Many enzymes are switched "on" by attachment of a phosphate group at a specific serine somewhere on the protein (phosphorylation). The basic reaction is: E + ATP² Ep+ ADP アSHO ELIAC フ多 (Note the "squiggles" before the backone amide and carbonyl indicate the polypeptide chain continues on either side of the serine). For phosphorylation to have this effect, there has to be some equilibrium between inactive and active forms conformations of the enzyme: [Eactive] [Einactive] Einactive 2 Eactive; K* : The same basic equilibrium must exist for the phosphorylated protein: [Ep,active] [Ep,inactive] Epinactive 2 EP,active; Kp (a) If phosphorylation increases the measured activity of the enzyme, is K* or K larger? Why? (b) Does the phosphorylation site need to be near the site where the enzyme binds its substrate (e.g. the reactant whose chemistry it catalyzes)? Why or why not?
Many enzymes are switched "on" by attachment of a phosphate group at a specific serine somewhere on the protein (phosphorylation). The basic reaction is: E + ATP² Ep+ ADP アSHO ELIAC フ多 (Note the "squiggles" before the backone amide and carbonyl indicate the polypeptide chain continues on either side of the serine). For phosphorylation to have this effect, there has to be some equilibrium between inactive and active forms conformations of the enzyme: [Eactive] [Einactive] Einactive 2 Eactive; K* : The same basic equilibrium must exist for the phosphorylated protein: [Ep,active] [Ep,inactive] Epinactive 2 EP,active; Kp (a) If phosphorylation increases the measured activity of the enzyme, is K* or K larger? Why? (b) Does the phosphorylation site need to be near the site where the enzyme binds its substrate (e.g. the reactant whose chemistry it catalyzes)? Why or why not?
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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![Many enzymes are switched "on" by attachment of a phosphate group at a specific serine somewhere
on the protein (phosphorylation). The basic reaction is:
E + ATP2 Ep + ADP
Po
SERINE
PHOSPHO SERINC
(Note the "squiggles" before the backone amide and carbonyl indicate the polypeptide chain continues
on either side of the serine). For phosphorylation to have this effect, there has to be some equilibrium
between inactive and active forms conformations of the enzyme:
[Eactive]
[Einactive]
Einactive 2 Eactive; K*
The same basic equilibrium must exist for the phosphorylated protein:
[Ep,active]
[Ep,inactive]
EP,inactive 2 Ep,active; Kp =
(a) If phosphorylation increases the measured activity of the enzyme, is K* or K larger? Why?
(b) Does the phosphorylation site need to be near the site where the enzyme binds its substrate
(e.g. the reactant whose chemistry it catalyzes)? Why or why not?](/v2/_next/image?url=https%3A%2F%2Fcontent.bartleby.com%2Fqna-images%2Fquestion%2Fb71ce249-cea7-4f69-bc85-b306daaebb91%2F8bf14bd7-4bc2-4383-8006-d35799faf585%2Faeaza_processed.png&w=3840&q=75)
Transcribed Image Text:Many enzymes are switched "on" by attachment of a phosphate group at a specific serine somewhere
on the protein (phosphorylation). The basic reaction is:
E + ATP2 Ep + ADP
Po
SERINE
PHOSPHO SERINC
(Note the "squiggles" before the backone amide and carbonyl indicate the polypeptide chain continues
on either side of the serine). For phosphorylation to have this effect, there has to be some equilibrium
between inactive and active forms conformations of the enzyme:
[Eactive]
[Einactive]
Einactive 2 Eactive; K*
The same basic equilibrium must exist for the phosphorylated protein:
[Ep,active]
[Ep,inactive]
EP,inactive 2 Ep,active; Kp =
(a) If phosphorylation increases the measured activity of the enzyme, is K* or K larger? Why?
(b) Does the phosphorylation site need to be near the site where the enzyme binds its substrate
(e.g. the reactant whose chemistry it catalyzes)? Why or why not?
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