Temperature, pH, substrate and enzyme concentration, and inhibitors all alter the rate of enzyme-catalysed reactions.
Rate rises with temperature to an optimum then drops sharply when denaturation begins; each enzyme has an optimum pH (pepsin about 2, trypsin about 8). Increasing substrate raises rate until enzyme saturation (Vmax). More enzyme increases rate if substrate is not limiting.
Cofactors, inhibitors and product accumulation can also change rate.
Temperature, pH, substrate and enzyme concentration, and inhibitors all alter the rate of enzyme-catalysed reactions.
Factors Affecting Enzymes is one of the 51 topics in Biomolecules & Biochemistry. It is rated Intermediate, so it suits learners who already know the core vocabulary. Related topics in this area include Michaelis-Menten Kinetics, Induced Fit Model, Cofactors and Coenzymes.
Taq polymerase from hot-spring bacteria works at around 72 degrees Celsius.
Work through the Beginner topics in Biomolecules & Biochemistry first, such as Water Properties, Carbon Chemistry, Carbohydrates, then return to Factors Affecting Enzymes. Intermediate topics assume the Beginner vocabulary.
The closest topics to Factors Affecting Enzymes are Michaelis-Menten Kinetics, Induced Fit Model, Cofactors and Coenzymes, pH and Buffers. Comparing them side by side is a good way to see how the ideas connect.
Read the summary and the in-depth section, then use the quick check on the interactive lesson for Factors Affecting Enzymes. To practise the whole of Biomolecules & Biochemistry, use the Biomolecules & Biochemistry quiz.
Factors Affecting Enzymes: Temperature, pH, substrate and enzyme concentration, and inhibitors all alter the rate of enzyme-catalysed reactions. Michaelis-Menten Kinetics: Models reaction velocity as Vmax times substrate over Km plus substrate, describing enzyme saturation. Read both side by side and note what each one explains.
First, read the summary and write the definition in your own words. Second, read the in-depth section and note any example. Third, compare it with Michaelis-Menten Kinetics and explain the difference aloud. Finally, take the Biomolecules & Biochemistry quiz and come back to this page for any question you miss.
Models reaction velocity as Vmax times substrate over Km plus substrate, describing enzyme saturation.
⚗️ Biomolecules & BiochemistrySuggests the enzyme's active site changes shape slightly as the substrate binds, improving the fit.
⚗️ Biomolecules & BiochemistryNon-protein helpers such as metal ions or vitamin-derived molecules that many enzymes require to function.
⚗️ Biomolecules & BiochemistryThe pH scale measures hydrogen ion concentration; buffers resist pH change to keep conditions stable in cells.
⚗️ Biomolecules & Biochemistry