Enzyme Regulation I: Zymogens And Protien Inhibiotrs Flashcards
What are four examples of enzyme regulation we need to know?
Define what Zymogens are. And why we need them.
The inactive precursors of enzymes.
We need them because we cannot create the enzyme in the pancreas otherwise, it would just break down molecules in the pancreas, as well as we don’t want them to be breaking down stuff all the time only when they are. So just making the precursors that can easily form into the enzyme as much more efficient and safe.
Very important they aren’t active when they are made in the pancrease!
How do we activate zymogens?
They are activated by cleavage by another protease.
Zymogen activation is a cascade effect. Explain it.
Trypsin can activate more trypsin and activate lots of other things as you can see in the picture. And one trypsin can activate way more than one thing it can activate multiple things from one trypsin.
Explain enzyme activity control by an inhibiting protein. Why is it so important we inhibit them?
Important: cause of how powerful the enzymes cascade effect is.
Note: VERY small Ki, one of the tightest attachments!
What is the same and what difference between enzyme control by an inhibiting protein of Pancreatic Trypsin inhibitor (PTI) VS. Ribonuclease inhibitor.
Both have some of the tightest known protein/protein interface.
But unlike the pancreatic inhibitor which very closely mimics the substrate molecular structure, the ribonuclease inhibitor instead has incredible electrostatic complementary interface that is also very large.
