Cooperativity & Glycolysis: Regulation of Enzymes

In summary, the efficiency and rarity of cooperativity in enzymes with tertiary structure suggests that glycolysis is inefficient and rarely found in present day organisms. Additionally, the lactate produced as a result of fast glycolisis pathways is moved to mitochondria for further oxidation.
  • #1
DemiMike
9
0
is it true that cooperativity is rare in enzymes with tertiary structure
and that Glycolysis is inefficient and therefore rarely found in present day organisms

i am not sure.. but iwas also wondering that a particular enzyme is likely subject to only a few forms of the regulation we discussed in lecture

=o
 
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  • #2
If glycolysis is inefficient and rare, what am I doing storing up all this glycogen in my muscles and liver?
 
  • #3
DemiMike said:
is it true that cooperativity is rare in enzymes with tertiary structure
and that Glycolysis is inefficient and therefore rarely found in present day organisms

i am not sure.. but iwas also wondering that a particular enzyme is likely subject to only a few forms of the regulation we discussed in lecture

=o

Glycolysis is a major energetic pathway in any organism I can think of. The net yield of ATP in glycolisis is quite small , of only 2 ATPs.This pushes many ppl to label glycolisis as an "inefficient pathway"

But there are other considerations as well. Skeletal muscles are highly efficient in breaking down glucose at very high rates. In effect, this yields large quantities of ATP formation in quite short times. It is this high rate which makes possible high intensity efforts, which in no way can be sustained by oxidative metabolism.

Besides, oxidative metabolism and glycolityc metabolism are intrinsically linked. The lactate which is formed as a result of fast glycolityc pathways is moved, through the intracellular lactate shuttle, from cytosol to mitochondria, where it is further oxidized. Cell to Cell lactate shuttles also appear to exist. This is opposed to the "classic" view where the only fate for the lactate produced as the result of fast glycolisis is reconversion to glucose through the pathways of Cori cycle.

As for regulation what did you discussed in lecture ?
 
Last edited:

Related to Cooperativity & Glycolysis: Regulation of Enzymes

1. What is cooperativity?

Cooperativity is a type of enzyme regulation in which the binding of one substrate molecule to an enzyme affects the binding of subsequent substrate molecules. This can either enhance or inhibit the enzyme's activity.

2. How does cooperativity relate to glycolysis?

In glycolysis, cooperativity plays a crucial role in the regulation of enzymes. For example, the enzyme phosphofructokinase (PFK) exhibits positive cooperativity with its substrate, fructose-6-phosphate. This means that as more fructose-6-phosphate molecules bind to PFK, the enzyme's activity increases, leading to an overall increase in glycolysis.

3. What is the role of allosteric regulators in cooperativity?

Allosteric regulators are molecules that bind to an enzyme at a location other than the active site, and can either enhance or inhibit the enzyme's activity. In cooperativity, allosteric regulators can bind to an enzyme and cause conformational changes that affect the enzyme's cooperativity with its substrate.

4. How is enzyme cooperativity regulated?

Enzyme cooperativity is regulated by various factors, including substrate concentration, pH, and temperature. Additionally, allosteric regulators and the presence of other enzymes or cofactors can also affect cooperativity.

5. What are the implications of dysregulation of cooperativity in glycolysis?

Dysregulation of cooperativity in glycolysis can lead to various metabolic disorders. For example, mutations in the gene that codes for PFK can result in a decrease in cooperativity and ultimately lead to a decrease in glycolysis, causing conditions such as glycogen storage disease. On the other hand, overactivation of cooperativity can lead to excessive glycolysis and contribute to diseases such as cancer.

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