Yes, almost all work on a single substrate.
Most enzymes are substrate specific because they have a specific shapes active site in which only a specific substrate can fit.
The enzyme's surface folds are complementary to the substrate's surface folds.
Depends on how much substrate the enzyme can process. Most enzymes can process more than one molecule of substrate without denaturing or becoming unusable. However, in the terms of your question. More substrate is better. Too many enzymes would mean the reaction would be cut short, because they would all react the substrate at once. So for a prolonged, efficient reaction more substrate would be proper.
Human enzymes are most effective within a specific range of pH and temperature that optimizes their activity. This range is usually near the body's physiological conditions to ensure optimal enzyme function. Additionally, enzymes have specific substrate molecules they interact with, which allows for highly efficient catalysis of chemical reactions.
They are type of proteins. They are 3D globular proteins
Most enzymes are substrate specific because they have a specific shapes active site in which only a specific substrate can fit.
The enzyme's surface folds are complementary to the substrate's surface folds.
Depends on how much substrate the enzyme can process. Most enzymes can process more than one molecule of substrate without denaturing or becoming unusable. However, in the terms of your question. More substrate is better. Too many enzymes would mean the reaction would be cut short, because they would all react the substrate at once. So for a prolonged, efficient reaction more substrate would be proper.
Yes, pH level can affect the activity of enzymes. Enzymes have an optimal pH at which they function most efficiently, and deviations from this pH can decrease enzyme activity. Changes in pH can affect the enzyme's structure and alter the interactions between the enzyme and its substrate.
low, as they can exhibit cooperative binding of substrates and activators at low concentrations. At high substrate concentrations, the active site may become saturated, reducing the impact of allosteric regulation.
While the structure of an enzyme can, and often does, change over the course of a reaction, after a reaction has completed, enzymes are returned to their starting state. It is worth noting that certain cofactors (such as ATP or GTP) may also need to be replaced in order for the reaction to procede again.
Some thing then ase. So if the substrate was called B the enzyme would B+ase, Base. Or substrate Z, the enzyme would be Z+ase, Zase. Some examples, amylase, maltase, catalase, sucrase. That is the most common naming, but it is not ALWAYS the case.
Each enzyme has its' own "perfect" temperature. This varies with the enzyme, the substrate and the environment. In most cases, increasing the temperature above the normal will increase the rate up to a point. Lowering the temperature will slow it down.
Human enzymes are most effective within a specific range of pH and temperature that optimizes their activity. This range is usually near the body's physiological conditions to ensure optimal enzyme function. Additionally, enzymes have specific substrate molecules they interact with, which allows for highly efficient catalysis of chemical reactions.
Enzymes break down specific molecules e.g. amalyse enzyme breaks down hydrogen peroxide, the substrate is on the molecule and then the enzyme comes along, the substrate goes in the active site, then it breaks the molecule down
They are type of proteins. They are 3D globular proteins
The induced fit hypothesis proposes that enzymes undergo conformational changes upon binding to a substrate, allowing for optimal binding and catalytic activity. In this model, the enzyme and substrate mold together to form the most complementary fit, aiding in the catalytic process. This hypothesis accounts for the specificity and efficiency of enzyme-substrate interactions.