Enzymes

• The active site is the part of an enzyme where substrate molecules bind, while other parts of the enzyme do not interact with the substrates.
• Enzymes have specificity for their substrates due to complementary shape between active sites on enzymes and substrates.
• Enzymes are proteins that act as biological catalysts to speed up chemical reactions without being consumed or altered by them.
• When the substrate enters the active site, it undergoes chemical change (catalysis).
• The active site of an enzyme has a specific shape that fits only one type of molecule, called its substrate.
• Enzymes are classified according to the reaction they catalyze.
• Enzyme-substrate complex is formed when the substrate binds to an enzyme.
• Enzyme inhibitors can either decrease or completely stop the activity of enzymes.
• Active sites are usually clefts or pockets that can accommodate only one type of substrate at a time.
• Enzymes increase rate of reaction by providing a pathway for reaction to proceed more easily than normal.
• Enzymes work best under optimal conditions such as pH and temperature.
• Enzymes lower activation energy required for reactions to occur.
• The active site of an enzyme has a complementary shape to its substrate.
• Enzymes have specificity, meaning they catalyze only certain types of chemical reactions.
• Substrates bind to the active site through weak interactions like hydrogen bonds, ionic bonds, van der Waals forces, and hydrophobic interactions.
• Once bound, the substrate is held firmly enough so it cannot escape from the active site until the chemical reaction occurs.
• Enzymes do not change the equilibrium position of a reversible reaction but speed up both forward and reverse reactions equally.
• When the substrate is bound to the active site, the enzyme-substrate complex forms.