(a) Interpretation: The difference between the phosphofructokinase (PFK) activity in P. Furiosus and other animals should be determined. Concept introduction: Phosphofructokinase is an allosteric enzyme which converts fructose-1-phopshate to fructose-1,6-bisphosphate. It acts as a regulatory enzyme in the glycolysis process. High ATP concentration inside the cell inhibits the activity of PFK.

Question

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

Answer 1

Question

Chapter 16, Problem 57P

Interpretation Introduction

(a)

Interpretation:

The difference between the phosphofructokinase (PFK) activity in P. Furiosus and other animals should be determined.

Concept introduction:

Phosphofructokinase is an allosteric enzyme which converts fructose-1-phopshate to fructose-1,6-bisphosphate. It acts as a regulatory enzyme in the glycolysis process. High ATP concentration inside the cell inhibits the activity of PFK.

Interpretation Introduction

(b)

Interpretation:

Effect of ATP and AMP on ADP should be determined.

Concept introduction:

Phosphofructokinase is an allosteric enzyme which converts fructose-1-phopshate to fructose-1,6-bisphosphate. It acts as a regulatory enzyme in the glycolysis process. High ATP concentration inside the cell inhibits the activity of PFK.

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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!