5 QUESTION 5Enzymes reduce entropy of their substrates in reactions with multiple reactants. This is possiblebecause:Entropy reduction does not require energy. It can happen on its own.Thermal kinetic energy provides enough energy to reduce the entropy.High energy molecules like ATP provide energy that allows for the reduction in entropy.Bonding between enzyme and substrates causes an enthalpy change that counteracts thereduction in entropy.Click Save and Submit to save and submit. Click Save All Answers to save all answers.un Population.pdfHuman Population.pdfPOF

The enzyme is a biomolecule, often a protein, that catalyzes a reaction that can be either…

Answered: QUESTION 5 Enzymes reduce entropy of…

Biochemistry

9th Edition

ISBN:9781319114671

Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Publisher:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Chapter1: Biochemistry: An Evolving Science

Section: Chapter Questions

Problem 1P

See similar textbooks

Similar questions

QUESTION 22 When the final product of a series of enzymatically-catalyzed reactions binds to the first enzyme in the pathway to limit its production, it generally uses ___ because the structure of this final product is generally not similar to that of any of the enzyme's normal substrates. Allosteric activation Zymogen activation Covalent modification Competitive inhibition Allosteric inhibition
QUESTION 10 Catabolic metabolic pathways generally involve what type of chemical reactions? Reactions that are spontaneous inside an active cell. Reactions that require the use of energy. Reactions that result in the release energy. Reactions that build complex molecules.
QUESTION 2 Compound X is a potent competitive inhibitor of enzyme Y. Addition of 10 nM compound X increases the measured Km for enzyme Y by a factor of 3. What are the values for a and a' under these conditions? O a of 1 and a' of 3 a of 1/3 and a' of 1 O a of 1 and a' of 1/3 a of 3 and a' of 1 Show transcribed image text
Question 1. Enzymes, proteins and deoxyribonucleic acid (DNA) are important biological macromolecules. Enzymes are not only speed up the reaction, but also are necessary for DNA reproduction. e) Michaelis - Menten Kinetics model explains how reaction rates are depending on the concentration of enzyme and substrate. i. What is meant by the saturation of enzyme? ii. A decrement in enzyme activity is known as enzyme inhibition. Based on normal enzyme activity, explain the enzyme kinetics for competitive inhibition and noncompetitive inhibition, as shown in Figure 1. Normal enzyme Competitive inhibitor Noncompetitive inhibitor Substrate concentration Figure 1: Enzyme inhibition f) What is the importance of cofactor in the enzyme activity? Give an example of a disease that is related with cofactors. Rate of reaction
QUESTION 26 In the câtalytic mechanism of an aminotransferase, one substrate binds and reacts, leaving behind an amine group covalently attached to the enzyme, then the second substrate can bind. This is best described as: Association dissociation O random single displacement ping-pong or double displacement O ordered single displacement QUESTION 27 For a Michaelis-Menten enzyme, kį = 4.0 x 10° M's,k] = 2.0 x 10° s-!, and kɔ = 5.0 x 10 s What is its Km? Give your answer in uM in four significant figures in normal notation. QUESTION 28 Which amino acid is most likely to break an alpha helix? Click Save and Submit to save and submit. Click Save All Answers to save all answers. 798 Mostly cloudy P Type here to search
QUESTION 38 In a 250µl reaction containing 0.3 nmol of a Michaelis enzyme with Km = 4.4 x 10 M and saturating substrate concentration, product was formed at an initial velocity of 6.3 x 10 M min-1. What is kcat for this enzyme? Give your answer in 3 sigfigs in scientific notation, for example 1.20 e -3 Click Save and Submit to save and submit. Click Save All Answers to save all answers. O Type here to search 78°F Mostly cloudy End 4) DII PrtScn F8 Home F9 F6 F2 F3 F4 *- & 7 8. 4. #3
Question 4 Lipids are the biomolecules of choice for storage of metabolic energy because they: O yield a large amount of energy after complete oxidation. O yield a large amount of energy after complete reduction O yield a large amount of energy after complete trans isomerization yield a large amount of energy after complete hydrolysis
QUESTION 3 Biocatalysts are effective because: O a. They increase the activation energy of a reaction Ob. They stabilize the transition state O. They decrease the rate of the reaction Od. They decrease the activation energy of a reaction QUESTION 4 Which of the following statements is INCORRECT regarding L-amino acids and D-amino acids? O NH3 group on the left of the chiral carbon in both isomers O b. They are nonsuperimposable mirror images of each other O NH group on the left of chiral carbon in L isomers Od. They are enantiomers
QUESTION 6 If a drug is built to bind to the active site of the enzyme, it will prevent substrate binding. This drug would be classified as a(n) allosteric activator. O allosteric inhibitor. noncompetitive inhibitor. competitive inhibitor.
QUESTION 1 Enzyme concentration affects the rate of an enzymatic reaction by. OIt actually has no effect on the reaction rate. by increasing the rate of reaction when it is low. by decreasing the rate of reaction when it is high O by increasing the rate of reaction when it is high. Click Save and Submit to save and submit. Click Save All Ansuwers to save all answers. 16 Machook 20 F3 000 O00 F4 F2 F5 F6 F7 F8 $ & * 4 6 7 8 # 3
Question 4 There are many functions of enzymes that are essential for cellular processes. A ligase is used to O split larger molecules with the use of water. split a compound by using water. removes electrons from an element. O join two molecules. Question 5 Apoenzymes are always active. inactive when they are not bound to their cofactors and/or coenzymes. built from holoenzymes. O found only in eukaryotic cells. Question 6 Allosteric inhibitors will change the shape of the substrate so that enzymatic function increases. change the shape of the substrate so that enzymatic function decreases. change the shape of the enzyme so that enzymatic function decreases. change the shape of the enzyme so that enzymatic function increases.
QUESTION 18 In the serine protease trypsin, the specificity for one substrate over another describes what type of catalysis? OA. proximity B. acid-base C. covalent OD. metal ion

SEE MORE QUESTIONS

Recommended textbooks for you

Biochemistry

ISBN:

9781319114671

Author:

Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Publisher:

W. H. Freeman

Lehninger Principles of Biochemistry

Biochemistry

ISBN:

9781464126116

Author:

David L. Nelson, Michael M. Cox

Publisher:

W. H. Freeman

Fundamentals of Biochemistry: Life at the Molecul…

Biochemistry

ISBN:

9781118918401

Author:

Donald Voet, Judith G. Voet, Charlotte W. Pratt

Publisher:

WILEY

Biochemistry

ISBN:

9781319114671

Author:

Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Publisher:

W. H. Freeman

Lehninger Principles of Biochemistry

Biochemistry

ISBN:

9781464126116

Author:

David L. Nelson, Michael M. Cox

Publisher:

W. H. Freeman

Fundamentals of Biochemistry: Life at the Molecul…

Biochemistry

ISBN:

9781118918401

Author:

Donald Voet, Judith G. Voet, Charlotte W. Pratt

Publisher:

WILEY

Biochemistry

ISBN:

9781305961135

Author:

Mary K. Campbell, Shawn O. Farrell, Owen M. McDougal

Publisher:

Cengage Learning

Biochemistry

ISBN:

9781305577206

Author:

Reginald H. Garrett, Charles M. Grisham

Publisher:

Cengage Learning

Fundamentals of General, Organic, and Biological …

Biochemistry

ISBN:

9780134015187

Author:

John E. McMurry, David S. Ballantine, Carl A. Hoeger, Virginia E. Peterson

Publisher:

PEARSON

SEE MORE TEXTBOOKS