Enzimas: Estructura, Catálisis e Inhibición

Study Notes

Enzymes: Structure, Catalysis, and Inhibition

Enzymes are biological molecules that catalyze specific chemical reactions in living organisms. They are crucial for maintaining the balance and functionality of biological systems. Enzymes are primarily proteins, though some ribonucleic acid (RNA) molecules can also act as enzymes. These biological catalysts perform the critical task of lowering a reaction's activation energy, which is the amount of energy required for a chemical reaction to start. Enzymes work by binding to reactant molecules, stabilizing the transition state, and facilitating the reaction to occur more readily.

Enzyme Structure and Substrate Specificity

Enzymes are composed of amino acids, and the active site, where the substrate binds, gets its properties from the amino acids it is built out of. The set of amino acids and their positions in 3D space give the active site a specific size, shape, and chemical behavior, allowing it to bind to a particular target, the enzyme's substrate or substrates. Different types of enzymes have varying degrees of specificity, or "pickiness" about which molecules can be used as substrates. Some enzymes accept only one particular substrate, while others can act on a range of target molecules provided they contain the type of bond or chemical group that the enzyme targets.

Catalysis and the Active Site

Enzymes are catalysts that speed up chemical reactions by lowering the activation energy required for the reaction to occur. They do this by binding to reactant molecules and holding them in a specific conformation, making the chemical bond-breaking and bond-forming processes more likely to take place rapidly. Enzymes don't affect the overall free energy change of a reaction, only the energy of the transition state, which is the unstable state that products must pass through to become reactants.

Induced Fit Model and Substrate Binding

The active site of an enzyme is a groove or crevice where the substrate binds to facilitate the catalyzed chemical reaction. The matching between an enzyme's active site and the substrate is not like a key fitting into a lock, but rather a process called the induced fit model, where the enzyme and substrate do not initially have the precise complementary shape/chemistry. Upon binding, the substrate induces the active site to change its shape to better fit the substrate.

Enzyme Inhibition

Enzyme inhibitors are compounds that modify the catalytic properties of the enzyme, slowing down the reaction rate or even stopping it entirely. There are three main types of inhibition: competitive, non-competitive, and uncompetitive.

Competitive inhibition occurs when the inhibitor binds to the active site of an enzyme, preventing the substrate from binding. This results in a reduction in the reaction rate.
Non-competitive inhibition occurs when the inhibitor binds to an allosteric site on the enzyme, affecting the enzyme's activity without directly competing with the substrate. This leads to a decrease in the enzyme's effectiveness in catalyzing the reaction.
Uncompetitive inhibition occurs when the inhibitor binds only to the enzyme-substrate complex, decreasing the catalytic efficiency of the enzyme. This results in a reduction in the reaction rate and the binding affinity of the enzyme for its substrate.

In conclusion, enzymes are essential biological catalysts that accelerate chemical reactions and maintain the balance of living organisms. Their structure and specificity allow them to bind to substrates and lower the activation energy of a reaction, while inhibitors can be used to modulate or regulate their activity. Understanding enzymes and their mechanisms is crucial for various applications, including medicine, biotechnology, and understanding the fundamentals of life.

Description

Aprende sobre la estructura y función de las enzimas, cómo catalizan reacciones químicas y cómo se inhiben. Descubre cómo las enzimas reducen la energía de activación y cómo se unen a los sustratos para facilitar la reacción. También se explora la inhibición competitiva, no competitiva y no competitiva.