Lock and key is an analogy of enzyme catalysis in a cellular reaction. The lock and key are compared directly to the substrate and enzyme, because of the high specificity of their physical shape.
Enzymes participate in the reaction they catalyze.
The reactant molecule (substrate) binds to the enzyme molecule at a particular location called the active site. (this is compared to the lock with keyhole)
The highly specific nature of an enzyme is due to very precisely defined arrangement of atoms in the active site(again, this is the lock in the analogy). The substrate molecule must have a matching shape (here is the key) that will fit into the active site.
The bond breaking and bond forming processes that transform the substrate into products occur while the substrate is bound to the active site of enzyme.
In other words its something like a jigsaw puzzle where the substrate fits into the enzyme. The reaction occurs and the substrate then leaves the enzyme as products.
( Not my work. Found it on Yahoo Answers.....Do not give me credit...Thought I should do this to help people out =] )
Edited answer for readability and clarity - thanks!
An enzyme and its substrate work like a lock and key. The enzyme (lock) has a specific shape that perfectly fits the substrate (key), allowing them to bind together. This precise interaction facilitates the chemical reaction, much like a key unlocking a door. If the key doesn't fit, the lock won't open, illustrating the specificity of enzyme-substrate interactions.
ALL enzymes use the lock and key model!
The lock-and-key model provides a useful illustration of how an enzyme interacts with a substrate molecule. In this model, the enzyme's active site is complementary in shape to the substrate, similar to a key fitting into a lock. This specificity allows for efficient catalysis of the reaction.
In a model of enzyme action, the enzyme can attach only to a substrate (reactant) with a specific shape. The enzyme then changes and reduces the activation energy of the reaction so reactants can become products. The enzyme is unchanged and is available to be used again.
The modification of the lock and key model that suggests the active site of an enzyme is known as the "induced fit model." This model proposes that while the active site of an enzyme has a specific shape (like a lock), it can undergo conformational changes upon substrate binding (like a key adjusting to fit the lock). This flexibility allows for a more precise interaction between the enzyme and its substrate, enhancing catalytic efficiency. The induced fit model highlights the dynamic nature of enzyme-substrate interactions compared to the rigidity of the original lock and key model.
the answer is lock and key model .
Easily Explained thusly: When the key is in the lock the Enzyme has one Structure, and when the key is not in the lock the Enzyme has another Structure. Note that the presence of a key may either activate or deactivate an Enzyme, depending upon the conditions.
The Key is the substrate while the key is the enzyme. Just finished learning this :)
A substrate and its enzyme are like a lock and key because they have specific shapes that fit together perfectly. Just like a key must fit exactly into a lock to open it, the substrate must fit into the enzyme's active site for a reaction to occur. This specific interaction ensures that only the correct substrate is acted upon by the enzyme.
ALL enzymes use the lock and key model!
It is called a lock and key mechanism.Actually is more than one word. It is called a lock and key mechanism. Only one key can unlock one lock.
The lock-and-key model provides a useful illustration of how an enzyme interacts with a substrate molecule. In this model, the enzyme's active site is complementary in shape to the substrate, similar to a key fitting into a lock. This specificity allows for efficient catalysis of the reaction.
enzyme specificity
Lock and Key hypothesis
lock and key theory
In a model of enzyme action, the enzyme can attach only to a substrate (reactant) with a specific shape. The enzyme then changes and reduces the activation energy of the reaction so reactants can become products. The enzyme is unchanged and is available to be used again.
The modification of the lock and key model that suggests the active site of an enzyme is known as the "induced fit model." This model proposes that while the active site of an enzyme has a specific shape (like a lock), it can undergo conformational changes upon substrate binding (like a key adjusting to fit the lock). This flexibility allows for a more precise interaction between the enzyme and its substrate, enhancing catalytic efficiency. The induced fit model highlights the dynamic nature of enzyme-substrate interactions compared to the rigidity of the original lock and key model.