Michaelis-Menten Kinetics

Enzymes are known as protein catalysts. The name protein catalyst suggests that most enzymes are made of proteins. A catalyst is a substance that speeds up chemical reactions without being consumed in the process. (Giuseppe, M 2002, p.69). After a reaction has been catalyzed, the catalyst can be used again to catalyze the same reaction. Enzymes reduce the activation energy (minimal energy) it takes for a reaction to take place. Enzymes can either catabolize (destroy), or anabolize (build up) a chemical system.

From Figure 4, the maximum velocity is the highest point on the curve and the constant (km) is ½ the maximum velocity. However, it is difficult to estimate Vmax using Michaelis-Menten curve with precision since the limits of the hyperbolic curve deviate at varying concentrations of the substrate. The data can be linearized using Lineweaver-Burk Plot to obtain Vmax and Km as follows: Slope=Km/V_max

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.

Enzymes are types of proteins that work as a substance to help speed up a chemical reaction (Madar & Windelspecht, 104). There are three factors that help enzyme activity increase in speed. The three factors that speed up the activity of enzymes are concentration, an increase in temperature, and a preferred pH environment. Whether or not the reaction continues to move forward is not up to the enzyme, instead the reaction is dependent on a reaction’s free energy. These enzymatic reactions have reactants referred to as substrates. Enzymes do much more than create substrates; enzymes actually work with the substrate in a reaction (Madar &Windelspecht, 106). For reactions in a cell it is

Enzymes are biological catalysts, which speed up the rate of reaction without being used up during the reaction, which take place in living organisms. They do this by lowering the activation energy. The activation energy is the energy needed to start the reaction.

In the lab it uses the definition equilibrium constant, what is meant when equilibrium constant is referred to, is the ratio of the molar concentrations of the reactants and products for the reaction. But in order for the ratio to be accurate the system must of reached equilibrium and temperature must have stayed constant. The value of Keq obtained from all our experiments was nearly

Enzymes are specific-type proteins that act as a catalyst by lowering the activation energy of a reaction. Each enzyme binds closely to the substrate; this greatly increases the reaction rate of the bounded substrate. Amylase enzyme, just like any other enzyme, has an optimum PH and temperature range in which it is most active, and in which the substrate binds most easily.

Enzymes are proteins that act as catalysts during a biochemical process. Catalysts are non-changing enzymes that can increase or decrease activation energy to accelerate or slow down a biochemical reaction without using additional energy.

Enzyme binds to a substrate molecule and catalyzes a reaction, thereby converting the substrate into product. Enzyme-catalyzed reactions proceed through an enzyme-substrate (ES) complex as shown in equation 3 (Boon, 2007).

In this experiment we tested the effects that enzymes and substrate have on chemical reaction rates, which is the rate at which chemical reactions occur.. This experiment tested how different concentrations of enzyme and substrate affected the light absorption measurements on a spectrophotometer. The experiment also tested how temperature affected the light absorption, and in a separate test, the effect of the enzyme inhibitor hydroxylamine was also tested. In the first test conducted, 3 different concentrations of enzyme, and three different concentrations of substrate were measured in a spectrophotometer. For the enzyme and the substrate, the measurements got higher as the concentrations were higher, but the over measurements of the substrate were smaller than those of the enzyme. In the second test conducted, the medium concentration enzyme was tested under the temperatures; 4°C, 23°C, 37°C, and 60°C. The measurements in this test got higher as the temperature got higher, but did the measurements under 4°C were overall significantly higher than the other temperature measurements. Lastly, the last test conducted showed that the measurements of the substance with 0 and 1 drop of hydroxylamine inhibitor went up, but the measurements of the enzyme with 5 drops of hydroxylamine inhibitor stayed rather low and did not change much. In conclusion, these experiments showed that chemical reaction rates are sped up with higher concentrations of enzyme, substrate,

Enzymes are proteins that catalyze (speed up) biological reactions in an organism by lowering the activation energy of a reaction. They do this by either straining the bonds in a molecule so that is easier to break up or by placing separate molecules/elements close to each other so that bonds are formed. Enzyme activity is influenced by an array of different factors such as enzyme concentration, substrate concentration, temperature, pH and inhibitor concentration. All of these affect the rate of reactions of enzymes and some such as temperature, inhibitors and pH can under circumstances cause enzymes to become permanently affected. Catalase is an enzyme found in almost all organisms on earth exposed to Oxygen.

The slope of this graph, calculated using the average rise / run is also 1. As [S2O8-2] is held constant during these trials, the exponent n for [I-] equals one. The k constant can now be calculated.

Abstract: From the shown calculations & graphical analysis, the experimentally determined rate law is rate = K[I-].969 [H2O2].991 and the experimentally determined activation energy is 59.50 kJ/mole.

Enzymes are very efficient catalysts for biochemical reactions. They speed up reactions by providing an alternative reaction pathway of lower activation energy. Like all catalysts, enzymes take part in the reaction - that is how they provide an alternative reaction pathway. But they do not undergo permanent changes and so remain unchanged at the end of the reaction. They can only alter the rate of reaction, not the position of the equilibrium. Enzymes are usually highly selective, catalyzing specific reactions only. This specificity is due to the shapes of the enzyme molecules.

Enzymes are proteins that act as catalysts and help reactions take place. In short, enzymes reduce the energy needed for a reaction to take place, permitting a reaction to take place more easily. Some enzymes are shape specific and reduce the energy for certain reactions. Enzymes have unique folds of the amino acid chain which result in specifically shaped active sites (Frankova Fry 2013). When substrates fit in the active site of an enzyme, then it is able to catalyze the reaction. Enzyme activity is affected by the concentrations of the enzymes and substrate present (Worthington 2010). As the incidence of enzyme increases, the rate of reaction increases. Additionally, as the incidence of substrate increases so does the rate of reaction.