The glycogen cleavage reaction forming glucose 1-phosphate is readily reversible. What is the primary reason that this reaction proceeds? O The equilibrium ratio of orthophosphate to glucose 1-phosphate is very low. Glucose 1-phosphate is phosphorylated. The ratio of orthophosphate to glucose 1-phosphate is very high. The value of AGo is low. The value of AGo is high What might be the result of a mutation in the functional lysine in glycogen phosphorylase? The enzyme would be unable to bind glycogen. The N-terminal domain would rotate away from the C-terminal domain, moving the enzyme into the T state. The N-terminal domain would rotate away from the C-terminal domain, moving the enzyme into the R state The enzyme would be less likely to bind Pi. The enzyme would no longer bind pyridoxal phosphate.
The glycogen cleavage reaction forming glucose 1-phosphate is readily reversible. What is the primary reason that this reaction proceeds? O The equilibrium ratio of orthophosphate to glucose 1-phosphate is very low. Glucose 1-phosphate is phosphorylated. The ratio of orthophosphate to glucose 1-phosphate is very high. The value of AGo is low. The value of AGo is high What might be the result of a mutation in the functional lysine in glycogen phosphorylase? The enzyme would be unable to bind glycogen. The N-terminal domain would rotate away from the C-terminal domain, moving the enzyme into the T state. The N-terminal domain would rotate away from the C-terminal domain, moving the enzyme into the R state The enzyme would be less likely to bind Pi. The enzyme would no longer bind pyridoxal phosphate.
Biochemistry
6th Edition
ISBN:9781305577206
Author:Reginald H. Garrett, Charles M. Grisham
Publisher:Reginald H. Garrett, Charles M. Grisham
Chapter26: Synthesis And Degradation Of Nucleotides
Section: Chapter Questions
Problem 10P
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