Cyp Enzyme Lab Report

Enzymes are biological catalysts that speed up chemical reactions, without being used up or changed. Catalase is a globular protein molecule that is found in all living cells. A globular protein is a protein with its molecules curled up into a 'ball' shape. All enzymes have an active site. This is where another molecule(s) can bind with the enzyme. This molecule is known as the substrate. When the substrate binds with the enzyme, a product is produced. Enzymes are specific to their substrate, because the shape of their active site will only fit the shape of their substrate. It is said that the substrate is complimentary to their substrate.

Background and Introduction: Enzymes are proteins that process substrates, which is the chemical molecule that enzymes work on to make products. Enzyme purpose is to increase the rate of activity and speed up chemical reaction in a form of biological catalysts. The enzymes specialize in lowering the activation energy to start the process. Enzymes are very specific in their process, each substrate is designed to fit with a specific substrate and the enzyme and substrate link at the active site. The binding of a substrate to the active site of an enzyme is a very specific interaction. Active sites are clefts or grooves on the surface of an enzyme, usually composed of amino acids from different parts of the polypeptide chain that are brought together in the tertiary structure of the folded protein. Substrates initially bind to the active site by noncovalent interactions, including hydrogen bonds, ionic bonds, and hydrophobic interactions. Once a substrate is bound to the active site of an enzyme, multiple mechanisms can accelerate its conversion to the product of the reaction. But sometimes, these enzymes fail or succeed to increase the rate of action because of various factors that limit the action. These factors can be known as temperature, acidity levels (pH), enzyme and/or substrate concentration, etc. In this experiment, it will be tested how much of an effect

Enzymes are catalysts that function to speed up reactions; for example, the enzyme sucrose speeds up the hydrolysis of sucrose, which breaks down into glucose and fructose. They speed up reactions but are not consumed by the reaction that is taking place. The most important of the enzyme is the shape as it determines which type of reaction the enzyme speeds up. Enzymes work by passing/lowering and energy barrier and in doing so; they need to bind to substrates via the active. Once they do, the reaction speeds up so much more quickly than it would without the enzyme. Coenzymes and cofactors aid the enzyme when it comes to binding with the substrate. They change the shape of the active site so the substrate can bind properly and perform its function.

B. Catalysis occurs on a specific site on the enzyme (the active site). The active site is usually less than 5% of the surface area of the protein, and is always in a cleft. The rest of the molecule serves to present the active site in a three dimensional structure that is capable of binding substrate and catalyzing the reaction. Binding to a substrate is very specific, and involves ionic interactions, H bonds and van der Waals forces.

On the other hand, based on the MCD intensity graph, free Rv0805 with 2.5 molar equivalence of cobalt ion added (black fold line on right graph A) showed two distinct peaks at 500nm and 570nm wavelength. Compared with GpdQ graph, we can conclude that the metal ion affinity in α-site is very strong for both enzymes, but Rv0805 has a significant higher metal ion affinity in β-site. Therefore, the overall metal ion affinity is higher for the Rv0805 enzyme.

Enzymes are very large globular proteins with three dimensional shapes which is vital for enzyme activity as natural catalyst in chemical reactions within the living organisms (7).

All enzymes are structured to react with unique substrates. and each enzyme has an active site where the substrate bonds to the enzyme. The active site of an enzyme is shaped to fit the specific substrate it reacts with.

The independent variable in this investigation is pH. Each individual enzyme has it’s own pH characteristic. This is because the hydrogen and ionic bonds between –NH2 and –COOH groups of the polypeptides that make up the enzyme, fix the exact arrangement of the active site of an enzyme. It is crucial to be aware of how even small changes in the

Cells are the building blocks of life. Life itself would not be possible without cells and the actions they carry out. Hundreds of biological and chemical reactions take place in the cell every second. Most of the reactions in a cell use enzymes to speed up the reaction. An enzyme is a protein catalyst used by living organisms to increase the rate of biological reactions (Freeman et. al. 2016, p90). A catalyst brings substrates together in a precise orientation that makes reactions more likely. Enzymes have an “active site,” which is where the reactants bind to the enzyme. The active site is where catalysis occurs. The reactants of the enzyme are called the substrates. Enzymes are extremely effective at catalyzing reactions because

Introduction: Enzymes are protein catalysts facilitating the conversion of substrates into products (Alexander and Peters, 2011). They go through a whole chemical reaction which starts off with the substrate and then ends up with a product. The only way this reaction can be adjusted or not even work is if they end up going through some sort of affect which only temperature and pH levels can do determining the environment. When enzymes are in an environment that is too acidic or alkaline, their chemical properties, sizes and shapes can become altered (Magher, 2015) Chemical modification of proteins is widely used as a too; to maintain a native conformation, improving stability (Rodriguez-Cabrera, Regalado, and Garcia-Almendarez, 2011) In this experiment, four trials were conducted and recorded every 15 seconds for 5 minutes in order to calculate the optimum levels and IRV.

“Enzymes are proteins that have catalytic functions” [1], “that speed up or slow down reactions”[2], “indispensable to maintenance and activity of life”[1]. They are each very specific, and will only work when a particular substrate fits in their active site. An active site is “a region on the surface of an enzyme where the substrate binds, and where the reaction occurs”[2].

Each enzyme is very specific and can only catalyze a certain reaction. The specific reaction catalyzed by an enzyme depends on the molecular structure and shape of a small area of the enzyme’s surface called the active site. The active site an attract and hold only its specific molecules. The target molecule that the enzyme attracts and acts upon is called the substrate. The substrate and the active site of the molecule must fit together very closely. Sometimes the enzyme changes its shape slightly to bring about the necessary fit.

Enzymes are natural catalysts that work from the ability to increase the rate of reaction by decreasing the activation energy of a reaction. (Blanco, Blanco 2017) An enzyme can do this 10^8- to 10^10 fold, sometimes even 10^15 fold. (Malacinsk, Freifelder 1998) The substrate will momentarily bind with the enzyme making the enzyme-substrate complex, of which the shape of the substrate is complimentary to the shape of the active site on the enzyme it is binding with. There are two main theories as to how an enzymes and substrates interact, the lock-and-key model and induced fit theory. The lock-and-key model suggests that the enzyme has a specific shape that fits the substrate and only that substrate. The induced fit theory says the active site and substrate are able to change shape or distort for the reaction to take place with (Cooper,

W. John Albery (1976) stated that the “improvement in the catalytic efficiency of enzymes, compared with simple organic molecules, is separated into three broad types of alteration to the Gibbs free-energy profile” (Albery, 1976).

Enzymes owe their activity to the precise three-dimensional shape of their molecules. According to the 'lock-and-key' hypothesis, the substrates upon which an enzyme fit into a special slot in the enzyme