C. running the reaction at 70What are the functions of Allosteric enzymesWhat are some factors that affects enzyme activity?I.II.III.IV.V.VI.Enzyme activity can be regulated by allostericenzymes, feedback control, and covalentmodifications. T/FExamples of Zymogens are the proteasestrypsinogen and chymotrypsinogen. T/F?Trypsin catalyzes the removal of dipeptides frominactive chymotrypsinogen and trypsinogen togive the active proteases chymotrypsin andtrypsin. T/FThe removal of a polypeptide chain fromproinsulin produces the active form of insulin.T/F?A kinase can activate an inactive enzyme byphosphorylation, ie adding a phosphate group.T/F?A phosphatase can activate an inactive enzymeby removal of phosphate. T/F?Identify each description of an inhibitor that is eithercompetitive or noncompetitive.A. Increasing substrate reverses inhibition.B. It binds to the enzyme's surfacebut not to the active site.C. Its structure is similar to that ofthe substrate.D. Inhibition is not reversed by addingmore substrate.What are the types of Reversible inhibition?What are properties of Reversible inhibitors?For example, they cause a loss of enzyme activitythat can be restored.

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Answered: I. Enzyme activity can be regulated by…

Biochemistry

6th Edition

ISBN:9781305577206

Author:Reginald H. Garrett, Charles M. Grisham

Publisher:Reginald H. Garrett, Charles M. Grisham

Chapter27: Metabolic Integration And Organ Specialization

Section: Chapter Questions

Problem 20P: Figure 27.3 illustrates the response of R (ATP-regenerating) and U (ATP-utilizing) enzymes to energy...

