Karteikarten: Enzyme Function and Regulation — 20 Karten

Enzyme modes of action

Lower activation energy via substrate binding.

Enzyme-substrate complex

Intermediate formed during catalysis.

Lock-and-key model

Active site and substrate are complementary.

Induced fit model

Enzyme changes shape upon substrate binding.

Factors influencing activity

Substrate, temperature, pH, inhibitors.

Substrate saturation

All active sites occupied; max rate.

Optimal temperature

Temperature at which enzyme activity peaks.

Enzyme concentration effect

Increases reaction rate until saturation.

Enzyme inhibition types

Reversible and irreversible.

Competitive inhibitors

Bind active site, resemble substrate.

Non-competitive inhibitors

Bind allosteric site, change shape.

Enzyme cofactors

Non-protein helpers for activity.

Coenzymes

Organic cofactors derived from vitamins.

Metal ion cofactors

Inorganic helpers like zinc, iron.

Effects of pH

Optimal pH maintains enzyme shape.

Denaturation

Loss of enzyme structure and activity.

Activation energy

Energy barrier lowered by enzymes.

Transition state

High-energy intermediate in reactions.

Enzyme properties

Reusable, specific, sensitive to environment.

Metabolic pathways

Series of interconnected reactions.