The effect of pH on the speed of enzyme interaction with substrate chemicals Hypothesis: About pH: If the pH level is less than 5, then the speed of the enzyme reaction will be slower. About temperature: If the temperature stays the same, then the speed of the enzyme reaction will not be completely affected. Background information: The function of enzymes is to speed up the biochemical reaction by lowering the activation energy, they do this by colliding with the substrate.
a. What are Enzymes Enzymes are very efficient protein based catalysts for biochemical reactions, which are essential to all living this to sustain life. Enzymes itself are not alive as they are proteins, however they are still made by living things and act as a catalyst to speed up the overall chemical reaction, asmost chemical reactions in biological cells would occur too slowly if it was not for these enzymes. Despite them making chemical reactions move quicker, they are not changed by the reaction. b. Optimal Enzyme Temperature There is a certain temperature at which an enzyme's catalytic activity works at its best and is at its greatest.
Introduction: Enzymes are biological catalysts that increase the rate of a reaction without being chemically changed. Enzymes are globular proteins that contain an active site. A specific substrate binds to the active site of the enzyme chemically and structurally (4). Enzymes also increase the rate of a reaction by decreasing the activation energy for that reaction which is the minimum energy required for the reaction to take place (3). Multiple factors affect the activity of an enzyme (1).
The first step is where the substrate enters the active site on the enzyme. It is held there by hydrophobic interactions between the exposed non-polar groups of the enzyme residues and the side chain of the substrate. The second step is where the hydroxyl group on Serine 195, aided by the histidine-serine hydrogen bonding, preforms its nucleophilic attack on the carbonyl carbon of an aromatic amino acid. While this happens, it also transfers the hydroxyl hydrogen to the histidine nitrogen. The nucleophilic attack pushes the carbonyl electrons onto the carbonyl oxygen, which forms a short-lived intermediate.
INTRODUCTION: Arginase is an enzyme- enzymes are biological catalyst which drives a reaction at the speed of life. Arginase is a hydrolase, hydrolases catalyze hydrolysis reactions, this is determined via the E.C number (Nelson and Cox 2008). Arginase has the EC number is 220.127.116.11 (Schomburg 2015). The enzyme ‘commission number’ is the arithmetical classification that is used for enzymes which indicates the chemical reaction they catalyze.
During the binding process the substrate requires some assistance in order to bind to the enzyme properly. This is done by several different catalytic mechanism. The most abundant catalytic mechanism is known as the general acid-base catalysis. For this reaction to occur, one of the eight amino acid residues, shown in fig 6-9, will act as a proton donor or a proton acceptor. The amino acid residues known for their acidic form will function as the proton donor and the residues that form a base will act as a proton acceptor.
The products are released from the enzyme surface to regenerate the enzyme for another reaction cycle. The active site has a unique geometric shape that is complementary to the shape of a substrate molecule, similar to the fit of puzzle pieces.
Energy between the bacterial cells can be transformed from one another in a development called transduction. The chemical energy stored is called the glucose fuel, it allows the protons to move in and out of the cell. The cell has to waste its own energy and is produce in a similar way that fuel is transferred into a car engine to make it
They can only quicken reactions that will eventually occur, but this enables the cell to have a productive metabolism, routing chemicals through metabolic pathways. Enzymes are very specific for the reactions they catalyze; they make sure the chemical processes go in the cell at any given time. Peroxidase was the enzyme being testing in this experiment. A peroxidase is an enzyme that acts as catalysts, which occurs in biological systems. Peroxidase is found in plants, which they play a role in helping to minimize damage caused by stress factors or insect pests.
Lab Report -- Relationship on Enzyme activity and substrate concentration Research Question: Is the more concentrated the substrate of hydrogen peroxide is, the shorter the time taken for the paper disc to rise from the bottom of the beaker? Aim: The opposite of hull hypothesis Background Information: This experiment aimed to investigate on the relationship of the substrate concentration and enzyme activity. Enzymes are proteins produced by a cell that acts as catalysts to increase the rate of a specific chemical reaction without changing the reaction itself.
Enzymes are catalysts in biological systems, that lower the activation energy, so that molecules can begin reacting with each other. Since enzymes have a very selective active site, if the enzyme shape is changed or denatured, it won’t allow the enzyme to bind. Catalytic enzymes break down the toxic hydrogen peroxide into water and oxygen gas. (Bryer) (Baker) The purpose of these labs were to see how different concentrations of pH, and hydrogen peroxide would affect the enzymes, catalase and
Hypoxia: is the lack of adequate oxygen but hypoxic injury is due to low blood supply, which impacts the heart muscle (Huether & McCance, 2012, p. 63-65 ). After the cessation of blood supply to the heart muscle, the contraction stops due to decline in mitochondrial phosphorylation. This leads to low ATP production, which causes an increase in anaerobic metabolism, producing ATP from glycogen. Even when that is used up, the sodium and potassium pump on the plasma membrane and the sodium-calcium exchange fail to function. All of this causes cellular swelling and also lead to vacuolation, formation of vacuoles.