Log out Go to App
Go to App

Learning Materials

Features

Discover

Chapter 23: Q15 P (page 1085)

Explain why the ability of PLP to catalyze an amino acid transformation is greatly reduced if a PLP- requiring enzymatic reaction is carried out at a pH at which the pyridine nitrogen is not protonated.

Short Answer

Expert verified

If the pyridine nitrogen is not protonated on to the positively charged protonated nitrogen of pyridine ring then it would be less attractive to electrons and thereby decreases enzymatic reactions.

Step by step solution

01

Reason behind less ability of PLP

Amino acid reacts with imine formed by PLP and the lysine side chain converts to another imine by transimination reaction. The next step after this reaction is breaking substituents from α- carbon of amino acid. The electrons left behind when bond breaks are delocalized on to the positively charged protonated nitrogen of pyridine ring. If the pyridine nitrogen is not protonated, then it would be less attractive to electrons. Hence, pyridine nitrogen less crowded with electrons.

02

Imine between PLP and amino acid

Here the structure represents an imine linkage in between PLP coenzyme and an amino acid containing hydrocarbon side chain.

Thus, the reason behind the reduction in PLP to catalyze an amino acid transformation is discussed above.

Unlock Step-by-Step Solutions & Ace Your Exams!

  • Full Textbook Solutions

    Get detailed explanations and key concepts

  • Unlimited Al creation

    Al flashcards, explanations, exams and more...

  • Ads-free access

    To over 500 millions flashcards

  • Money-back guarantee

    We refund you if you fail your exam.

Start your free trial

Over 30 million students worldwide already upgrade their learning with Vaia!

One App. One Place for Learning.

All the tools & learning materials you need for study success - in one app.

Get started for free

Most popular questions from this chapter

What is the product of the following reaction?

Question: What is the source of the methyl group in thymidine?

a. What acyl group does pyruvate decarboxylase transfer to a proton?

b. What acyl group does the pyruvate dehydrogenase complex transfer to coenzyme A?

c. What acyl group does transketolase transfer to ribose-5-P?

Question:Five coenzymes are required by -ketoglutarate dehydrogenase, the enzyme in the citric acid cycle that converts -ketoglutarate to succinyl-CoA.

a. Identify the coenzymes.

b.Propose a mechanism for the reaction.

Explain why the hydrogens of the C-8 methyl group are more acidic than those of the C-7 methyl group.
See all solutions

Recommended explanations on Chemistry Textbooks

Making Measurements

Read Explanation

Chemical Analysis

Read Explanation

Chemical Reactions

Read Explanation

Chemistry Branches

Read Explanation

Ionic and Molecular Compounds

Read Explanation

Kinetics

Read Explanation
View all explanations

What do you think about this solution?

We value your feedback to improve our textbook solutions.

Study anywhere. Anytime. Across all devices.

Sign-up for free