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Several factors affect the rate at which enzymatic reactions proceed - temperature, pH, enzyme concentration, substrate concentration, and the presence of any inhibitors or activator

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Alvah Stokes

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3y ago

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Related Questions

What does the enzyme activity curve reveal about the relationship between enzyme concentration and reaction rate?

The enzyme activity curve shows that as enzyme concentration increases, the reaction rate also increases. However, there is a point where adding more enzyme does not further increase the reaction rate, indicating that there is a limit to the effect of enzyme concentration on reaction rate.


What do you call the rate of an enzyme catalyzed reaction?

The rate of an enzyme-catalyzed reaction is often referred to as the enzyme's catalytic activity or turnover rate. It is a measure of how quickly the enzyme can convert substrate molecules into products.


What is the enzyam activity?

The enzyme activity depends on the conditions of the reaction and the enzmye used. The term enzyme activity refers to the rate at which substrate is converted into product and can be measured in many different ways.


Which variable is the student's experiment described in the Prelab Activity designed to test?

The student's experiment in the Prelab Activity is designed to test the effect of changing the concentration of hydrogen peroxide on the rate of enzyme activity in the enzyme catalase. This involves manipulating the independent variable (concentration of hydrogen peroxide) to observe its impact on the dependent variable (rate of enzyme activity).


How do you calculate specific activity of salivary amylase?

Specific activity of salivary amylase can be calculated by dividing the total enzyme activity (in units) by the total protein concentration (in mg). The formula is: Specific activity = Total enzyme activity (units) / Total protein concentration (mg). This calculation gives a measure of the enzyme's activity per unit of protein.


What is the Effect of dilution on enzyme activity?

At a high ion concentration, the ion interfere with the bonds between the side groups of the amino acids making up the enzyme (which is a protein). This causes the enzyme to lose its shape, called denaturation. If the enzyme loses its shape, it can no longer accept and react substrate, so the rate of enzyme activity decreases.


What is a substrate effector?

A substrate effector is a molecule that can bind to an enzyme's substrate and either enhance or inhibit the enzyme's activity. This can influence the rate of the enzyme-catalyzed reaction.


What is the relationship between substrate concentration and enzyme activity?

At low substrate concentrations, the rate of enzyme activity is proportional to substrate concentration. The rate eventually reaches a maximum at high substrate concentrations as the active sites become saturated.


What accurately describes how temperature affects enzyme activity?

Temperature can affect enzyme activity by either increasing or decreasing the rate of the reaction. Low temperatures can slow down enzyme activity, while high temperatures can denature enzymes, leading to a loss of function. Each enzyme has an optimal temperature at which it functions most efficiently.


What is a question that can be answered using scientific method?

"What effect does temperature have on the rate of enzyme activity?"


How do you calculate Vmax and Km for enzyme activity data?

To calculate Vmax and Km for enzyme activity data, you can use the Michaelis-Menten equation. Vmax is the maximum reaction rate of the enzyme, and Km is the substrate concentration at which the reaction rate is half of Vmax. By plotting a Lineweaver-Burk plot or a double reciprocal plot of the enzyme activity data, you can determine Vmax and Km by analyzing the slope and intercept of the line.


Why does increase enzymes concentration promote enzyme activity?

Increasing enzyme concentration increases the number of collisions between the enzyme molecules and the substrate molecules. This increases the number of successful collisions and the number of enzyme-substrate complexes. Therefore the reaction rate is increased as well and enzyme activity is promoted.