Question 1

Which modified amino acid is found in prothrombin that allows for Ca2+ binding?

Accepted Answer

A)  acetyl lysine 
B)  phosphoserine 
C)  $\gamma$-carboxyglutamate 
D)  hydroxyproline 
E)  None of the answers is correct. 
A)  acetyl lysine 
B)  phosphoserine 
C)  $\gamma$-carboxyglutamate 
D)  hydroxyproline 
E)  None of the answers is correct. C

Question 2

How is chymotrypsinogen activated?

Accepted Answer

A)  cleavage between an Arg and Ile by chymotrypsin 
B)  cAMP binding, followed by cleavage by elastase 
C)  cleavage between an Arg and Ile by trypsin 
D)  All of the answers are correct. 
E)  None of the answers is correct. 
A)  cleavage between an Arg and Ile by chymotrypsin 
B)  cAMP binding, followed by cleavage by elastase 
C)  cleavage between an Arg and Ile by trypsin 
D)  All of the answers are correct. 
E)  None of the answers is correct. C

Question 3

How is the clotting cascade initiated?

Accepted Answer

Both intrinsic (damaged surface)and extrinsic (trauma)pathways can induce the cascade.The initial steps differ but lead to a final common path to form the fibrin clot.

Question 4

The ____________ pathway is activated by exposure of anionic surfaces on ruptured endothelial cells.

Accepted Answer

The answer of The ____________ pathway is activated by exposure...

Question 5

What protein is administered after heart attacks to increase survival odds,and what is the biochemistry involved?

Accepted Answer

Tissue-type plasminogen activator,or TPA

Question 6

Protein kinase A is activated by the binding of ________________ to specific sites on the regulatory subunit.

Accepted Answer

The answer of Protein kinase A is activated by the...

Question 7

A regulatory mechanism that is NOT readily reversible is

Accepted Answer

A)  phosphorylation. 
B)  allosteric control. 
C)  proteolytic cleavage. 
D)  All of the answers are correct. 
E)  None of the answers is correct. 
A)  phosphorylation. 
B)  allosteric control. 
C)  proteolytic cleavage. 
D)  All of the answers are correct. 
E)  None of the answers is correct.

Question 8

The less active conformational form of an allosteric enzyme is called the _____.

Accepted Answer

A)  T-state 
B)  M-state 
C)  R-state 
D)  I-state 
E)  L-state 
A)  T-state 
B)  M-state 
C)  R-state 
D)  I-state 
E)  L-state

Question 9

What is the function of aspartate transcarbamoylase?

Accepted Answer

The enzyme catalyzes the first

Question 10

The relaxed form of an allosteric enzyme has _________ affinity for the substrates than the tense form.

Accepted Answer

A)  higher 
B)  equal 
C)  lower 
D)  no 
E)  None of the answers is correct. 
A)  higher 
B)  equal 
C)  lower 
D)  no 
E)  None of the answers is correct.

Question 11

Blood clotting cascades are controlled mostly by

Accepted Answer

A)  zymogen activation. 
B)  phosphorylation. 
C)  allosteric activation. 
D)  All of the answers are correct. 
E)  None of the answers is correct. 
A)  zymogen activation. 
B)  phosphorylation. 
C)  allosteric activation. 
D)  All of the answers are correct. 
E)  None of the answers is correct.

Question 12

Multifunctional protein kinases

Accepted Answer

A)  carry out phosphorylation as well as sulfation reactions. 
B)  can modify several different targets. 
C)  conserve energy in the form of ATP from the degradation of proteins. 
D)  All of the answers are correct. 
E)  None of the answers is correct. 
A)  carry out phosphorylation as well as sulfation reactions. 
B)  can modify several different targets. 
C)  conserve energy in the form of ATP from the degradation of proteins. 
D)  All of the answers are correct. 
E)  None of the answers is correct.

Question 13

Aspartyl transcarbamylase catalyzes the first step in the synthesis of ______________.

Accepted Answer

The answer of Aspartyl transcarbamylase catalyzes the first step in...

Question 14

How is trypsin activity turned off?

