1) 4 ms. Name an enzyme that requires NAD/NADH for activity.Draw the chemistry of this reaction (show mechanism).

Enzymes are highly specialized proteins that have extraordinary catalytic power, greater than that…

Answered: 1)s. Name an enzyme that requires…

Biochemistry

6th Edition

ISBN:9781305577206

Author:Reginald H. Garrett, Charles M. Grisham

Publisher:Reginald H. Garrett, Charles M. Grisham

Chapter17: Metabolism: An Overview

Section: Chapter Questions

Problem 20P

See similar textbooks

Similar questions

. 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.
Name: Date: Year/Section: Score: ACTIVITY 5.1.1 Determine the catalytic power of jack bean urease in catalyzing the hydrolysis of urea given the following conditions: At 20C, the rate constant for enzyme-catalyzed reaction is 3x104/sec The rate constant for the uncatalyzed hydrolysis of urea is 3x10-10/sec. ACTIVITY 5.1.2 Give examples of enzymatic reaction for each type of specificity 96 Copyright 2019. All Rights Reserved. 2--------
Given the following information, calculate the catalytic efficiency of the enzyme. Step by step please [S] = 100 mM k1 = 10 sec-1 k2 = 3000 sec-1 k-1 = 20 sec-1 [E]T = 1 \muμM
h. When 10 ug of an enzyme of Mr 50,000 is added to a solution containing its substrate at a concentration one hundred times the KM, it catalyzes the conversion of 75 µmol of substrate into product in 3 min. What is the enzyme's turnover number?
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.
Directions: Solve the following problem: The enzyme ẞ-methylaspartase catalyzes the deamination of ẞ-methylaspartate: CH,NH, CH OOC-CH-CH-COOOOC-CH-CH-COO+NH mesaconate Williams and Selbin The effects of hydroxymethylaspartate as an inhibitor for this enzyme was studied. The following data wer Substrate Concentration obtained: Reaction Rate without inhibitor (mM) 1 × 10-4 5 x 10-4 1.5 x 10-3 2.5 x 10-3 5 x 10-3 (mM/s) 0.026 0.092 0.136 0.150 0.165 Reaction Rate with inhibitor (mM/s) 0.010 0.040 0.086 0.120 0.142 Use Lineweaver-Burk plot to determine the KM and Vmax of the enzyme in the absence of inhibitor. Moreover, determine as well whether the inhibitor is competitive or noncompetitive. Show the graphs and calculations below.
2. Enzyme-catalyzed reactions. Answer the following with true or false. If false, explain why. (a) The initial rate of an enzyme-catalyzed reaction is independent of substrate concentration. (b) At saturating levels of substrate, the rate of an enzyme-catalyzed reaction is proportional to the enzyme concentration. (c) The Michaelis constant Km equals the substrate concentration at which velocity (v) = Vmax/2. (d) The Km for a regulatory enzyme varies with enzyme concentration. (e) If enough substrate is added, the normal Vmax of an enzyme-catalyzed reaction can be attained even in the presence of a noncompetitive inhibitor. (f) The Km of some enzymes may be altered by the presence of metabolites structurally unrelated to the substrate. (g) The rate of an enzyme-catalyzed reaction in the presence of a rate-limiting concentration of substrate decreases with time. (h) The sigmoidal shape of the v versus [S] curve for some regulatory enzymes indicates that affinity of the enzyme for the…
6F. What conformational state is stabilized by y in ATP synthase? Why might achieving this state require energy input from the PMF?
5. You discover a new cysteine protease similar to papain. Cysteine proteases are proteolytic enzymes that utilize a cysteine residue in the active site for the nucleophilic attack of a peptide bond, while a second residue acts as a base for proton abstraction in the reaction (acid base catalysis). In this novel enzyme the pKa of the cysteine residue is significantly lowered by the active site environment to pKa=4. a. Knowing that the protease shows highest activity between pH 4-6, what could be the identity of the base residue acting as a in the reaction? Explain and write the expected mechanism for the reaction. SH он
Please note the reaction expression below. Which of the following rate constants describes the breakdown of the enzyme-substrate complex? There may be more than one answer. k₂ E+S OK-2 U k₂ 0 k₁ OK.1 k3 k.3 SES EPE+P K.3 K.₂ k.
Describe the mechanism of a-chymotrypsin. Explain the roles of constituents of the catalytic triad, their modes of catalysis, and the significance of the oxyanion hole in the catalysis.
IDENTIFICATION 1. A type of reaction that occurs when an energy absorbing reaction requires an input from an energy releasing reaction. 2. What does ATP stands for? 3. What does ADP stands for? 4. When a phosphate bond is broken energy is released from ATP. This type of reaction is 5. To reconnect the phosphate with ADP energy must be absorbed from the breakdown of glucose during cellular metabolism. This type of reaction that occurs with glucose is 6. A biochemical process that involves the addition of phosphate to an organic compound. 7. How many kilojoules is released with ADP is reduced to ADP? 8. ATP is also formed from the process of cellular respiration in the mitochondria of a cell through 9. ATP is also produced in bacteria in the absence of oxygen called 10. A method in food processing which can produce small amounts of ATP is called

SEE MORE QUESTIONS

Recommended textbooks for you

Biochemistry

ISBN:

9781305577206

Author:

Reginald H. Garrett, Charles M. Grisham

Publisher:

Cengage Learning

Biochemistry

ISBN:

9781305577206

Author:

Reginald H. Garrett, Charles M. Grisham

Publisher:

Cengage Learning

SEE MORE TEXTBOOKS

1)s. Name an enzyme that requires NAD/NADH for activity. Draw the chemistry of this reaction (show mechanism).