Enzymes are proteins that act as catalysts in biochemicalreactions.
Enzymes are dynamic structures that respond to changes in conditions, such as substrate concentration, temperature, pH, and cofactors.
Enzymes have a specific three-dimensional structure that allows them to bind to specific substrates.
The active site is the part of an enzyme where substrates bind to initiate chemical reactions.
Substrate specificity refers to the ability of an enzyme to recognize and interact with only one or a few types of molecules, known as its substrates.
The active site is the region where enzyme-substrate interactions occur.
Active sites can be specific or non-specific depending on their shape and chemical properties.
Substrates bind to the active site through weak intermolecular forces like hydrogen bonds, van der Waals forces, ionic bonds, and hydrophobic interactions.
The active site is the region on an enzyme where the substrate molecule fits perfectly.
Active sites can be modified by other substances called inhibitors or activators.
Specific active sites require precise complementarity between the substrate's shape and the active site's geometry.
Non-specific active sites allow multiple substrates to fit into the same binding pocket.
Catalytic activity involves lowering the activation energy required for a reaction to proceed.
Catalysts are substances that increase the rate of a reaction without being consumed by it.
Enzymes act as catalysts by lowering the activation energy required for a reaction to take place.
Enzymes are biological catalysts that speed up biochemical reactions by lowering activation energy barriers.
Enzymes are proteins that catalyze biochemical reactions without being consumed themselves.