Concentration of the enzyme or it's substrate and the temperature.
pH and temperature.
AnswerWhat does inhibitor do to enzyme activity?They prevent the reactions from happening. Non-competative inhibitors alter the shape of the active site so that the substrate no longer fits, and competative inhibitors block the active site.
When investigating the rate of an enzyme-controlled reaction, two measurable factors are the amount of product formed over time and the decrease in substrate concentration over time. By monitoring the rate at which product accumulates or substrate is consumed, researchers can determine the enzyme's activity and efficiency under varying conditions. Additionally, factors such as temperature and pH can be varied and measured to assess their impact on the reaction rate.
Yes, both salinity and inhibitors can affect enzyme activity. There are two types of inhibitors, non-competitive and competitive inhibitors that will either bind to the allosteric or active site respectively.
Minerology of the area
temperature and pH
Temperature can affect enzyme activity because enzymes work best within specific temperature ranges. At low temperatures, enzyme activity decreases as the molecules move more slowly, decreasing the likelihood of enzyme-substrate collisions. At high temperatures, enzyme activity can be disrupted because the enzyme structure can become denatured, leading to a loss of function. Optimal temperature for enzyme activity varies depending on the specific enzyme.
Two features of a denatured enzyme are loss of its three-dimensional structure and subsequent loss of its biological activity. Denaturation can be caused by factors such as high temperature or extreme pH levels, leading to irreversible changes in the enzyme's shape and function.
Two main factors that affect the absorption of a mineral are the presence of other nutrients or substances that can enhance or inhibit absorption, and the health and integrity of the digestive system, including factors such as pH levels, enzyme activity, and gut health.
Temperature: Enzyme activity can be controlled by adjusting the temperature, as most enzymes have an optimal temperature at which they function best. pH: Enzyme activity is also influenced by the pH of the environment, and maintaining an appropriate pH level can help regulate enzyme function. Inhibitors: Enzyme activity can be inhibited by specific molecules that bind to the enzyme and prevent it from carrying out its catalytic function. This can be used as a way to control enzyme activity in biological systems.
temperature and pH
pH and temperature.
AnswerWhat does inhibitor do to enzyme activity?They prevent the reactions from happening. Non-competative inhibitors alter the shape of the active site so that the substrate no longer fits, and competative inhibitors block the active site.
Extreme temperatures and pH levels outside of the enzyme's optimal range are two factors that could cause enzyme denaturation. Additionally, exposure to certain chemicals or heavy metals can also lead to enzyme denaturation.
- with enzymes the rate of reaction is higher- an important characteristic of an enzyme is the specifity
Yes, both salinity and inhibitors can affect enzyme activity. There are two types of inhibitors, non-competitive and competitive inhibitors that will either bind to the allosteric or active site respectively.
Temperature, pH, solute concentration, and salt content just to name a few. Temperature and Ph affect the function of enzymes because our body has a temperature of around 37 degrees and the conditions in our stomach are acidic. So9f or the enzyme to work properly then the working condidtions have to be at least 37 degrees and they need to acidic otherwise the enzyme won't work properly.