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

Human Physiology: From Cells to Systems (MindTap Course List)
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Chapter16: The Digestive System
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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

Chymotrypsinogen
(inactive)
Trypsinogen
(inactive)
245
1
6
Val-(Asp)4-Lys-Ile-
enteropeptidase
trypsin
>Val-(Asp)4-Lys
T-Chymotrypsin
(active)
Trypsin
(active)
1 15 16
245
7
245
Arg Ile
Ile
T-chymotrypsin
(autolysis)
FIGURE 6-33 Activation of zymogens by proteolytic cleavage.
Shown here is the formation of chymotrypsin and trypsin from their
zymogens. The bars represent the primary sequences of the polypep-
tide chains. Amino acid residues at the termini of the polypeptide
fragments generated by cleavage are indicated below the bars. The
numbering of amino acid residues represents their positions in the
Ser14-Arg15
+ Thr147_Asn148
a-Chymotrypsin
(active)
1 13 16
146 149
245
primary sequence of the zymogens, chymotrypsinogen or trypsino-
gen (the amino-terminal residue is number 1). Thus, in the active
Leu Ile
Тyr Ala
A
C
forms, some numbered residues are missing. Recall that the three
polypeptide chains (A, B, and C) of chymotrypsin are linked by disul-
fide bonds (see Fig. 6–18).
Transcribed Image Text:Chymotrypsinogen (inactive) Trypsinogen (inactive) 245 1 6 Val-(Asp)4-Lys-Ile- enteropeptidase trypsin >Val-(Asp)4-Lys T-Chymotrypsin (active) Trypsin (active) 1 15 16 245 7 245 Arg Ile Ile T-chymotrypsin (autolysis) FIGURE 6-33 Activation of zymogens by proteolytic cleavage. Shown here is the formation of chymotrypsin and trypsin from their zymogens. The bars represent the primary sequences of the polypep- tide chains. Amino acid residues at the termini of the polypeptide fragments generated by cleavage are indicated below the bars. The numbering of amino acid residues represents their positions in the Ser14-Arg15 + Thr147_Asn148 a-Chymotrypsin (active) 1 13 16 146 149 245 primary sequence of the zymogens, chymotrypsinogen or trypsino- gen (the amino-terminal residue is number 1). Thus, in the active Leu Ile Тyr Ala A C forms, some numbered residues are missing. Recall that the three polypeptide chains (A, B, and C) of chymotrypsin are linked by disul- fide bonds (see Fig. 6–18).
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