8. a. Which steps and enzymes are targets of regulation in the metabolism and catabolism of glucose through glycolysis and gluconeogenesis?
Be sure to include what molecules are utilized in regulation and their potential effects in each pathway.
For the following scenarios, please explain in detail the effect on both glycolysis and gluconeogenesis, as well as the effects on any of the enzymes.
b. The cellular concentration of ATP increases
c. The cellular concentration of ATP decreases
d. The body has high blood sugar
e. The body has low blood sugar
In: Biology
Applying your knowledge of metabolism, glycolysis starts with one molecule of glucose (6C) and produces a net total of __________.
View Available Hint(s)
Applying your knowledge of metabolism, glycolysis starts with one molecule of glucose (6C) and produces a net total of __________.
| 1) one pyruvates; 2 NADH; 2 ATP |
| 2) one pyruvate; 2 NADH; 4 ATP |
| 3) two pyruvates; 4 NADH; 2 ATP |
| 4) two pyruvates; 2 NADH; 2 ATP |
In: Biology
In order to move from one place to another in the cell fatty acids need to associate with lipid chaperones. Why are these chaperones required, and what is the name of this group of proteins that are responsible for this trafficking of fatty acids within the cell? What is the main distinguishing feature of these proteins that makes it possible for fatty acids to move within the cell?
In: Biology
Describe the characteristics of inorganic and organic catalysts (enzymes), as well as the characteristics that apply only to enzymes.
Explain how and why temperature and pH affect enzyme activity
Explain how enzyme concentration, substrate concentration, and enzyme inhibitors affect the rate of enzymatic activity according to the Michaelis-Menten model.
In: Biology
Sketch a general Lineweaver-Burke plot that illustrates the kinetic behavior of a non-allosteric enzyme. Identify on your plot the features that allow one to determine Vmax and KM for the enzyme.
How would one use a Lineweaver-Burke plat of enzyme kinetic data to identify an inhibitor's mode of action?
In: Chemistry
|
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
|
|
In: Accounting
what is the difference of enzyme from body and enzyme which had been created or they are just the same thing?
In: Biology
Explain why the enzyme carbonyl phosphate synthetase can be considered the most important enzyme in the to the urea cycle?
In: Biology
Hurry please!!
For the following allosteric regulators of CAC:
In: Biology
An enzyme with a Vmax of 100 umol/minute and a Km of 10 uM was
reacted with a irreversible active site specific inhibitor. After
reaction with the inhibitor, the enzyme was assayed using a 2 mM
concentration of substrate, and it gave a reaction rate of 20
umol/min. What percentage of the enzyme did the inhibitor
inactivate?
In: Biology