A balance equation that showing the effect of simultaneous activation of glycogen phosphorylase and glycogen synthase including the reaction catalyzed by phosphoglucomutase and UPD-glucose pyrophosphorylase should be written. Concept introduction: Enzyme phosphoglucomutase breakdown glycogen into glucose 6-phosphate. The enzyme phosphoglucomutase converts glucose 6-phosphate into glucose 1-phosphate. glucose 1-phosphate reacts with UTP (Uridine-5’-triphosphate) to form UDP − glucose. UDP − glucose act as the substrate of the glycogen synthesis process.

Question

Want to see the full answer?

Answer 1

Question

Chapter 21, Problem 32P

Interpretation Introduction

Interpretation:

A balance equation that showing the effect of simultaneous activation of glycogen phosphorylase and glycogen synthase including the reaction catalyzed by phosphoglucomutase and UPD-glucose pyrophosphorylase should be written.

Concept introduction:

Enzyme phosphoglucomutase breakdown glycogen into glucose 6-phosphate.

The enzyme phosphoglucomutase converts glucose 6-phosphate into glucose 1-phosphate.

glucose 1-phosphate reacts with UTP (Uridine-5’-triphosphate) to form UDP − glucose.

UDP − glucose act as the substrate of the glycogen synthesis process.

Expert Solution & Answer

Want to see the full answer?

Check out a sample textbook solution

See solution

Students have asked these similar questions

The beta-lactamase hydrolyzes the lactam-ring in penicillin. Describe the mechanism of hydrolysis, insuring to include the involvement of S, D, & K in the reaction sequence. Please help

To map the active site of beta-lactamase, the enzyme was hydrolyzed with trypsin to yield a hexapeptide (P1) with the following amino acids. Glu, Lys, Leu, Phe, Met, and Ser. Treatment of P1 with phenyl isothiocyanate yielded a PTH derivative of phenylalanine and a peptide (P2). Treatment of P1 with cyanogenbromide gave an acidic tetrapeptide (P3) and a dipeptide (P4).Treatment of P2 with 1-fluoro-2,4-dinitrobenzene, followed by complete hydrolysis, yields N-2,4-dinitrophenyl-Glu. P1, P2, and P3 contain the active site serine. Why doesn't D in this hexapeptide not participate in the hydrolysis of the beta-lactam ring even though S, K, and D are involved in the catalyst?

To map the active site of -lactamase, the enzyme was hydrolyzed with trypsin to yield a hexapeptide (P1) with the following amino acids. Glu, Lys, Leu, Phe, Met, and Ser. Treatment of P1 with phenyl isothiocyanate yielded a PTH derivative of phenylalanine and a peptide (P2). Treatment of P1 with cyanogenbromide gave an acidic tetrapeptide (P3) and a dipeptide (P4).Treatment of P2 with 1-fluoro-2,4-dinitrobenzene, followed by complete hydrolysis, yields N-2,4-dinitrophenyl-Glu. P1, P2, and P3 contain the active site serine. Using the experimental results described above derive the primary sequence of the active site hexapeptide. Please help!