Accepted Answer

A)  by dephosphorylation 
B)  by binding an inhibitor protein 
C)  by a second cleavage 
D)  All of the answers are correct. 
E)  by dephosphorylation and binding an inhibitor protein 
A)  by dephosphorylation 
B)  by binding an inhibitor protein 
C)  by a second cleavage 
D)  All of the answers are correct. 
E)  by dephosphorylation and binding an inhibitor protein

Question 15

_______________ are multiple forms of homologous enzymes within the same organism that catalyze the same reaction but with different kinetic properties.

Accepted Answer

Isozymes o

Question 16

What is (are)the most common strategy(ies)for enzymatic regulation?

Accepted Answer

A)  multiple enzyme forms 
B)  allosteric control 
C)  reversible covalent modification 
D)  proteolytic activation 
E)  All of the answers are correct. 
A)  multiple enzyme forms 
B)  allosteric control 
C)  reversible covalent modification 
D)  proteolytic activation 
E)  All of the answers are correct.

Question 17

Do allosteric enzymes follow traditional Michaelis-Menten kinetics? Draw a graph of rate relative to substrate concentration for ATCase and compare it to a Michaelis-Menten enzyme.

Accepted Answer

No,ATCase displays different kinetics.A

Question 18

The regulatory effects of substrates on allosteric enzymes are referred to as _______________ effects.

Accepted Answer

A)  homotropic 
B)  heterotropic 
C)  allotropic 
D)  All of the answers are correct. 
E)  None of the answers is correct. 
A)  homotropic 
B)  heterotropic 
C)  allotropic 
D)  All of the answers are correct. 
E)  None of the answers is correct.

Question 19

What molecule is required for the proper production of prothrombin?

Accepted Answer

A)  factor Xa 
B)  factor Va 
C)  tissue factor 
D)  fibrin 
E)  vitamin K 
A)  factor Xa 
B)  factor Va 
C)  tissue factor 
D)  fibrin 
E)  vitamin K

Question 20

Removal of protein phosphates is catalyzed by protein _____.

Accepted Answer

A)  phosphate hydrolase 
B)  phosphatase 
C)  kinase 
D)  dephosphorylase 
E)  None of the answers is correct. 
A)  phosphate hydrolase 
B)  phosphatase 
C)  kinase 
D)  dephosphorylase 
E)  None of the answers is correct.

Exam 10: Regulatory Strategies

Which modified amino acid is found in prothrombin that allows for Ca2+ binding?

How is chymotrypsinogen activated?

How is the clotting cascade initiated?

The ____________ pathway is activated by exposure of anionic surfaces on ruptured endothelial cells.

What protein is administered after heart attacks to increase survival odds,and what is the biochemistry involved?

Protein kinase A is activated by the binding of ________________ to specific sites on the regulatory subunit.

A regulatory mechanism that is NOT readily reversible is

The less active conformational form of an allosteric enzyme is called the _____.

What is the function of aspartate transcarbamoylase?

The relaxed form of an allosteric enzyme has _________ affinity for the substrates than the tense form.

Blood clotting cascades are controlled mostly by

Multifunctional protein kinases

Aspartyl transcarbamylase catalyzes the first step in the synthesis of ______________.

How is trypsin activity turned off?

_______________ are multiple forms of homologous enzymes within the same organism that catalyze the same reaction but with different kinetic properties.

What is (are)the most common strategy(ies)for enzymatic regulation?

Do allosteric enzymes follow traditional Michaelis-Menten kinetics? Draw a graph of rate relative to substrate concentration for ATCase and compare it to a Michaelis-Menten enzyme.

The regulatory effects of substrates on allosteric enzymes are referred to as _______________ effects.

What molecule is required for the proper production of prothrombin?

Removal of protein phosphates is catalyzed by protein _____.

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

Enzymes: Basic Concepts and Kinetics

Catalytic Strategies

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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

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The Control of Gene Expression in Prokaryotes

The Control of Gene Expression in Eukaryotes

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Which modified amino acid is found in prothrombin that allows for Ca²⁺ binding?