Q1. Why is PFK important in the glycolysis pathway? What does it
do within it's rate-limiting...
Q1. Why is PFK important in the glycolysis pathway? What does it
do within it's rate-limiting step? Think about the Committed,
rate-limiting and reversible steps in this pathway.
Solutions
Expert Solution
Answer-
According to the given
question-
We know that Glycolysis occurs in
the cytosol of the cell and convert glucose molecule into pyruvate,
Gluconeogenesis occurs mainly in the liver, and responsible for
providing the glucose when the amount of stored glycogen become
exhausted. Gluconeogenesis is defined as the reverse process of
Glycolysis. In Glycolysis seven enzymatic steps are reversible and
three reactions are Exergonic and are irreversible, such as the
reaction catalyzed by the enzyme phosphofructokinase – 1 or PFK-1,
pyruvate kinase, and hexokinase.
Phosphofructokinase – 1 enzyme is
responsible for converting the fructose 6- phosphate into fructose
1, 6- bisphosphate while fructose 1,6-bisphosphate is converted to
fructose 6-phosphate with the help of enzyme fructose 1,6-
bisphosphatase or FBPase-1 in Gluconeogenesis.
Glucose 6-phosphate has several
fates, it can join the Glycolysis, or pentose phosphate
Pathway as well as glycogen synthesis. The reaction catalyzed by
phosphofructokinase – 1 is irreversible and considered as
rate-limiting steps of Glycolysis because the glucose will join the
pathway of Glycolysis.
phosphofructokinase – 1 is a
complex enzyme and has substrate-binding sites, as well as several
regulatory sites for binding of several allosteric activators as
well as inhibitors. ATP is work as the substrate for
phosphofructokinase – 1 but also end product of Glycolysis. When
the concentration of ATP inside the cell is high which means that
the rate of producing of ATP is very high than its consumption then
the ATP is responsible for inhibiting the activity of
phosphofructokinase – 1 by binding its allosteric site and lower
the binding affinity of phosphofructokinase – 1 for the substrate
fructose 6-phosphate .
Adenosine Diphosphate or ADP, as
well as Adenosine monophosphate or AMP, increases inside the cell
when the concentration of ATP decreases and act allosterically on
the enzyme phosphofructokinase – 1 and reverse the inhibition by
ATP on the enzyme phosphofructokinase – 1.
So the activity of
phosphofructokinase – 1 is increases when Adenosine Diphosphate or
Adenosine monophosphate accumulates inside the cell and becomes
lower when ATP accumulates. Citrate also works as an allosteric
regulator of phosphofructokinase – 1. high concentration of citrate
increases the effect of ATP on phosphofructokinase – 1 and reduces
the glucose flow through glycolysis.
Phosphofructokinase is an enzyme that controls the rate of
glycolysis. The activity of PFK happens in allosteric regulation by
several molecules. Which of the following specific allosteric
regulator or regulators would most likely be bound to PFK in yeast
cells that are growing in anaerobic conditions?
1. citrate as an allosteric inhibitor
2. ADP as an allosteric inhibitor
3. citrate as an allosteric activator
4. ADP as an allosteric activator
5 AMP as an allosteric activator
6. ATP as an...
Q1. What is the S-layer? How does it function and what is it's
structure?
Q2. What benefits do gut microbes offer humans and what do
humans offer gut microbes?
what does the Federal reserve do? what are it's roles
and responsibilities? how does the Federal reserve regulate the
flow and creation of U.S. currency?