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1)Catalase a. Is catalase activity endothermic or exothermic? b. What classification of enzyme is catalase? c. Give the Enzyme Commission (E.C.) number of catalase. d. Is catalase reusable? answer all and don't copy from other sources I will downvote for sure
1. What is koji and how is it used and prepared as starter enzyme in certain production of food products? list some of its application. (2 pts.) 2. Draw a schematic diagram/process flow diagram of the following enzyme prepared products: Indicate the microorganism used to make the process. (Reminder: Topic is enzyme, here you are applying enzyme-producing microorganisms to produce food/beverage products) 2.1 soy sauce (2 pts) 2.2 miso (2 pts) 2.3 sake (2 pts) 2.4 OTHER PRODUCT YOU CAN FIND involving enzyme preparation (3 pts) 3. Write the chemical reaction involve or show chemical reaction mechanism in(for) the production of the following: (Reminder: deduce the basic chemical reaction, don't provide complex reaction mechanism(s). Quiz will not give you a complex reaction :) 3.1 soy sauce (3 pts) 3.2 miso (3 pts) 3.3 sake (3 pts)
I. Indicate whether each of the following statements are true or false. _1. According to the lock-and-key model of enzyme action, the active site of an enzyme is flexible in shape. 2. In an enzyme-catalyzed reaction, the compound that undergoes a chemical change is called the substrate. 3. The nonprotein portion of a conjugated enzyme is the enzyme's active site. _4. Simple enzymes have inorganic cofactors, and conjugated enzymes have organic cofactors. 5. Vitamins are required in minute quantities for normal cellular function. 6. vitamins are found in all food groups. 7. Ribose sugars are found on one chain of the DNA molecule and deoxyribose sugars are found on the other chain of the DNA molecule. 8. A DNA molecule has a double helix at one end of the molecule and a single helix at the other end of the molecule. _9. Complementary bases are held together by covalent bonds. 10. DNA molecules always contain the nitrogenous base thymine.
Sucrase has an optimum temperature of 37°C and an optimum pH of 6.2. Determine the effect of the following on its rate of reaction: 1) no change 2) increase decrease 3) A. increasing the concentration of sucrase B. changing the pH to 4.0 C. running the reaction at 70°C What are the functions of Allosteric enzymes What are some factors that affects enzyme activity? I. II. III. IV. V. VI. Enzyme activity can be regulated by allosteric enzymes, feedback control, and covalent modifications. T/F Examples of Zymogens are the proteases trypsinogen and chymotrypsinogen. T/F? Trypsin catalyzes the removal of dipeptides from inactive chymotrypsinogen and trypsinogen to give the active proteases chymotrypsin and trypsin. T/F The removal of a polypeptide chain from proinsulin produces the active form of insulin. T/F? A kinase can activate an inactive enzyme by phosphorylation, ie adding a phosphate group. T/F? A phosphatase can activate an inactive enzyme by removal of phosphate. T/F? Identify…
Explain why catalase activity is lower at: i. Low temperature ii. High temperature
. The optimal conditions for salivary lysozyme (hydrolyzing glycoproteins of bacterial wall) are 37 C - temperature and pH is 5.2. Explain the decrease in this enzyme activity if the temperature will rise up to 60 °C and pH will be changed to 8.0. To answer the question: a) draw the graph of the velocity dependency on temperature and pH; b) calculate the relative enzyme activity if 10 mg of lysozyme catalyzes the formation of 5 uM of the product per 2 minutes. Concidor NH3: 5.
A generalized enzyme active site is shaped like a hemisphere with a radius of 45Å. The active site holds the following amino acids in a homeostatic solution (pH = 7.38): -HAVARILKHAVARILKHAVARILK- Assuming the charge is distributed uniformly along the hemisphere, determine the force at which this active site acts upon a single ATP molecule at the center of the hemisphere.
1. What are the effects of pH and temperature to catalase? What is the optimum pH and optimum temperature for catalase? 2. Explain why the rate of reaction initially increases with increase in temperature then gradually declines as the temperature is further increased. 3. Is the rate of enzymatic reaction always directly dependent on enzyme concentration? Explain. 4. Explain the effect of substrate concentration on enzyme activity. 5. What is the effect of CuSO, on the enzymatic activity of catalase? 6. Is CuSO4 an activator or inhibitor? If it is an inhibitor, what kind of inhibitor is it?
1. The optimal conditions for salivary lysozyme (hydrolyzing glycoproteins ofbacterial wall) are 37 C- temperature and pH is 5.2. Explain the decrease in this enzyme activity if the temperature will rise up to 60 °C and pH will be changed to 8.0. To answer the question: a) draw the graph of the velocity dependency on temperature and pH; b) calculate the relative enzyme activity if 10 mg of lysozyme catalyzes the formation of 5 uM of the product per 2 minutes. 2 Consider the matic reaction schee: Asnaragine + H20 Aspartate+ NH3:
3) Read the situations below and indicate which of the four methods of enzyme regulation is occurring for each. a) The energy-carrying molecule ATP is made by the enzyme ATP synthase. Muscle cells use a lot of energy and also have higher amounts of the ATP synthase enzyme than many other cell types. General mechanism of enzyme regulation: S b) Prostaglandins are messenger molecules involved in the inflammatory response, as well as the perception of pain. They are synthesized from polyunsaturated fatty acid substrates by an enzym called cyclo-oxygenase. "Ibuprofen" is the active ingredient in a variety of anti-inflammatory medications such as Motrin® and Advil®. It reduces pain and swelling by binding to a hydrophobic channel in the active site of cyclo-oxygenase, blocking the polyunsaturated fatty acids from binding to the enzyme, and therefore stopping production of prostaglandins. General mechanism of enzyme regulation:
The following statements refer to enzyme inhibition. Match the statement to the one of the following descriptors to which it is best associated. Descriptors: competitive inhibition; non-competitive inhibition; un-competitive; covalent inhibition. 9a. Inhibition is not reversed even after the inhibitor (1) is removed from solution by dialysis or drug metabolism/excretion. 9b. Inhibitor and substrate reversibly compete for occupancy of a common binding site 9c. The inhibitor binds reversibly only to the preformed E.S (enzyme-substrate) complex forming an inactive E.S.I. 9d. The inhibitor binds reversibly and independently of substrate to an allosteric site producing E.I or a ternary E.S.I complex which can't form product. 9f. The relative amount of inhibition decreases as [S] (the concentration of substrate) increases and S better competes for occupancy of the active site.
The blue structure in the diagram below is an enzyme. Please discuss what these diagrams (A and B) show. Please explain whether the grey tube within the enzyme would be effective as a drug or medication to inhibit this enzyme in both A and B. What type of drug or medication would this be called? A B ( ES ES OO #

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