However, when the substrate enters the active

Enzymes globular proteins with catalytic properties, i. ie they increase the reaction rate by lowering the activation energy (minimum energy required to start the reaction). Reagents and substrates fit into the enzyme active center, where they spent together to react and form the product easier. Chemistry section covers catalysis in more detail (or will do, if it exists). Lock and key hypothesis of enzyme: in this hypothesis, the active center of the enzyme is in addition to the substrate and the reaction proceeds as below

substrate is the key that fits exactly in the castle of the enzyme. This modified version lock theory. Here, the active center of the enzyme does not add to the substrate. However, when the substrate enters the active center, its shape is changed so that the substrate is suitable for sure. Enzyme groups: oxidoreductases catalyze all redox reactions (ie reactions involving the transfer of oxygen and hydrogen). Dehydrogenase and oxidase both oxidoreductases. catalyze the transfer of chemical / functional groups between substances, e. by enzymes and phosphorylase. Hydrolyzing enzyme catalyzing the hydrolysis reactions e. by lipase, protease and carbohydrases. no reaction, which break down large molecules into smaller ones. no reaction, where smaller molecules are built to high. However, anabolic and catabolic reactions are classified as metabolic reactions (as metabolism). Council to remember which way around the anabolic and catabolic go. Remember that the positive anode and anabolic increases (+) while the negative cathode and catabolic destroyed (C-). C, the optimum temperature ~ 40 >> << C (body temperature). If the temperature is high enough energy to destroy the tertiary structure of the enzyme (weak hydrogen bonds that define the shape of the molecules are destroyed). This changes the shape of the active center so that the substrate is not suitable, an enzyme called denatured. If the temperature is very low, simple substrate molecules have enough energy to move the active center and be a catalyst. Effect of pH on enzyme activity: the optimal pH for each enzyme is different depending on where in the body it should work (pepsin works best in acidic conditions and is in the stomach, trypsin works best in alkali conditions). Schedule has the same form as for temperature. ions (see chemistry for more information on pH). If the concentration of H

too high, the presence of ions alters the tertiary structure of proteins, breaking the weak hydrogen bonds that define the shape of molecules, again changing the shape of the active center so that the substrate does not fit. The influence of substrate concentration on enzyme activity: Influence of enzyme concentration on enzyme activity: schedule similar to the above, until the excess substrate is present, the reaction rate increases with the concentration of enzymes. If there is no excess, no further increase is possible (there are no more available substrate for the catalyst, regardless of how much enzyme is added). Typically, the concentration of substrate is about 1000 times the concentration of enzyme. This is where the inhibitor molecule binds to the enzyme from the active center to substrate can no longer suitable, and the enzyme is inactivated. (In fact, the concentration of the enzyme is reduced). Cyanide is a noncompetitive inhibitor, it inhibits cytochrome oxidase, preventing electron transfer during respiration. In this case, molecule inhibitor, has the same form as the substrate because the substrate and inhibitor compete for the active site. When the inhibitor is active centers, decreasing the likelihood that the enzyme-substrate complexes form. Malonat is a competitive inhibitor, which inhibits succinate dehydrogenase (competes with succinate molecules). If an excess of D (final product) is formed, it does not inhibit an enzyme that converts B (to be noncompetitive inhibitor in the other case it Wouldnt work at high concentrations). It actually stops the production of B, and hence, C and D. As no more than D is, the excess D eventually be used. When this happens, the brake response

B rises and the system starts again. This is an example

negative feedback and is useful in the fact that an infinite number of unnecessary final product is produced. not a protein whose presence is necessary for the functioning of certain enzymes. There are three basic types:

inorganic / mineral ions, in combination with enzyme and substrate are likely lasix online no prescription to make education an enzyme-substrate complex easier. Saliva amylase requires chloride ions while thrombokinase requires Ca

ion activators. are organic molecules. NAD is one of the enzyme, which picks up excess hydrogen ions, which helps maintain pH dehydrogenase enzyme. Prosthetic group of organic molecules that are physically associated with the enzyme, e. heme, the molecule must catalase. enzymes can be used for the production and detection of some compounds because, unlike inorganic catalysts, they are specific and not give harmful byproducts. They can also operate at low temperatures and pressures, as well as a range of pH (more cost effective than inorganic catalyst, which may require high temperature in order to work). enzymes can be used to identify specific compounds. For example it uses glucose analysis:

first reaction catalyzed by glucose oxidase, the second peroxidase. Obviously, the appearance of color D means that the connection of glucose in the initial sample. Some enzymes are changed so that they will be stable at high temperatures. For example, subtilisin modified for use in detergent so it will work effectively for 60

From wash! )

Immobilization of enzymes: the enzyme attached to an inert material, e. , the membrane or ceramic / polymer gel. Reactants can now be transferred to the enzyme almost continuously, while the contamination of products occurs. Efficiency increases as the enzyme can be easily restored quickly. Production of fructose enzymatic hydrolysis of starch: First

osaharyvayuschyh enzymes are being used to break dextrins to glucose. Finally, immobilized hlyukozoizomeraza used to convert glucose into fructose. The product, high fructose corn syrup (HFCS) is used in the U.S., in Europe its production is limited to protect the farmers of sugar beet. .