CH, o-CH, CH, 0- 0. CH, OH ATP ADP O. H HO H. HO. H HỌ OH phdrutk 1 H HỌ OH H Frucione& phosphate Fructose-1,6-bisphosphate SG--14.2 kJ/mol . Notably, the reaction is irreversible. What do you hink most accounts for its irreversiblity?

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
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In the following is the rate-limiting reaction of
glycolysis. Study the reaction and answer the
following questions:
o-P-O CH,
O P-O CH, o
ATP
CH, OH
H HO
ADP
M
phalructkna-1
H HỌ
OH H
OH H
Fructose-& phosphatë
Fructone- 1,6-bisphosphate
AG"-14.2 kJ/mol
1. Notably, the reaction is irreversible. What do you
think most accounts for its irreversiblity?
Choose...
2. If you know that the molecule fructose-6-phosphate
(F-6-P) binds the enzyme PFK-1 at its active site.
Fructose 2,6-bisphosphate (F-2,6-BP) is a molecule
that binds the enzyme at a site other than the active
site and activates it. Mg+2 is required by the enzyme to
catalyze the reaction. What do you think the most
accurate descriptions of each of F-6-P/F-2,6-BP/and
Mg respectively are?
Choose...
Transcribed Image Text:Badges Course dashboard In the following is the rate-limiting reaction of glycolysis. Study the reaction and answer the following questions: o-P-O CH, O P-O CH, o ATP CH, OH H HO ADP M phalructkna-1 H HỌ OH H OH H Fructose-& phosphatë Fructone- 1,6-bisphosphate AG"-14.2 kJ/mol 1. Notably, the reaction is irreversible. What do you think most accounts for its irreversiblity? Choose... 2. If you know that the molecule fructose-6-phosphate (F-6-P) binds the enzyme PFK-1 at its active site. Fructose 2,6-bisphosphate (F-2,6-BP) is a molecule that binds the enzyme at a site other than the active site and activates it. Mg+2 is required by the enzyme to catalyze the reaction. What do you think the most accurate descriptions of each of F-6-P/F-2,6-BP/and Mg respectively are? Choose...
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