None Environmental conditionthat can affect enzymeactivityA substance that lowersthe activation energy for achemical reaction; enzymesare biological (mainlyprotein based) versions ofthis substanceOne process by which ametabolic pathway can beinhibited; the product ofreaction or metabolicpathway inhibits and earlierenzyme to shut down thepathway when enough ofthe product is producedA substance that binds toan apoenzyme to form theholoenzyme which is theactive form of the enzyme1. Substrate concentration2. pH3. Feedback inhibition4. Co-factor/co-enzyme5. CatalystDon't use Ai foranswering this

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Biochemistry

6th Edition

ISBN:9781305577206

Author:Reginald H. Garrett, Charles M. Grisham

Publisher:Reginald H. Garrett, Charles M. Grisham

Chapter18: Glycolysis

Section: Chapter Questions

Problem 21P

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Two experiments were performed with the enzymeribonuclease. In experiment 1 the effect of increasingsubstrate concentration on reaction velocity was measured.In experiment 2 the reaction mixtures were identical tothose in experiment 1 except that 0.1 mg of an unknowncompound was added to each tube. Plot the data accordingto the Lineweaver-Burk method. Determine the effect of theunknown compound on the enzyme’s activity. (Substrateconcentration is measured in millimoles per liter. Velocity ismeasured in the change in optical density per hour.)
Catalane in un enzyme that speeds up the decomposition ot hydrogen peroxide H0) to waler and axvgen. Students conducted two investigationa to determine the ideal conditions for the function of catalane. One wetigation compared catalase activity at diferent values of pH. The other imvestigation compared catalane activity al diferent temperatures. Enayme Activity ve pH Enzyme Aetivity vs Temperature Teate C) According to the data in the graphs, which pH and temperature combination provides the BEST conditions for catalase to tunction? Anury lag a
Which of the following statements DOES NOT describe the enzyme active site? O tis where the substrate binds. O is where catalysis occurs, Ctis wherc aninhibilormay bind.
Enzymes act by reducing the activation energy of areaction. Describe several ways in which this isaccomplished.
-n f estion B I ut of question PF budy As you increase the amount of substrate in a reaction (while keeping the enzyme concentration the same): Select one: O A. The amount of products formed should decrease OB. The amount of products formed should remain the same OC. The amount of products formed should increase Clear my choice Mixing hydrogen peroxide with an enzyme different than catalase (such as lactase) should also result in the formation of products. Select one: O True O False The temperature at which an enzyme works best can differ from enzyme to enzyme. Select one: O True False B 7 O
Suicide substrates are substances that resemble the substrate,but when incorporated into the active site they form a covalent bond with the enzyme, permanently inhibiting it. Thesemolecules have been used to label the amino-acid side chainsthat are involved in the catalytic reaction occurring withinthe active site. This is usually accomplished by hydrolyzingthe inhibited enzyme. How could an investigator identify theamino acid bound to the suicide substrate molecule?
A catalase is an antioxidant enzyme that requires ferric ion for catalysis. Under conditions of iron deficiency, when the catalase lacks ferric ion, it would be referred to as: O prosthetic group O holoenzyme ароenzyme coenzyme
Given the following enzyme catalyzed reaction, identify the class and subclass of the enzyme involved: %3D CH3CH CH,CH2 SCOA SCOA COO СО
Phosphorylation is one of the most common mechanisms for regulating the activity of enzymes thatfunction in metabolic pathways. What might the advantage be of exploiting a covalent modificationthat makes use of ATP as a substrate to control the activity of these enzymes?
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Another member of your research group studied the kinetics of theGAPDH from the organism. They also determined if the GAPDH fromthe organism is also inhibited by the known inhibitor of GAPDH fromhumans. From the following data, determine the KM (Michaelis-Menten Constant) and the Vmax(maximum velocity) of the enzyme without and with the inhibitor.
(Part A) Coenzyme-dependent enzymes can catalyze the general transformations shown below. What would be the best coenzymes to use for the two steps in the scheme, and why? в CO2H R SCOA R

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