Induced fit: is a more recent theory which suggests that the substrate attaches to the enzyme in a relatively accurate fit, then the enzyme moulds around it, then continues the chemically complex reaction.
Lock and Key Mechanism: As obvious as the name states, the lock and key model is simply the substrate fitting acutely into the enzyme with no adjustments required to the enzyme.
K.G. ;)
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Induced fit refers to the concept that enzymes can change their shape slightly to better accommodate the substrate, leading to a tighter binding and improved specificity. The structural adjustments that occur during induced fit can create a better alignment between the enzyme's active site and the substrate, increasing the likelihood of a successful reaction. This process helps ensure that the enzyme specifically recognizes and binds to its intended substrate, enhancing its catalytic efficiency.
substrate goes into activity site
gets lulzed
and come out with 2 serperate molecules.
It moves the reactive portion of the enzyme closer to the substrate. The enzyme's active site changes shape to fit the correct substrate but not other molecules.
The lock and key model means that the substrate must perfectly fit the enzyme, and the enzyme does not change. The induced fit model is different as when the substrate fits together with the enzyme, the enzyme itself will change to either join substrates together or break a substrate down.
The lock and key theory and the induced fit theory are two theories that explain enzyme specificity. The lock and key theory proposes that the enzyme's active site is already in the correct shape to bind the substrate, like a key fitting into a lock. The induced fit theory suggests that the active site of the enzyme can change its shape slightly to accommodate the substrate, similar to a glove molding around a hand.
This situation is known as induced fit. When a substrate binds to an enzyme, the enzyme's shape can change to better accommodate the substrate, creating a more optimal environment for the catalytic reaction to occur. This induced fit mechanism helps enzymes to be more specific and efficient in their function.
Enzyme-substrate specificity refers to the ability of an enzyme to selectively bind to and catalyze a specific substrate or group of chemically related substrates. This specificity is determined by the enzyme's active site, which is complementary in shape and charge to the substrate. The specificity allows enzymes to perform their biological functions efficiently and without interfering with other cellular processes.
The lock and key method is a concept in enzyme-substrate interaction where the enzyme's active site is specific in shape, like a lock, to fit the substrate, like a key. This specificity allows for efficient catalysis of reactions as only the correct substrate can bind to the enzyme's active site. Any change in the shape of the enzyme or substrate can disrupt this interaction and affect the enzyme's function.