Question 1

.Enzyme populations are studied with the use of ensemble methods.How would the data differ from a single-enzyme study?

Accepted Answer

In the ensemble method study,you would g

Question 2

What term describes the substance that is bound by an enzyme and converted to product?

Accepted Answer

A)  inhibitor 
B)  substrate 
C)  coenzyme 
D)  prosthetic group 
E)  cofactor 
A)  inhibitor 
B)  substrate 
C)  coenzyme 
D)  prosthetic group 
E)  cofactor

Question 3

You believe a substrate fits rigidly into a cleft like a key into a lock,but your roommate believes that the structure of the enzyme adapts to the substrate.Who is right?

Accepted Answer

You are both partially correct.Like a lo

Question 4

Examples of cofactors include

Accepted Answer

A)  Zn2+, Mg2+, and Ni2+. 
B)  biotin and thiamine pyrophosphate. 
C)  pyridoxal phosphate and coenzyme A. 
D)  biotin and thiamine pyrophosphate and pyridoxal phosphate and coenzyme A 
E)  All of the answers are correct. 
A)  Zn2+, Mg2+, and Ni2+. 
B)  biotin and thiamine pyrophosphate. 
C)  pyridoxal phosphate and coenzyme A. 
D)  biotin and thiamine pyrophosphate and pyridoxal phosphate and coenzyme A 
E)  All of the answers are correct.

Question 5

A tightly bound cofactor for an enzyme is often called a(n)_____.

Accepted Answer

A)  prosthetic group 
B)  coenzyme 
C)  allosteric activator 
D)  inorganic cofactor 
E)  None of the answers is correct. 
A)  prosthetic group 
B)  coenzyme 
C)  allosteric activator 
D)  inorganic cofactor 
E)  None of the answers is correct.

Question 6

Give an example of a reaction catalyzed by a hydrolase.

Accepted Answer

Hydrolases catalyze a reaction where a w

Question 7

What is an affinity label?

Accepted Answer

This is a substrate analog that is struc

Question 8

A reaction can occur spontaneously only if ΔG is __________________.

Accepted Answer

The answer of A reaction can occur spontaneously only if...

Question 9

What term describes an enzyme without its required cofactor?

Accepted Answer

A)  holoenzyme 
B)  coenzyme 
C)  isozyme 
D)  apoenzyme 
E)  None of the answers is correct. 
A)  holoenzyme 
B)  coenzyme 
C)  isozyme 
D)  apoenzyme 
E)  None of the answers is correct.

Question 10

What does Vmax indicate?

Accepted Answer

The maximum velocity or rate o

Question 11

The Circe effect enhances what aspect of enzyme catalysis?

Accepted Answer

A)  catalysis of substrate to product 
B)  binding of substrate 
C)  removal of product(s) from active site 
D)  prevention of enzyme inhibition 
E)  None of the answers is correct. 
A)  catalysis of substrate to product 
B)  binding of substrate 
C)  removal of product(s) from active site 
D)  prevention of enzyme inhibition 
E)  None of the answers is correct.

Question 12

What type of enzymes often display sigmoidal plots of activity versus substrate concentration?

Accepted Answer

A)  holoenzymes 
B)  monomeric enzymes 
C)  allosteric enzymes 
D)  Michaelis-Menten enzymes 
E)  isozymes 
A)  holoenzymes 
B)  monomeric enzymes 
C)  allosteric enzymes 
D)  Michaelis-Menten enzymes 
E)  isozymes

Question 13

What conclusion can be drawn concerning an inhibitor if the Vmax is the same in the presence and absence of the inhibitor?

Accepted Answer

A)  The inhibitor binds to the substrate. 
B)  The inhibitor can be overcome with sufficiently high concentrations of substrate. 
C)  The inhibitor reacts with a critical residue of the enzyme. 
D)  The inhibitor binds to the same active site as the substrate. 
E)  The KM is smaller in the presence of inhibitor. 
A)  The inhibitor binds to the substrate. 
B)  The inhibitor can be overcome with sufficiently high concentrations of substrate. 
C)  The inhibitor reacts with a critical residue of the enzyme. 
D)  The inhibitor binds to the same active site as the substrate. 
E)  The KM is smaller in the presence of inhibitor.

Question 14

A(n)_____ requires an input of energy to proceed.

