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 feature of an enzyme that determines its chemical process it aids is it's shape. This can be compared to a lock and key. Where an enzyme, as the key, must have a certain structure or multi-dimensional shape that matches a specific section of the substrate, the compound or substance that undergoes the change.
In biology the lock and key method states that an enzyme and it's substrate are complementary and only the correct substrate can bind with the enzyme, this is due to the folding in the protein structure. However this theory is outdated and the inducted fit method is a much better representation.
The model you are referring to is the lock-and-key model of enzyme-substrate interaction. This model proposes that enzymes have specific active sites that perfectly fit the substrate, similar to how a lock fits a key. This precise fit allows for the formation of the enzyme-substrate complex and subsequent catalysis of the reaction.
Today
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.
the answer is lock and key model .
The Key is the substrate while the key is the enzyme. Just finished learning this :)
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.
Active site of an enzyme is fixed for particular substrate, or you can understand it better via lock-key theory, in which substrate acts as a lock and active side of the enzyme as a key, and you know well that each lock has a specific key to make it unlock. So if active site of an enzyme is altered due to any reason, it can not be fixed into the its particular substrate, and functioning of an enzyme obliviously requires a substrate.
An enzyme has only one substrate that it works with so it has only one function. This is called a lock and key mechanism. Other things can affect the enzyme such as temperature, pH level and levels of either the substrate or the products. High temperature can denature the enzyme (they are proteins). They can not fit the lock (substrate).
An enzyme has only one substrate that it works with so it has only one function. This is called a lock and key mechanism. Other things can affect the enzyme such as temperature, pH level and levels of either the substrate or the products. High temperature can denature the enzyme (they are proteins). They can not fit the lock (substrate).
The lock and key hypothesis explains enzyme functioning. It suggests that enzymes and substrates fit together like a lock and key, with specific enzyme-active sites binding to specific substrates to catalyze reactions.