enzymes as drug targets Flashcards
what is an enzyme
Enzymes are biological catalysts that speed up the pace of
chemical reactions.
what are ezymes examples of
protein
what is the difference between a reaction with and without enzyme
- enzyme have reduced activation energy
what is Vmax
The maximum rate at which an enzyme
can carry out a reaction
what is Km
Substrate concentration at which the
enzyme will work at ½ Vmax
A molecule binds to an enzyme and decreases the ability of the active site to bind to the substrate. This is called
competitive inhibitor
define enzyme inhibitor
molecules that reduce or abolish enzyme activity
what is competitive inhibition
the inhibitor will bind to an enzyme at the
active site, competing with the substrate. As a result, the KM will
increase, and the Vmax will remain the same
How do a competitive inhibitor affects enzymes
Binds to the active site and blocks the substrate + compete
Why is the Km affected in the presence of a competitive inhibitor
Because it requires more substrate to achieve the same max as without the inhibitor
What happens to Km in the presence of a non-competitive inhibitor?
Km will not be affected in the presence of a non-competitive inhibitor
define non competitive inhibition
In non-competitive inhibition, the inhibitor will bind to an enzyme at
its allosteric site away from the active site; therefore, the binding affinity KM, of the substrate with the enzyme will remain the same and vmax will decrease.
what is DD transeptidase?
- pencillin binding protein
- carries out cross-linking of peptidoglycan wall subunit for bacteria
- beta lactam antibiotics bind to and irreversibly inhibit DD transeptidase
- beta lactam preventing the building of new bacterial cell wall - spheroplast
beta lactamases
enzymes produced by bacteria that breaks open the beta lactam ring, in activating beta lactam antibiotic ( antibiotic resistance)
HIV protease
- activity central to HIV replication
- processes viral proteins required for formation of active virus
- atazanavir
