Pernicious anemia is a megaloblastic anemia resulting from vitamin B12 deficiency that develops as a result of a lack of intrinsic factor being released from stomach parietal cells leading to subsequent malabsorption of the vitamin. The major cause of the loss of intrinsic factor is an autoimmune destruction of the parietal cells that secrete it.
Factors affecting Enzyme Activity Factors affecting Enzyme Activity The activity of an Enzyme is affected by its environmental conditions. Changing these alter the rate of reaction caused by the enzyme.
In nature, organisms adjust the conditions of their enzymes to produce an Optimum rate of reaction, where necessary, or they may have enzymes which are adapted to function well in extreme conditions where they live.
Temperature Increasing temperature increases the Kinetic Energy that molecules possess. In a fluid, this means that there are more random collisions between molecules per unit time.
Since enzymes catalyse reactions by randomly colliding with Substrate molecules, increasing temperature increases the rate of reaction, forming more product. However, increasing temperature also increases the Vibrational Energy that molecules have, specifically in this case enzyme molecules, which puts strain on the bonds that hold them together.
As temperature increases, more bonds, especially the weaker Hydrogen and Ionic bonds, will break as a result of this strain. Breaking bonds within the enzyme will cause the Active Site to change shape.
This change in shape means that the Active Site is less Complementary to the shape of the Substrate, so that it is less likely to catalyse the reaction. Eventually, the enzyme will become Denatured and will no longer function.
This will decrease the rate of reaction. In summary, as temperature increases, initially the rate of reaction will increase, because of increased Kinetic Energy. However, the effect of bond breaking will become greater and greater, and the rate of reaction will begin to decrease.
This is different for different enzymes. Most enzymes in the human body have an Optimum Temperature of around It ranges from pH1 to pH Acid solutions have pH values below 7, and Basic solutions alkalis are bases have pH values above 7.
This interference causes a change in shape of the enzyme, and importantly, its Active Site. Different enzymes have different Optimum pH values.
At the Optimum pH, the rate of reaction is at an optimum. Any change in pH above or below the Optimum will quickly cause a decrease in the rate of reaction, since more of the enzyme molecules will have Active Sites whose shapes are not or at least are less Complementary to the shape of their Substrate.
However, extreme changes in pH can cause enzymes to Denature and permanently lose their function. Enzymes in different locations have different Optimum pH values since their environmental conditions may be different. For example, the enzyme Pepsin functions best at around pH2 and is found in the stomach, which contains Hydrochloric Acid pH2.
Concentration Changing the Enzyme and Substrate concentrations affect the rate of reaction of an enzyme-catalysed reaction. Controlling these factors in a cell is one way that an organism regulates its enzyme activity and so its Metabolism.
Changing the concentration of a substance only affects the rate of reaction if it is the limiting factor: If it is the limiting factor, increasing concentration will increase the rate of reaction up to a point, after which any increase will not affect the rate of reaction.
This is because it will no longer be the limiting factor and another factor will be limiting the maximum rate of reaction. As a reaction proceeds, the rate of reaction will decrease, since the Substrate will get used up.
The highest rate of reaction, known as the Initial Reaction Rate is the maximum reaction rate for an enzyme in an experimental situation.
Substrate Concentration Increasing Substrate Concentration increases the rate of reaction. This is because more substrate molecules will be colliding with enzyme molecules, so more product will be formed.
However, after a certain concentration, any increase will have no effect on the rate of reaction, since Substrate Concentration will no longer be the limiting factor.
The enzymes will effectively become saturated, and will be working at their maximum possible rate. However, this too will only have an effect up to a certain concentration, where the Enzyme Concentration is no longer the limiting factor.By completing this lab about enzyme activity, the knowledge about the five main factors that affect the rate of enzyme activity was easier to comprehend.
Before understanding those concepts, it’s crucial to understand the background information of the molecules involved with this lab. Published: Mon, 5 Dec Enzymes are catalysts made within the human body. Catalysts naturally, lower the activation energy required for reactions.
The lower the activation energy is, the faster the rate of reaction is, and therefore enzymes speed up reactions in . 1 Lipase solution is best freshly made, but it will keep for a day or two in a refrigerator. Don’t try to study different temperatures on different days for the same investigation; the activity of the enzyme will change and it will not be a fair test.
Summary. α-Lipoic acid (LA), also known as thioctic acid, is a naturally occurring compound that is synthesized in small amounts by humans.
(More information) Endogenously synthesized LA is bound to protein and functions as a cofactor for several important mitochondrial enzymes.
Factors affecting Enzyme Activity. The activity of an Enzyme is affected by its environmental regardbouddhiste.comng these alter the rate of reaction caused by the enzyme. In nature, organisms adjust the conditions of their enzymes to produce an Optimum rate of reaction, where necessary, or they may have enzymes which are adapted to function well in extreme conditions where they live.
Enzyme activity is affected by various factors, including substrate concentration and the presence of inhibiting molecules. The rate of an enzymatic reaction increases with increased substrate concentration, reaching maximum velocity when all active sites of the enzyme molecules are engaged.