answersLogoWhite

0


Best Answer

Pepsin degrades proteins so if it was active it would immediately begin digesting all the proteins in the cell. Therefore it is produced from a precursor known as a zymogen or proenzyme. Pepsin's proenzyme form is pepsinogen which is transformed to the activated pepsin protein.

User Avatar

Wiki User

14y ago
This answer is:
User Avatar

Add your answer:

Earn +20 pts
Q: Why can pepsin not be produced in its active form?
Write your answer...
Submit
Still have questions?
magnify glass
imp
Related questions

Does hydrochloric acid produced in the stomach destroy pepsin?

No quite the opposite the low pH allows the autocleavage of pepsins zymogen pepsinogen into the active form pepsin.


What enzyme start to digest proteins in the stomatch?

Pepsin is produced by stomach cells in its inactive form pepsinogen, Pepsinogen is then activated by the stomach acid into its active form, pepsin. Pepsin breaks down the protein in the food into smaller particles.


What is the difference between pepsin and pepsinogen?

Pepsin is a powerful protein digesting enzyme which is far too dangerous in its active form so it is released in an inactive pepsinogen form by the cell and activated only in the digestive tract where it is required to be active.


What are the enzymes produced in the stomach?

The main enzyme in the Stomach is Pepsin which is used to digest protein. Only protein digestion occurs in the stomach and almostt no absorption, (only a little alcohol). This protein is not secreted as its active form (ie not as pepsin) but as the Zymogen (the inactive precursor to proteins) Pepsinogen which cleaves in a low pH to form the active enzyme.


What will happen if body just makes fully active form of enzymes?

Consider the stomach. The inactive form of the digestive enzyme pepsin is called pepsinogin. ( spelling may be wrong ) It takes the release of hydrochloric acid in the stomach to activate this pre-enzyme into pepsin, the active form. You would be digesting your own stomach tissue if pepsin was always active.


Why would you predict the pepsin would not digest starch?

Because Pepsin is the active form of a protein manufactured in the stomach.


Where is pepsin produced What is the effect of pepsin on protein?

Pepsin is produced in the stomach. Pepsin is an enzyme that digests (hydrolyses) proteins into smaller polypeptide molecules.


Is pepsin produced by the pancreas?

Pepsin is an enzyme whose responsibility it is to break down proteins in the body. Pepsin is not produced by the pancreas; it is produced by the stomach.


Why is pepsin stored under pepsinogen?

Pepsinogen becomes pepsin when activated by the stomach's Hydrochloric acid. This protein digest proteins, it could not be produced nor stored in the body's cells in its active form because it would destroy the cell that made it. The cells protect themselves by producing and storing the enzyme in an inactivated form.


Does pepsin affect pH?

Pepsin doesn't affect the pH but it is active in an acidic environment.


Would pepsin work in your mouth?

No. Pepsin is the active form of a protein manufactured in the stomach called pepsinogen. In order to become active, it has to come into contact with HCl (hydrochloric acid). HCl isn't present in your mouth (I hope!), so pepsinogen, even if it WERE in your mouth, could never become active there.No, the pepsin enzyme is located in the stomach, the enzymes amylase and lipase are found in saliva in the mouth


Which of these enzymes is not produced by the pancreas?

Pepsin