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Enzymes and their importance
Describe the use of enzymes in biological systems and some industrial processes
Describe the use of enzymes in biological systems and some industrial processes
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Introduction Enzymes are known as biological catalysts. (Ahmed) These enzymes bind to substrates. They have specific substrates that they have to bind to. The are where enzymes bind are called an active site. The job that a catalyst holds is to speed up the reaction. All this is only possible through chemical reaction. The input of energy given to chemical reactions is called activation energy. This is the process is what pushes the reaction to happen. Enzymes acts like a catalyst that speeds up without being consumed by the reaction. Enzymes are a huge part of the body that speeds up the chemical process, they are needed otherwise our bodies would not be able to Another essential part of an enzyme is its substrate. These are needed in order for them to act on. The specific area where the enzyme binds with the substrate is called an activation site. The activation site is where the reaction speed up occurs. The binding reaction is divided into three main sections. These reactions are called forward reaction, reverse reaction, and at equilibrium. These illustrat...
This hurdle is called the activation energy of the reaction. [IMAGE] By decreasing the activation energy, more substrate is changed to product in a certain amount of time. That is, the enzyme increases the rate of the reaction. [IMAGE] The activity of catalase can be measured by finding the rate of which the oxygen gas is released from the breakdown of Hydrogen Peroxide.
Enzymes are proteins that increase the speed of reactions in cells. They are catalysts in these reactions which means that they increase the speed of the reaction without being consumed or changed during the reactions. Cofactors are required by some enzymes to be able to carry out their reactions by obtaining the correct shape to bind to the other molecules of the reaction. Chelating agents are compounds that can disrupt enzyme reactions by binding to metallic ions and change the shape of an enzyme. Catechol is an organic molecule present under the surface of plants. When plants are injured, catechol is exposed to oxygen and benzoquinone is released because of the oxidation of catechol. Catecholase aids in the reaction to produce
Jim Clark. (2007). The effect of changing conditions in enzyme catalysis. Retrieved on March 6, 2001, from http://www.chemguide.co.uk/organicprops/aminoacids/enzymes2.html
That means the active site and the substrate should be exactly complementary so that the substrate can fit in perfectly. Once they collide, the substrate and. some of the side-chains of the enzyme’s amino acids form a temporary. bond so that the substrate can be held in the active site. They combine to form an enzyme-substrate complex and the enzyme can start.
Enzymes are biological catalysts - catalysts are substances that increase the rate of chemical reactions without being altered itself. Enzymes are also proteins that fold into complex shapes that allow smaller molecules to fit into them. The place where these substrate molecules fit is called the active site. The active site is the region of an enzyme where substrate molecules bind and undergo a chemical reaction. The active site consists of residues that form temporary bonds with the substrate and residues that catalyse a reaction of that substrate. (Clark, 2016)
Sequence of events when the union of a substrate with its enzyme occurs. Preliminary Work: Preliminary work was carried out to find a suitable range to collect data in a way that is appropriate. From the preliminary work I was able to determine suitable intervals of time to collect data. It showed that a volume of amylase below 4cm3 took a very long time to react thus making the experiment takes too long to do. From this I worked out that I should start.
An enzyme can be defined as a protein that acts as a catalyst in a biological system. It increases the rate of reaction by decreasing the activation energy. The catalytic power and specificity of an enzyme can be altered by the binding of certain molecules. These molecules are referred to as inhibitors. An inhibitor works to prevent the formation, or to cause the breakdown of an enzyme-substrate compound. There are two categories of inhibitors. The first being irreversible inhibitors, and the second being reversible inhibitors. Irreversible inhibitors tend to be more tightly bound, covalently or noncovalently (mostly covalently), to the enzyme than reversible inhibitors, which tend to dissociate more rapidly from the enzyme. Reversible inhibitors can be subdivided into three groups: competitive, uncompetitive, and noncompetitive.
The enzymes have active sites on their surfaces to allow the binding of a substrate through the help of coenzymes to form enzyme-substrate complex. The chemical reaction thus converts the substrate to a new product then released and the catalytic cycle proceeds.
The 'lock and key' hypothesis explains how enzymes only work with a specific substrate. The hypothesis presents the enzyme as the 'lock, and the specific substrate as 'key'. The active site binds the substrate, forms a product, which is then released. Diagram 1- a diagram showing the 'lock and key' mechanism works
Enzymes as mentioned before help speed up reactions, they generally work by bonding to a substrate, this bonding occurs at the active site. This link then forms a different molecule which will benefit its respective process. Every enzyme has its own optimum pH level to work under, if too low the enzyme will be very slow. However if too high the enzyme will then denature and be obsolete. This is why it is important to know the optimum pH level for whatev...
Enzymes work by lowering the activation energy required by molecules to start the reaction off. Enzymes also react (reversibly) with substrates (The molecule(s) that the enzyme is catalysing) this is done by forming Enzyme-substrate complex, which is then broken down into products. As well as being affected by temperature and pH enzymes optimum rate of reaction is also changed by competitive and non competitive inhibitors. Competitive inhibitors inhibit the enzyme so that enzyme-substrate complex’s cant form until it’s unblocked or there is a change in concentration in substrate, this means it takes longer to reach the optimum rate of reaction.
Also changes in pH affect the charges on the amino acids. within the active site such that the enzyme will not be able to form. an enzyme substrate complex. The pH at which an enzyme catalyses a reaction at the maximum rate is called the optimum pH. This can vary considerably from pH 2 for pepsin. to pH 9 for pancreatic lipase.
However, the initial purpose of the enzyme is to speed up reactions for a certain reason because they are “highly selective catalysts” (Castro J. 2014). The 'Secondary' of the 'Secondary' of the 'Secondary' of the 'Secondary' of the ' In other words, an enzyme is a catalyst, which is a substance that increases the rate of a reaction without undergoing changes. Moreover, enzymes work with substrates that bind to a region of the enzyme (the active site). Without enzymes, reactions wouldn’t occur and living organisms would die. For instance, the enzyme in the stomach breaks down large molecules into smaller molecules to absorb nutrition faster.
The type seen throughout the human body involve enzyme catalysis. Enzymes are present throughout many key bodily processes and keep the body from malfunctioning. An enzyme catalyzes a reaction by having the substrate bind to its active site.2 This is known as the Lock and Key Theory, which states that only the correctly oriented key (substrate) fits into the key hole (active site) of the lock (enzyme).2 Although this theory makes sense, not all experimental data has explained this concept completely.2 Another theory to better accurately explain this catalysis is known as the Induced-Fit Theory.2 This theory explains how the substrate determines the final form of the enzyme and shows how it is moderately flexible.2 This more accurately explains why some substrates, although fit in the active site, do not react because the enzyme was too distorted.2 Enzymes and substrates only react when perfectly aligned and have the same
Coenzymes are a type of cofactor and they are bound to enzyme active sites to help with their accurate functioning. Coenzymes which are directly concerned and altered in the course of chemical reactions are measured to be a kind of secondary substrate. This is as they are chemically changed as a result of the reaction unlike enzymes. However unlike the primary substrates, coenzymes can be used by a amount of different enzymes and as such are not specific. For example hundreds of enzymes are able to use the coenzyme NAD.