enzyme 2. When an enzyme catalyzes a reaction: a. Substrate(s) bind in the active site b. Products bind in the active site c. The shape of the enzyme remains unchanged d. The enzyme is consumed by the reaction 3. Which of the following would interfere most with the ability of an enzyme to catalyze a reaction? a. Reduced concentration of substrate available b. Reduced concentration of product available c. Increased concentration of substrate available d. A change in the pH 4. Feedback mechanisms
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Study of stereospecificity in mushroom tyrosinase and the inhibiting effects of thiourea‚ cinnamic acid and benzoic acid BIOL/BIOC 393 L03 Dr. Judit Moldovan Submitted: Nov. 22nd‚ 2010 By: Jackie Minnick (Partners Amanda Verwoerd & Kersti Ojamaa) Study of stereospecificity in mushroom tyrosinase and the inhibiting effects of thiourea‚ cinnamic acid and benzoic acid. Jackie Minnick This paper reports experiments on the stereospecificity observed in the monophenolase and diphenolase activities
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exist. Sigmoidal curve- indicates cooperative behavior of enzymes. (ATCase: Aspartate is the substrate while carbomyl phosphate is constant). Reaction rate of CTP= sigmoidal‚ higher substrate conc. (aspartate) needed Vmax- changes when a reaction takes place in the presence of noncompetitive inhibitor. Competitive inhibitors- bind to the same site because of its similarity of structure with substrate. *CTP is very different in terms of the structure and bounds to the diffent site of ATCase
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Experiment #1 1. At substrate concentration‚ the enzyme is working at “maximum efficiency.” With a concentration at 40‚ it produced 2‚339 products. 2. The maximum velocity of a reaction is reached when the active sites are almost continuously filled. Increased substrate concentration after this point will not increase the rate. The reaction rate increases as substrate concentration is increased. It will soon level off though. 3. When the concentration is at low substrate‚ most of the enzyme
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produced in the Krebs cycle is important as this is the dependant variable. Enzymes are proteins that can effectively increase the rate of a reaction by lowering the required energy (activation energy) needed in order for the reaction to occur. The substrate must be specific to the active site because if they were
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Enzyme Catalase Activity in Reaction with the Substrate Hydrogen Peroxide Abstract We performed these experiments to observe the effects of enzymes on the rate of reactions. We tested and compared the activity of the enzyme catalase on the substrate H2O2 in various states and percentages‚ and observed the absorption values of the enzyme-substrate relationship at different concentrations. Our results show that the more substrate available‚ the quicker the reaction will happen except in one test
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Research Question Does the concentration of substrate (H2O2 (hydrogen peroxide)) have an effect on the activity of the enzyme (catalase)? Theory The higher the substrate concentration the more quickly product is produced (rate of reaction increases) until enzyme saturation is reached at which time more substrate has no further effect. Enzymes such as Catalase are protein molecules which are found in living cells. They are used to speed up specific reactions in the cells. They are all
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Results from the tests showed a negative correlation‚ this means that the more diluted the solution of 95% ethanol was‚ the less oxygen gas collected. Controlling a number of factors which include human error‚ temperature change‚ pH levels‚ substrate concentrations and ensuring a controlled experimental environment will work to increase the accuracy of the experiment. Purpose/Hypothesis If
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Additional analysis questions for Part 1: 1. Which part of this model represents the Chainobead polymerase enzyme? The person constructing the chainobeads represents the chainobead polymerase enzyme. 2. Which part of this model represents the substrate?
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relationship between the attenuation of light and concentration of the material through which the light is travelling. It states the absorbance is proportional to the concentration when a parallel beam of monochromatic radiation of equal pathlength is passing through a homogenous concentration. A=εbc‚ where A is absorbance‚ ε is molar absorptivity (L molˉ1cmˉ1)‚ b is the pathlength (1cm) and c is the concentration of the solution (L molˉ1) At high concentration beer lambert law is not applied because of
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