24. What is the role of hydrophobic interaction in the active site of this enzyme? A. It keeps the substrate in place during enzymatic reaction. B. It changes the functional group location of the substrate. C. It keeps amino acids in the active site in position. D. It allows permanent binding of substrate to the active site.
24. What is the role of hydrophobic interaction in the active site of this enzyme? A. It keeps the substrate in place during enzymatic reaction. B. It changes the functional group location of the substrate. C. It keeps amino acids in the active site in position. D. It allows permanent binding of substrate to the active site.
Human Anatomy & Physiology (11th Edition)
11th Edition
ISBN:9780134580999
Author:Elaine N. Marieb, Katja N. Hoehn
Publisher:Elaine N. Marieb, Katja N. Hoehn
Chapter1: The Human Body: An Orientation
Section: Chapter Questions
Problem 1RQ: The correct sequence of levels forming the structural hierarchy is A. (a) organ, organ system,...
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![23. The active site of an enzyme in is shown below. Based on the interaction of the catalytic site of the enzyme to the 17th
position of the steroid ring, what is the sequence of the molecules (inhibitors) based on increasing affinity to the active
site?
A. Molecule 1 → Molecule 2 → Molecule 3
B. Molecule 3→ Molecule 1→ Molecule 2
C. Molecule 3 → Molecule 2 → Molecule 1
D. Molecule 2 → Molecule 1→ Molecule 3
Catalytic
end
Ile 14
Gly 13
The 190
NADP(H)
CONH,
Ho.
Tyr 153/
e 192 Gly 94
Met 193/
B.
Ou 282
Leu 9
Hydrophilic
recognition
end
His 221
218
S 222
Closed
24. What is the role of hydrophobic interaction in the active site of this enzyme?
A. It keeps the substrate in place during enzymatic reaction.
B. It changes the functional group location of the substrate.
C. It keeps amino acids in the active site in position.
D. It allows permanent binding of substrate to the active site.
25. As observed from the molecular structures, the inhibitors need to be structurally similar to estrone. Why is this so?
A. The principle of binding of the inhibitor is based on the presence of steroid rings.
B. Inhibitor binding needs to establish permanent interactions with the catalytic site.
C. Estrogen is a common molecule which makes its structure easy to manipulate.
D. The establis hment of hydrogen bonds need to be compatible with the active site.](/v2/_next/image?url=https%3A%2F%2Fcontent.bartleby.com%2Fqna-images%2Fquestion%2F508d072f-fc60-4e69-9f21-4c19d65b2c2d%2Fc5b1cafe-3579-4aa5-bf38-d551fe6f2441%2F61ofdre_processed.jpeg&w=3840&q=75)
Transcribed Image Text:23. The active site of an enzyme in is shown below. Based on the interaction of the catalytic site of the enzyme to the 17th
position of the steroid ring, what is the sequence of the molecules (inhibitors) based on increasing affinity to the active
site?
A. Molecule 1 → Molecule 2 → Molecule 3
B. Molecule 3→ Molecule 1→ Molecule 2
C. Molecule 3 → Molecule 2 → Molecule 1
D. Molecule 2 → Molecule 1→ Molecule 3
Catalytic
end
Ile 14
Gly 13
The 190
NADP(H)
CONH,
Ho.
Tyr 153/
e 192 Gly 94
Met 193/
B.
Ou 282
Leu 9
Hydrophilic
recognition
end
His 221
218
S 222
Closed
24. What is the role of hydrophobic interaction in the active site of this enzyme?
A. It keeps the substrate in place during enzymatic reaction.
B. It changes the functional group location of the substrate.
C. It keeps amino acids in the active site in position.
D. It allows permanent binding of substrate to the active site.
25. As observed from the molecular structures, the inhibitors need to be structurally similar to estrone. Why is this so?
A. The principle of binding of the inhibitor is based on the presence of steroid rings.
B. Inhibitor binding needs to establish permanent interactions with the catalytic site.
C. Estrogen is a common molecule which makes its structure easy to manipulate.
D. The establis hment of hydrogen bonds need to be compatible with the active site.
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