Allosteric Enzyme

Presentation on Topic: Allosteric Enzyme

M.Sc. Microbiology – Semester 1

Subject: Bioenzymes

Submitted to: Microbiology Department

Submitted by: Sakshi Jha

Introduction

Properties of Allosteric Enzymes

Kinetic Properties

Allosteric Effectors

Types of Allosteric Regulation

Definition of allosteric enzymes

General role in metabolism

Importance in regulation of biochemical pathways

Multi-subunit structure

Presence of active site & regulatory site

Conformational changes upon effector binding

Exhibit cooperative binding

Show sigmoidal (S-shaped) kinetics instead of hyperbolic curve

Positive & negative cooperativity

Role of substrate concentration

Activators: enhance enzyme activity

Inhibitors: reduce enzyme activity

Bind at regulatory (allosteric) sites

Positive Regulation (Activation)

Negative Regulation (Inhibition)

Homotropic effectors (substrate itself acts as effector)

Heterotropic effectors (different molecules act as effector)

Feedback inhibition in metabolic pathways

Example: ATCase inhibited by CTP

Importance in maintaining homeostasis

Drug design and therapeutic targets

Regulation of metabolic diseases

Industrial enzyme technology

Allosteric enzymes act as key regulatory proteins

Provide control over metabolic flux

Crucial in medical & industrial applications

Reference from local MSc book