Please wait while the transcript is being prepared...
Greetings. Welcome to this Principles of Biochemistry lecture series.
I am Jerry Feigenson.
I am a professor in
the Department of Molecular Biology and Genetics at Cornell University in the USA.
In the 10th lecture, you learn to think of
enzyme efficiency as the lowering of the free energy of the transition state.
You saw how measuring inhibition of enzymes can inform us about how the enzyme works.
Then you saw step-by-step how chymotrypsin catalyzes peptide hydrolysis.
In this 11th lecture you will learn that amino acids
need some help to accomplish all the chemistry that's used by enzymes.
To do this, you will see that besides amino acids,
proteins use multivalent cations,
or small organic molecules that are specialized for
redox reactions, or have long flexible linkers,
or facilitate electron transfer pathways.
You will see that regulated enzymes are controlled
by their concentration and by their activity.
For activity control, Allosteric regulation has special value.
We will look at two enzymes in detail.
The allostery of aspartate carbomoyl transferase and chymotrypsin activation.