BIOCHEMISTRY (LOOSELEAF)-W/ACCESS
BIOCHEMISTRY (LOOSELEAF)-W/ACCESS
9th Edition
ISBN: 9781319425784
Author: BERG
Publisher: Macmillan Higher Education
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Chapter 8, Problem 31P
Interpretation Introduction

Interpretation:

The four key types of irreversible inhibitors that are used for the study of enzyme function are to be stated.

Concept introduction:

A molecule which gets attached to an enzyme to decrease the activity of the same enzyme is known as enzyme inhibitor. The two types of enzyme inhibitor are reversible inhibitor and irreversible inhibitor.

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In full details. Define 'activation energy' of an enzyme catalysed single substrate reaction and mention the effects of an enzyme on this energy.
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I. Active site analysis. Below is a diagram of a putative active site for Monoamine oxidase. As we learned, the purpose of tertiary structure is to form a scaffold so you can orient just a few amino acids in the right orientation to promote binding and/or catalysis. The position where this occurs is the active site. The amino acid architecture of an active site is designed to bind substrates. Amino acid side chains are capable of hydrogen bonding, ionic and hydrophobic interactions. Fill in each amino acid that you think is suitable for interacting with the part of the substrate it is closest to. Assume the pH will be at 7.0 a.a.#1 a.a.#2 a.a.#6 HO Lond NH₂ НО a.a.#5 OH a.a.#3 a.a.#4
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