it. In competitive inhibition the inhibitor resembles the substrate therefore taking its place and binding to the active site of

Enzyme activity can be prevented by enzyme inhibitors, which can directly or indirectly interfere with the functioning of the active site of an enzyme and so reduce its activity. Inhibition can be competitive or non-competitive.

Many other molecules can also denature an enzyme and cause its function to become disabled. If the activity is increased, it is called an activator. But if the rate of reaction is decreased, then is it said to be an inhibitor (Berg, 2002). Competitive inhibitors will try to bind to the substrate; this can cause disruptions in the enzymatic structure (Berg, 2002). As said before, enzymes are catalysts.

Additionally, inhibitors affect the rate of reaction in varying ways – as the name suggests these would decrease. Competitive inhibitors are a similar shape of substrates which would mean the inhibitor would result in active site being occupied and lowering the chance of enzyme-substrate complexes being produced, therefore, reducing the rate of reaction. The enzymes requires particular conditions in order to function in certain areas – the most suitable conditions in which the enzyme work best i.e. pH levels and temperature are known as optimum conditions, for example, optimum pH conditions for enzyme amylase that catalyses breakdown of starch by hydrolysing glycosidic bonds resulting in the product maltose which is found in the salivary glands are neutral or slightly

Enzymes are proteins that function as biological catalysts. They increase the rate of reaction by providing an alternate pathway of lower activation energy. The rate of an enzyme-catalysed reaction is governed by multiple factors such as the temperature of the solution and concentration of the substrate.

What allosteric enzyme inhibitors do is that they act as modulators, attaching themselves to a molecule that will alter the binding site for the enzyme and make it unusable and as a result the enzyme becomes inactive. Theophylline inhibits the activity of the enzyme phosphodiesterase, which forms part of a group of enzymes that degrade the phosphodiester bond (DrugBank, n.d.).