Untitled Quiz

Study Notes

Enzymes are specialized protein molecules that function as biological catalysts in cellular processes.
Each enzyme is highly specific, catalyzing only a particular reaction and interacting with specific substrates.

Enzymes are reusable and not consumed in the reactions they catalyze, allowing for multiple reactions.
They form Enzyme-Substrate (ES) complexes upon interaction with substrates.
A small quantity of enzyme can catalyze a large amount of substrate, demonstrating efficiency.
Enzymes exhibit a high turnover rate, rapidly converting substrates into products.
Activity of enzymes is influenced by environmental factors like temperature and pH.
Many enzymes require cofactors, which can be essential for their catalytic functions.
Enzymatic reactions can be inhibited or slowed down by specific inhibitors.

Coenzymes are organic, non-protein compounds that assist enzymes in catalyzing reactions.
While coenzymes are often referred to as cofactors, they differ chemically from other types of cofactors.
Coenzymes cannot operate independently but can be recycled with enzymes during reactions.

Isozymes, or isoenzymes, are different forms of enzymes that catalyze the same reaction but have variations in their amino acid sequences.
They often exhibit distinct kinetic parameters and regulatory properties, such as differing Michaelis-Menten constants (KM values).

Proenzymes, or zymogens, represent the inactive forms of enzymes that require modifications to become active.
Activation typically involves biochemical changes like hydrolysis that expose the enzyme's active site.

Enzyme regulation involves managing enzymatic reactions through inhibitors or activators, based on specific rules or principles.
Changes in environmental conditions, such as pH, can also influence enzyme activity.

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