Biochemistry
Biochemistry
8th Edition
ISBN: 9781464126109
Author: Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr., Lubert Stryer
Publisher: W. H. Freeman
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Chapter 20, Problem 24P
Interpretation Introduction

(a)

Interpretation:

The stoichiometry of the synthesis of ribose5phosphate from glucose6phosphate without the generation of NADPH is to be stated.

Concept introduction:

The stoichiometry of a chemical species involved in a chemical reaction represents the number of chemical species involved in the chemical reaction. The stoichiometry of a chemical species helps in calculating the expected mass of reactant and product. The stoichiometry of a chemical species is also represented by a number of moles.

Interpretation Introduction

(b)

Interpretation:

The stoichiometry of the synthesis of NADPH from glucose6phosphate without the generation of pentose sugar is to be stated.

Concept introduction:

The stoichiometry of a chemical species involved in a chemical reaction represents the number of chemical species involved in the chemical reaction. The stoichiometry of a chemical species helps in calculating the expected mass of reactant and product. The stoichiometry of a chemical species is also represented by a number of moles.

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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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