Suggests the enzyme's active site changes shape slightly as the substrate binds, improving the fit.
Koshland proposed in 1958 that the enzyme and substrate adjust to each other, improving binding and positioning catalytic groups. It replaced the rigid lock-and-key model of Emil Fischer.
Induced fit helps explain why enzymes can accept related substrates and why binding at one site can affect another.
Suggests the enzyme's active site changes shape slightly as the substrate binds, improving the fit.
Induced Fit Model 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 Active Site, Allosteric Regulation, Noncompetitive Inhibition.
Hexokinase closes around glucose upon binding.
Work through the Beginner topics in Biomolecules & Biochemistry first, such as Water Properties, Carbon Chemistry, Carbohydrates, then return to Induced Fit Model. Intermediate topics assume the Beginner vocabulary.
The closest topics to Induced Fit Model are Active Site, Allosteric Regulation, Noncompetitive Inhibition, Factors Affecting Enzymes. 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 Induced Fit Model. To practise the whole of Biomolecules & Biochemistry, use the Biomolecules & Biochemistry quiz.
Induced Fit Model: Suggests the enzyme's active site changes shape slightly as the substrate binds, improving the fit. Active Site: The specific pocket on an enzyme where the substrate binds and the reaction takes place. 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 Active Site and explain the difference aloud. Finally, take the Biomolecules & Biochemistry quiz and come back to this page for any question you miss.
The specific pocket on an enzyme where the substrate binds and the reaction takes place.
⚗️ Biomolecules & BiochemistryBinding of a molecule at a site other than the active site changes enzyme shape and activity.
⚗️ Biomolecules & BiochemistryAn inhibitor binds elsewhere on the enzyme, lowering Vmax without changing Km.
⚗️ Biomolecules & BiochemistryTemperature, pH, substrate and enzyme concentration, and inhibitors all alter the rate of enzyme-catalysed reactions.
⚗️ Biomolecules & Biochemistry