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Parts of the enzyme molecule that interact with a substrate are called?
active sites
What are the deep folds in an enzyme called?
The deep folds in an enzyme are called active sites. These are specific regions where substrate molecules bind and chemical reactions take place. Active sites are crucial for enzyme function and specificity.
Why am enzyme can be used to catalyst a large quantity of substrate?
Many times enzymes have multiple active sites that allow for many simultaneous reactions. For example, it's possible to have a fourth of the number of enzymes as substrate molecules, but the enzyme may have four active sites, resulting in one active site per substrate molecule.
What would happen if a reactant molecule with a different shape to the enzyme came into contact with the enzymes active site?
If a reactant molecule with a different shape than the enzyme comes into contact with the enzyme's active site, it is unlikely to bind effectively. Enzymes have specific active sites that accommodate only particular substrates, a concept known as the "lock and key" model. If the shape does not fit, the molecule will not trigger the catalytic activity of the enzyme, and no reaction will occur. This specificity ensures that enzymes catalyze only the intended biochemical reactions.
Why histidine is often found at the active-site of enzyme?
Histidine can act as a versatile amino acid in enzyme active sites because of its ability to donate and accept protons over a wide pH range. This allows histidine to participate in various catalytic mechanisms, making it a common residue in enzyme active sites. Additionally, the imidazole side chain of histidine can form hydrogen bonds and coordinate with metal ions, further enhancing its role in enzyme catalysis.
Parts of the enzyme molecule that interact with a substrate are called?
active sites
What are the deep folds in an enzyme called?
The deep folds in an enzyme are called active sites. These are specific regions where substrate molecules bind and chemical reactions take place. Active sites are crucial for enzyme function and specificity.
Why am enzyme can be used to catalyst a large quantity of substrate?
Many times enzymes have multiple active sites that allow for many simultaneous reactions. For example, it's possible to have a fourth of the number of enzymes as substrate molecules, but the enzyme may have four active sites, resulting in one active site per substrate molecule.
What would happen if a reactant molecule with a different shape to the enzyme came into contact with the enzymes active site?
If a reactant molecule with a different shape than the enzyme comes into contact with the enzyme's active site, it is unlikely to bind effectively. Enzymes have specific active sites that accommodate only particular substrates, a concept known as the "lock and key" model. If the shape does not fit, the molecule will not trigger the catalytic activity of the enzyme, and no reaction will occur. This specificity ensures that enzymes catalyze only the intended biochemical reactions.
Molecule that binds to an enzyme?
A molecule that binds to an enzyme is usually referred to as a substrate. Substrates are the molecules on which enzymes act to catalyze a biochemical reaction. Upon binding to the enzyme's active site, substrates undergo a chemical transformation to form products.
Why must a molecule have a specific shape if it is to be a substrate of an enzyme?
Active sites of enzymes (where the substrates fit in) are substrate specific, and are complementary to the shape of the molecule (substrate). In this way, enzymes can only act on a specific substrate, since that is the only shape that it will accommodate in the active site.
Why histidine is often found at the active-site of enzyme?
Histidine can act as a versatile amino acid in enzyme active sites because of its ability to donate and accept protons over a wide pH range. This allows histidine to participate in various catalytic mechanisms, making it a common residue in enzyme active sites. Additionally, the imidazole side chain of histidine can form hydrogen bonds and coordinate with metal ions, further enhancing its role in enzyme catalysis.
What will happen if a reactant molecule with a reatant molecule with a different shape to the enzyme came into contact with the enzymes active site?
If a reactant molecule with a different shape than the enzyme comes into contact with the enzyme's active site, it is unlikely to bind effectively. Enzymes are highly specific, and their active sites are tailored to fit specific substrates, much like a key fits a lock. If the shape does not match, the molecule will not form the necessary interactions to catalyze a reaction, resulting in no enzymatic activity. This specificity is crucial for proper metabolic function and regulation within biological systems.
Why would a factor that changes the shape of an enzyme prevent it from functioning?
Enzymes are biologically active molecules with specific "active sites", a good analogy is a key and its characteristic notches. If the factor modifies the enzyme's shape then the locations of the enzyme's "active sites" (notches, so to speak) may also be changed, or the sites may be deleteriously affected. Thus the functionality of the enzyme is impaired.
Give 2 explanations for the fact that only certain substrate molecules will fit into this part of the enzyme molecule?
A substrate molecule will only fit into the active site if it is a complimentary shape. Also the amino acids that make up an enzyme have positively and negatively charged chemical groups so in orderr for a substrate to fit its active site any electrical charges on the substrate molecule must not be repelled by like charges on the enzyme so the charged groups on the enzyme molecule and substrate molecule must attract one another
What is an enzyme considered because of its ability to recognize the shape of a particular molecule?
An enzyme is considered a substrate-specific catalyst because it is able to recognize and bind to a specific substrate molecule due to the complementary shape of their active sites. This specificity allows enzymes to efficiently catalyze chemical reactions by facilitating the formation of enzyme-substrate complexes.
How does an enzyme's active sites relate to its substrate?
Their Shapes Fit Snugly Together.
