BIOCHEMISTRY 2 TERM ACCESS
BIOCHEMISTRY 2 TERM ACCESS
9th Edition
ISBN: 9781319402877
Author: BERG
Publisher: MAC HIGHER
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Chapter 17, Problem 21P
Interpretation Introduction

(a)

Interpretation:

The effect of a mutation that increases the kinase activity which is linked with the pyruvate dehydrogenase complex.

Concept introduction:

Pyruvate dehydrogenase enzyme complex is required for the linking of glycolysis and TCA. It helps in the conversion of pyruvate into Acetyl CoA. Acetyl CoA then enters into the series of the citric acid cycle.

Interpretation Introduction

(b)

Interpretation:

The effect of a mutation that reduces the phosphatase activity which is linked with the pyruvate dehydrogenase complex.

Concept introduction:

Pyruvate dehydrogenase enzyme complex is required for the linking of glycolysis and TCA. It converts the pyruvate into Acetyl CoA. Acetyl CoA then enters into the series of the citric acid cycle.

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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!
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