FUNDAMENTALS OF BIOCHEM.-NEXTGEN ACCESS
FUNDAMENTALS OF BIOCHEM.-NEXTGEN ACCESS
5th Edition
ISBN: 9781119661450
Author: Voet
Publisher: WILEY
Question
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Chapter 12, Problem 1E

(a)

Summary Introduction

To calculate: The rate constant for the nonenzymatic elementary reaction AàB.

Concept introduction: The rate constant is the proportionality constant in an elementary reaction. The rate constant helps to quantify the rate of the reaction.

(a)

Expert Solution
Check Mark

Explanation of Solution

Calculation:

Given:

The nonenzymatic elementary reaction is AàB, where A is the reactant and B is the product.

The concentration of A = 20mM

The reaction velocity = 5µm of B/minute

The velocity of an instantaneous reaction is v=k[A]

where,

 v is the reaction velocity

 k is the reaction constant

 [A] is the concentration of A

The given values are substituted in the following rearranged equation for velocity of an instantaneous reaction,

k=v[A]=5μMmin-120mM=5×10-3mMmin-120mM=2.5×10-4min-1

   FUNDAMENTALS OF BIOCHEM.-NEXTGEN ACCESS, Chapter 12, Problem 1E

Conclusion

Conclusion: The rate constant for the nonenzymatic elementary reaction AàB is

2.5×10-4 min-1.

(b)

Summary Introduction

To determine: The molecularity of the given nonenzymatic elementary reaction AàB

Concept introduction: Molecularity of elementary reaction is defined as the total number of molecules or ions in the reaction that participate in the rate determining step.

(b)

Expert Solution
Check Mark

Explanation of Solution

Explanation: In the given reaction, there is only one rate determining step. Here, only one molecule of A is participating in the rate determining step. Therefore, molecularity is one.

Conclusion

Conclusion: The molecularity of the given nonenzymatic elementary reaction AàB is 1.

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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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FUNDAMENTALS OF BIOCHEM.-NEXTGEN ACCESS

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