Accepted Answer

A)  reaction at equilibrium 
B)  irreversible reaction 
C)  spontaneous reaction 
D)  exergonic reaction 
E)  endergonic reaction 
A)  reaction at equilibrium 
B)  irreversible reaction 
C)  spontaneous reaction 
D)  exergonic reaction 
E)  endergonic reaction

Question 15

How are the types of inhibition kinetically distinguishable?

Accepted Answer

Competitive inhibition can be overcome b

Question 16

How is the substrate bound to the active site?

Accepted Answer

The active site is a small part of the t

Question 17

What is the Michaelis-Menten equation? Define all parameters.

Accepted Answer

V₀ = V_max([S]/([S] + K_M)) Initial v

Question 18

Five KM values are given for the binding of substrates to a particular enzyme.Which has the strongest affinity when k-1 is greater than k2?

Accepted Answer

A)  150 mM 
B)  0.15 mM 
C)  150$\mu$M 
D)  1.5 nM 
E)  15000 pM 
A)  150 mM 
B)  0.15 mM 
C)  150$\mu$M 
D)  1.5 nM 
E)  15000 pM

Question 19

The site on an enzyme where the reaction that is catalyzed by the enzyme occurs is the _____.

Accepted Answer

A)  binding site 
B)  substrate site 
C)  allosteric site 
D)  regulatory site 
E)  active site 
A)  binding site 
B)  substrate site 
C)  allosteric site 
D)  regulatory site 
E)  active site

Question 20

Enzymes accelerate the rate of a chemical reaction by __________________ the activation energy of the reaction.

Accepted Answer

The answer of Enzymes accelerate the rate of a chemical...

Exam 8: Enzymes: Basic Concepts and Kinetics

.Enzyme populations are studied with the use of ensemble methods.How would the data differ from a single-enzyme study?

What term describes the substance that is bound by an enzyme and converted to product?

You believe a substrate fits rigidly into a cleft like a key into a lock,but your roommate believes that the structure of the enzyme adapts to the substrate.Who is right?

Examples of cofactors include

A tightly bound cofactor for an enzyme is often called a(n)_____.

Give an example of a reaction catalyzed by a hydrolase.

What is an affinity label?

A reaction can occur spontaneously only if ΔG is __________________.

What term describes an enzyme without its required cofactor?

What does Vmax indicate?

The Circe effect enhances what aspect of enzyme catalysis?

What type of enzymes often display sigmoidal plots of activity versus substrate concentration?

What conclusion can be drawn concerning an inhibitor if the Vmax is the same in the presence and absence of the inhibitor?

A(n)_____ requires an input of energy to proceed.

How are the types of inhibition kinetically distinguishable?

How is the substrate bound to the active site?

What is the Michaelis-Menten equation? Define all parameters.

Five KM values are given for the binding of substrates to a particular enzyme.Which has the strongest affinity when k-1 is greater than k2?

The site on an enzyme where the reaction that is catalyzed by the enzyme occurs is the _____.

Enzymes accelerate the rate of a chemical reaction by __________________ the activation energy of the reaction.

Biochemistry: An Evolving Science

Protein Composition and Structure

Exploring Proteins and Proteomes

DNA, RNA, and the Flow of Genetic Information

Exploring Genes and Genomes

Exploring Evolution and Bioinformatics

Hemoglobin: a Portrait of a Protein in Action

Catalytic Strategies

Regulatory Strategies

Carbohydrates

Lipids and Cell Membranes

Membrane Channels and Pumps

Signal-Transduction Pathways

Metabolism: Basic Concepts and Design

Glycolysis and Gluconeogenesis

The Citric Acid Cycle

Oxidative Phosphorylation

The Light Reactions of Photosynthesis

The Calvin Cycle and the Pentose Phosphate Pathway

Glycogen Metabolism

Fatty Acid Metabolism

Protein Turnover and Amino Acid Catabolism

The Biosynthesis of Amino Acids

Nucleotide Biosynthesis

Biosynthesis of Membrane Lipids and Steroids

The Integration of Metabolism

DNA Replication, repair, and Recombination

RNA Synthesis and Processing

Protein Synthesis

The Control of Gene Expression in Prokaryotes

The Control of Gene Expression in Eukaryotes

Sensory Systems

The Immune System

Molecular Motors

Drug Development

Filters

What does V_max indicate?

What conclusion can be drawn concerning an inhibitor if the V_max is the same in the presence and absence of the inhibitor?

Five K_M values are given for the binding of substrates to a particular enzyme.Which has the strongest affinity when k_-1 is greater than k₂?