BIOCHEMISTRY-ACHIEVE (1 TERM)
BIOCHEMISTRY-ACHIEVE (1 TERM)
9th Edition
ISBN: 9781319402853
Author: BERG
Publisher: MAC HIGHER
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Chapter 8, Problem 19P
Interpretation Introduction

(a)

Interpretation:

Whether the given reaction proceeds as written or not is to be stated. The final concentrations of glucose6phosphate and glucose1phosphate is to be stated.

Concept introduction:

When any reaction is at equilibrium then a constant expresses a relationship between the reactant side and the product side. This constant is known as equilibrium constant. It is denoted by Keq. The equilibrium constant is independent of the initial amount of the reactant and product.

Interpretation Introduction

(b)

Interpretation:

The cellular condition under which glucose-1-phosphate is produced at a high rate is to be stated.

Concept introduction:

When any reaction is at equilibrium then a constant expresses a relationship between the reactant side and the product side. This constant is known as equilibrium constant. It is denoted by Keq. The equilibrium constant is independent of the initial amount of the reactant and product.

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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!
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