The concerted model and the sequential model are models used to explain the allosteric changes of conformation of an enzyme from the T structure to the R. ![]() This is often visualized in figures showing the enzyme and the substrate coming together, resembling a lock needing a specific key. This model opposes to the lock and key model that explains the formation of the E-S complex as a result of the binding of complementary geometrical rigid structures, as a lock and a key. Enzymes are highly specific catalysts, and their specificity is determined by the unique compatibility between the enzyme's active site and the structure of the substrate. These models are crucial for understanding the way enzymes function. What is Induced Fit Model Supporting findings that led to widely accepted induced fit model. ![]() In contrast, the induced fit model describes enzymes as flexible, where the active site can change shape to better accommodate and catalyze the reaction with the substrate only after the substrate has bound to the enzyme. A) the substrate change its shape slightly. MCQ 1: According to lock and key model the substrate acts as a. The lock-and-key model suggests that enzymes are conformationally rigid, only bonding with substrates that perfectly fit their active site. Induced Fit model MCQs: Questions and Answers PDF Download. The two primary models that describe enzyme specificity and catalytic action are the lock-and-key model and the induced fit model. ![]() The lock-and-key model describes enzyme specificity with a rigid active site that fits only certain substrates, while the induced fit model proposes that enzymes have flexible active sites that adapt to the substrates upon binding.
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