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When enzyme activity is graphed versus the following which graph is a straight line?
When enzyme activity is graphed against substrate concentration, the resulting graph typically shows a hyperbolic curve due to the saturation of the enzyme. However, if enzyme activity is plotted against the reciprocal of substrate concentration (1/[S]), the graph can produce a straight line, known as a Lineweaver-Burk plot. This linear relationship helps determine kinetic parameters such as the maximum velocity (Vmax) and the Michaelis constant (Km) of the enzyme.
What else can I help you with?
How would a graph show you that the enzyme was being denatured?
A graph illustrating enzyme activity over time or temperature would indicate denaturation by showing a significant decline in activity after reaching a certain threshold. For example, if the x-axis represents temperature and the y-axis represents enzyme activity, a sharp decrease in activity beyond the enzyme's optimal temperature suggests denaturation. This drop occurs because the enzyme's structure is compromised, leading to a loss of its catalytic function.
Why does enzyme activity differ at 0 degrees and 100 degrees?
it becomes denatured and inactive
When does lipase appear?
Lipase appears in the blood together with another enzyme called amylase following damage to or diseases affecting the pancreas. It was once thought that abnormally high lipase levels were associated only with diseases of the pancreas.
Which of the following procedures would identify the enzyme that catalyzes the carboxylation of ribulose 1 5 bisphosphate?
purifying a variety of proteins from plant extracts and testing each protein individually to see if it can carboxylate ribulose-1,5-bisphosphate
What does enzyme do between o degrees c and 30 degrees c?
What enzyme? There are several. I am pretty sure they don't all react the same.
The enzyme phosphofructokinase is an important enzyme that plays a significant regulatory role in glycolysis. Which of the following conditions would be expected to result in increased activity of this enzyme?
Low levels of ATP
What are the effects of physical activity on enzyme activity?
Physical activity can alter the shape of enzyme which can cause damage or may the enzyme become inactive
What switchs on enzyme activity while what can switch off or reduce enzyme activity?
Enzyme activators like cofactors or substrates can switch on enzyme activity by binding to the enzyme and promoting its function. Conversely, inhibitors can switch off or reduce enzyme activity by binding to the enzyme and preventing its normal function.
What do activators and inhibitors help regulate?
Activators and inhibitors help regulate the activity of enzymes. Activators can enhance enzyme activity by binding to the enzyme, while inhibitors can decrease enzyme activity by binding to the enzyme and preventing it from functioning properly.
Can the presence of inhibitors or activitors affect enzyme activity?
Yes, inhibitors can decrease enzyme activity by binding to the enzyme and preventing substrate binding. Activators can increase enzyme activity by binding to the enzyme and enhancing substrate binding or catalytic activity. Both inhibitors and activators can modulate enzyme activity by changing the enzyme's structure or function.
What can change the way an enzyme acts?
Enzyme activity is affected by other molecules, temperature, chemical environment (e.g., pH), and the concentration of substrate and enzyme. Activators are molecules that encourage enzyme activity, and inhibitors are enzymes that decrease enzyme activity. Sometimes a cofactor is necessary for the enzyme to work.
Which of the following is not used to determine metabolic activity?
Temperature is not typically used to determine metabolic activity, as metabolism is more directly influenced by factors such as enzyme activity, substrate availability, and hormonal regulation. Temperature can indirectly affect metabolic rate by influencing enzyme function and reaction rates.
Which blocks enzyme activity by binding to the site of an enzyme?
inhibitor
How does the allosteric enzyme curve illustrate the relationship between enzyme activity and the binding of regulatory molecules?
The allosteric enzyme curve shows how enzyme activity changes when regulatory molecules bind to the enzyme. This curve demonstrates that the binding of regulatory molecules can either increase or decrease enzyme activity, depending on the specific enzyme and regulatory molecule involved.
Why is protein concentration necessary for accurate comparison of the enzyme activity of the fractions?
Enzyme activity sometimes reflects the amount of protein expressed in a cell--however, due to enzyme inhibitors, the enzyme activity is not always reflective of the amount of protein expressed by a cell.
What determine an enzymes activity?
There are several things that determine an enzyme's activity. The main determinants include the structure of the enzyme, temperature, pH and so much more.
What can you do to regain the activity of the enzyme?
To regain the activity of an enzyme, you can try adjusting the pH and temperature to the optimal conditions for that specific enzyme. You can also remove any inhibitors that may be present, such as heavy metals or competitive inhibitors. Additionally, you can try adding cofactors or coenzymes that may be necessary for the enzyme to function properly.
