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Figure 6-33 (Subunit interactions in an allosteric enzyme, and interactions with inhibitors and activators) depicts allosteric modulation of an enzyme through non-covalent interactions. What features of an activator might lead to different levels of enzyme regulation? Select one or more: a. ability to cause a conformational change that results in an altered activity. b. affinity for the regulatory site c. boiling point d. bond flexibility (i.e. abundance of freely rotating single bonds instead of more rigid bonds like double bonds) e. molecular weight

Figure 6-33 (Subunit interactions in an allosteric enzyme, and interactions with inhibitors and activators) depicts allosteric modulation of an enzyme through non-covalent interactions. What features of an activator might lead to different levels of enzyme regulation? Select one or more: a. ability to cause a conformational change that results in an altered activity. b. affinity for the regulatory site c. boiling point d. bond flexibility (i.e. abundance of freely rotating single bonds instead of more rigid bonds like double bonds) e. molecular weight

Biochemistry
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
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Figure 6-33 (Subunit interactions in an allosteric enzyme, and interactions with inhibitors and activators) depicts allosteric modulation of an enzyme through non-covalent interactions. What features of an activator might lead to different levels of enzyme regulation?

Select one or more:
a.

ability to cause a conformational change that results in an altered activity.

b.

affinity for the regulatory site

c.

boiling point

d.

bond flexibility (i.e. abundance of freely rotating single bonds instead of more rigid bonds like double bonds)

e.

molecular weight

**Figure 6-33: Activation of Zymogens by Proteolytic Cleavage** This diagram illustrates the activation process of chymotrypsin and trypsin from their zymogen forms. 1. **Chymotrypsinogen (inactive)**: - It spans residues 1 to 245. - It is activated by the enzyme trypsin, which cleaves it at position 15. 2. **π-Chymotrypsin (active)**: - Formed from chymotrypsinogen; active form spans residues 1, 15, 16 to 245. - Trypsin cleavage results in fragments connected by disulfide bonds. - Further undergoes autolysis by π-chymotrypsin itself to remove: - Ser14–Arg15 - Thr147–Asn148 3. **α-Chymotrypsin (active)**: - Final active form with segments: - A: residues 1 to 13 (Leu to Ile) - B: residues 16 to 146 (Ile to Tyr) - C: residues 149 to 245 (Ala onward) 4. **Trypsinogen (inactive)**: - Spans residues 1 to 245. - Initial segment: Val-(Asp)4–Lys–Ile between positions 1 to 7. 5. **Activation to Trypsin (active)**: - Achieved via enterokinase, which removes the segment Val-(Asp)4–Lys. - Results in an active peptide spanning residues 7 to 245 (starting with Ile). **Explanation**: The bars represent the primary sequences of the polypeptide chains. Cleavage points and resulting molecule structures show the transition from inactive zymogens (chymotrypsinogen and trypsinogen) to their active enzymatic forms (π-chymotrypsin, α-chymotrypsin, and trypsin), with specific amino acids at cleavage points noted. The active α-chymotrypsin form comprises three segments (A, B, C) linked by disulfide bonds.
Transcribed Image Text:**Figure 6-33: Activation of Zymogens by Proteolytic Cleavage** This diagram illustrates the activation process of chymotrypsin and trypsin from their zymogen forms. 1. **Chymotrypsinogen (inactive)**: - It spans residues 1 to 245. - It is activated by the enzyme trypsin, which cleaves it at position 15. 2. **π-Chymotrypsin (active)**: - Formed from chymotrypsinogen; active form spans residues 1, 15, 16 to 245. - Trypsin cleavage results in fragments connected by disulfide bonds. - Further undergoes autolysis by π-chymotrypsin itself to remove: - Ser14–Arg15 - Thr147–Asn148 3. **α-Chymotrypsin (active)**: - Final active form with segments: - A: residues 1 to 13 (Leu to Ile) - B: residues 16 to 146 (Ile to Tyr) - C: residues 149 to 245 (Ala onward) 4. **Trypsinogen (inactive)**: - Spans residues 1 to 245. - Initial segment: Val-(Asp)4–Lys–Ile between positions 1 to 7. 5. **Activation to Trypsin (active)**: - Achieved via enterokinase, which removes the segment Val-(Asp)4–Lys. - Results in an active peptide spanning residues 7 to 245 (starting with Ile). **Explanation**: The bars represent the primary sequences of the polypeptide chains. Cleavage points and resulting molecule structures show the transition from inactive zymogens (chymotrypsinogen and trypsinogen) to their active enzymatic forms (π-chymotrypsin, α-chymotrypsin, and trypsin), with specific amino acids at cleavage points noted. The active α-chymotrypsin form comprises three segments (A, B, C) linked by disulfide bonds.
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