Zusammenfassung der Ressource
Enzymes
- Structure
- each reaction requires a specific enzyme
- globular proteins that act as catalysts
- Active site: the area involved in a reaction
- complementary in
shape to substrate
- enzyme-substrate
complex
- chemically changes the substrate by
breaking bonds within, the substrate
changes shape and no longer first substrate
- Models
- Lock and Key
- complementary
to one enzyme
- substrate molecules -
free kinetic energy
-collide with active site
- bonds break and end
product formed
- suggest that enzyme
works like a lock and
operated like a key
- induced fit
- suggest that enzyme's
active site is similar to
but not fully
complementary to the
substrate
- Substrate binds to enzyme,
active site changes shape to
become complementary to
substrate
- this explains how activation energy is
lowered, as the enzyme changes shape
it puts pressure on the bonds of the
substrate lowering the activation energy
- also explains why other molecules
can affect enzyme activity
- Factors effecting enzyme activity
- A change in shape of
active site
- A change in the number of
collisions
- Effect of Temp.
on Enzyme
- Above 40 degrees.
- kinetic energy causes
enzymes to vibrate
- hydrogen bonds break,
tertiary shape changes
enzyme denatures
- At 40 degrees
- more kinetic energy, more change of collisions, more e-s complexes,
more product, ROR increased
- Effect of pH on enzyme
- if higher than optimum pH, denatures due to
Hydrogen AND Ionic bonds breaking
- Competitive Inhibitors
- similar in shape
- competes for active site
- Fewer enzyme substrates
- lowers rate of reaction
- Non competitive inhibitors
- different in shape to substrate
- binds away
from active site
- changes active site
- no enzyme-substrate
complex