Study Guide with Student Solutions Manual and Problems Book for Garrett/Grisham's Biochemistry, 6th
Study Guide with Student Solutions Manual and Problems Book for Garrett/Grisham's Biochemistry, 6th
6th Edition
ISBN: 9798214167343
Author: GARRETT
Publisher: Cengage Learning US
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Chapter 19, Problem 2P
Interpretation Introduction

(a)

Interpretation:

The effect of increase in the concentration of NAD+ on the TCA cycle needs to be explained.

Concept Introduction:

Enzyme catalyzes chemical reaction in cells is called Tricarboxylic acid cycle (TCA).it is also known as Krebs cycle and citric acid cycle. The NAD+ is used in redox reactions.

Interpretation Introduction

(b)

Interpretation:

The effect of increase in the concentration of ATP on the TCA cycle needs to be explained.

Concept Introduction:

Enzyme catalyzes chemical reaction in cells is called Tricarboxylic acid cycle (TCA). It is also known as Krebs cycle and citric acid cycle. The NAD+ is used in the redox reactions.

Interpretation Introduction

(c)

Interpretation:

The effect of increase in the concentration of isocitrate on the TCA cycle needs to be explained.

Concept Introduction:

Enzyme catalyzes chemical reaction in cells is called Tricarboxylic acid cycle (TCA). It is also known as Krebs cycle and citric acid cycle. The NAD+ is used in the redox reactions.

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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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