Some enzymes contain molecules in the active site that help facilitate chemical transformations. These molecules are called:…
Kinetic constants are a good way to compare the effects of regulators on the enzyme. These kinetic constants include Vmax and Km. Vmax represents the maximal reaction rate and is the plateau of a Michaelis-Menten curve. At this point, the active sites are saturated or no longer as accessible due to conformational change. The Km is the Michaelis constant and is an inverse of the substrate’s affinity for the binding site. As an inverse, a lower Km represents a higher substrate affinity for the enzymatic binding site. Inhibitors should result in a lower Vmax due to their effects on the activity of the enzyme, while effectors should increase the enzymatic…
a cleft or depression. Substrates will bind to the active site of an enzyme if it is the…
The lock and key theory utilizes the concept of an "active site." The concept holds that one particular portion of the enzyme surface has a strong affinity for the substrate. The substrate is held in such a way that its conversion to the reaction products is more favourable. If we consider the enzyme as the lock and the substrate the key, the key is inserted in the lock, is turned, and the door is opened and the reaction proceeds. However, when an inhibitor which…
The first two are long–lasting inhibitors and the next three drugs are more specific and reversible competitive inhibitors.…
Small temp and ph changes will not result in the enzyme being inhibited from catalyzing its intended reaction. The occurrence of ph and temp ranges of optimum enzyme activity do no support the assumptions made by the lock and key model of ridged active site cavities.…
Products are results of the an enzyme cleaving to a specific substrate, by means of an induced fit. The induced fit is located at the active site of the enzyme or region of the enzyme where the substrate is bound. The substrate is the reactant within the reaction that fits with the enzyme like a key into a lock. Once the substrate enters the enzyme’s active site the enzyme can flexibly change shape to more snugly bind, via the induced fit, to form an enzyme-substrate complex. The substrate is then metabolized or broken down, resulting in a product, which can be utilized to energize cells. Once the product is released from the active site the enzyme returns to it’s original form.…
The rats will be placed in the light compartment of an inhibitory avoidance apparatus and will undergo inhibitory avoidance training on the first day and will undergo an inhibitory retention test one week later while we record the latencies of both tests to enter the dark compartment as a measure of memory…
“Enzymes are biological catalysts - catalysts are substances that increase the rate of chemical reactions without being used up”. The place where these substrate molecules fit is called the active site.…
7. [20 points] An enzyme-catalyzed reaction (KM = 2.7 × 10−3 M) is inhibited by a competitive inhibitor…
There are two types of inhibitors: competitive inhibitors and noncompetitive inhibitors, and their names give a good indication of what they actually do. Competitive inhibitors have a similar structure to the enzyme's substrate, so they can "compete" with the substrate for the active site of an enzyme. Often the enzyme will bond not to its substrate but to the competitive inhibitor, blocking the substrate from the active site and causing the formation of enzyme-substrate complexes to occur at a slower rate. Noncompetitive inhibitors, on the other hand, do not attach to the active site and block the enzyme-substrate complex from forming. Instead, they react with portions of the active site, which results in the changing of its shape. Once the active site's shape is changed, it can no longer attach to the substrate.…
There are two types of irreversible inhibitors, which are the kcat and the Ks inhibitor. Although both are regarded as irreversible inhibitor, the method in which the enzyme is made irreversible varies. The kcat inhibitors occur when an enzyme converts a substrate which is chemically unreactive into a highly reactive product. The product…
Abstract: Properties of enzymes were found in this experiment and some other factors, which affect enzyme activity. Enzymes are catalyst; they catalyze very specific reactions. Results relating to the active site of specific enzymes played a big role while performing this experiment. The purpose of this experiment was to fin how inhibitors affect enzyme’s activity by competing for the active site against substrates.…
normally meet outside the enzyme, or orienting them in a manner in which they would…
Competitive inhibition: resembles the enzyme’s normal substrate and competes with the substrate for the active site on the enzyme.…