Difference Between Allosteric Enzymes and Non-Allosteric Enzymes

Difference Between Allosteric Enzymes and Non-Allosteric Enzymes: Allosteric Enzymes show unique regulatory sites apart from their active sites, allowing them to adjust their activity in response to particular molecules binding to these sites. The Non-Allosteric enzymes lack these allosteric regulatory sites, operating solely based on substrate binding to their active sites. This fundamental difference in the regulation influences the kinetics and behaviour of these enzymes, shaping their roles in cellular processes.

Difference between Allosteric Enzymes and Non-Allosteric Enzymes

Allosteric Enzymes feature additional regulatory sites, different from active sites, altering enzyme activity by conformational changes in response to binding of allosteric effectors, enabling precise metabolic control. The table below provides the differences between Allosteric Enzymes and Non Allosteric Enzymes.


Allosteric Enzymes

Non-Allosteric Enzymes


Activity is regulated by the binding of specific molecules (allosteric regulators) to regulatory sites other than the active site

Activity is usually regulated by substrate concentration or covalent modification

Active Site

Contains both active sites (where substrates bind) and regulatory sites (where allosteric regulators bind)

Contains only active sites where substrates bind


Exhibits cooperativity, where the binding of one substrate molecule affects the binding of subsequent substrate molecules

Does not exhibit cooperativity

Regulation Type

Often displays sigmoidal kinetics due to cooperative binding

Usually follows Michaelis-Menten kinetics


Phosphofructokinase in glycolysis, ATP citrate lyase in fatty acid synthesis

Hexokinase in glycolysis, Catalase in peroxisomes

Role in Metabolism

Often control key steps in metabolic pathways, allowing for fine-tuned regulation

Participate in various metabolic pathways but usually regulate less critical steps

Sensitivity to Regulation

Sensitive to small changes in allosteric regulator concentration

Less sensitive to changes in substrate or covalent modification

What are Allosteric Enzymes?

Allosteric Enzymes are proteins that possess additional regulatory sites, known as allosteric sites, separate from their active sites where substrates bind. These enzymes undergo conformational changes when specific molecules, called allosteric effectors, bind to these sites. This mechanism enables Allosteric Enzymes to finely regulate metabolic pathways in response to cellular signals, ensuring dynamic metabolic control and homeostasis within the cell.

Key Features of Allosteric Enzymes

  • Allosteric Sites: Allosteric Enzymes possess regulatory sites, called allosteric sites, different from their active sites where substrates bind. These allosteric sites allow for the binding of regulatory molecules, known as allosteric effectors.
  • Conformational Changes: The binding of allosteric effectors to the allosteric sites induces conformational changes in the enzyme structure. 
  • Cooperativity: Allosteric Enzymes often exhibit cooperativity, meaning the binding of one substrate molecule influences the binding of subsequent substrate molecules. This results in sigmoidal kinetics in their substrate-activity curves.
  • Dynamic Regulation: Allosteric Enzymes provide a mechanism for dynamic regulation of metabolic pathways in response to cellular signals and changes in substrate or product concentrations. This allows for rapid adjustments to metabolic demands and maintenance of cellular homeostasis.

What is Non Allosteric Enzymes?

Non-Allosteric Enzymes, also known as simple enzymes, are proteins that lack allosteric regulatory sites different from their active sites. Instead, their catalytic activity is primarily regulated by factors such as substrate concentration, product inhibition, or competitive inhibition by other molecules that directly interact with the active site.

Key Features of Non Allosteric Enzymes

  • Single Active Site: Non-Allosteric Enzymes usually possess only one active site where the substrate binds and the catalytic reaction occurs. This is in contrast to Allosteric Enzymes, which may have multiple allosteric sites that can modulate the enzyme's activity.
  • Regulation by Substrate Concentration: The time of reaction catalyzed by Non-Allosteric Enzymes is mainly dependent on the concentration of substrate molecules available for binding to the active site. As substrate concentration increases, the rate of reaction also increases until it reaches a maximum rate determined by the enzyme's saturation with the substrate.
  • Michaelis-Menten Kinetics: Non-Allosteric Enzymes usually follow Michaelis-Menten kinetics, which describes the relationship between substrate concentration and reaction rate. According to this model, the initial velocity of the reaction (V0) is proportional to the substrate concentration and follows a hyperbolic curve.
  • pH and Temperature Dependence: The activity of Non-Allosteric Enzymes is influenced by factors such as pH and temperature. Each enzyme has an optimal pH and temperature at which it exhibits maximum activity. Deviation from these optimal conditions can lead to decreased enzyme activity.

Similarities between Allosteric Enzymes and Non-Allosteric Enzymes

  • Catalysis of Biochemical Reactions: Both Allosteric Enzymes and Non-Allosteric Enzymes catalyze specific biochemical reactions. They facilitate the conversion of substrates into products by lowering the activation energy required for the reaction to occur.
  • Specificity: Both types of enzymes exhibit substrate specificity, meaning they recognize and bind to specific substrates that fit into their active sites. This specificity ensures that enzymes catalyze only particular reactions within the complex network of cellular metabolism.
  • Enzyme-Substrate Complex Formation: Both Allosteric and Non-Allosteric Enzymes form enzyme-substrate complexes during the catalytic process. This occurs when the substrate molecules bind to the active site of the enzyme, forming a temporary intermediate complex that facilitates the chemical reaction.

In summary, Allosteric Enzymes are distinguished by their ability to undergo conformational changes in response to the binding of regulatory molecules at allosteric sites, while Non-Allosteric Enzymes are primarily regulated through competitive or non-competitive inhibition mechanisms at their active sites.

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What are Allosteric Enzymes?

Allosteric Enzymes are enzymes that have an additional site, known as the allosteric site, different from the active site. This allosteric site can bind regulatory molecules called allosteric modulators, which can alter the enzyme's activity.

What are Non-Allosteric Enzymes?

Non-Allosteric Enzymes are enzymes that do not possess an allosteric site. Their activity is solely regulated by the substrate binding to the active site.

How do Allosteric Enzymes differ from Non-Allosteric Enzymes in terms of regulation?

Allosteric Enzymes can be regulated by binding specific molecules to the allosteric site, which can either activate or inhibit the enzyme's activity. In contrast, Non-Allosteric Enzymes are usually regulated through mechanisms such as competitive inhibition or covalent modification at the active site.

What is the significance of allosteric regulation in cellular processes?

Allosteric regulation allows for rapid and reversible control of enzyme activity in response to changes in cellular conditions. This enables fine-tuning of metabolic pathways and coordination of cellular processes.

Can Allosteric Enzymes switch between active and inactive states?

Yes, Allosteric Enzymes can switch between active and inactive states based on the binding of allosteric modulators. The binding of activators stabilizes the active conformation, while the binding of inhibitors stabilizes the inactive conformation.