Which is the rate limiting step in this reaction?
The decomposition of the ES complex to form P + E
Explain the COMPETITIVE inhibitor.
- Reversible
- The inhibitor competes with the substrate for the active site of the enzyme.
What do the LONG-TERM mechanisms consist of?
Control of protein turnover (renovació)
What is Km? And which is its formula?
Km is the concentration of the substrate, S, when the initial rate is half of the maximum rate.
The combination of the reaction constants
Km = (K2 + K-1) / K1
Explain the UNCOMPETITIVE inhibitor:
- Reversible
- The inhibitor only binds when the substrate and the enzyme are bound together (enzyme-substrate complex)
What do the SHORT-TERM mechanisms consist of?
- Feedback inhibition
- Cooperativity
- Allosterism
Which is the Michaelis-Menten equation?
Explain the NON-COMPETITIVE inhibitor:
- Reversible
- The inhibitor binds to both the enzyme and the enzyme-substrate complex
What is the feedback inhibition?
The metabolic pathway is inhibited by the end product
What is Kcat? And its formula?
Constant of catalysis, number of molecules of substrate that can be converted into product per unit of time by enzyme molecules when it is fully saturated with substrate
Kcat = Vmax/Etotal
What are the irreversible inhibitions?
The inhibitor binds to the enzyme, leaving it inactivated (destroying it or making a very stable association with covalent bonds.)
What is cooperativity?
Influence that the binding of a ligand to an orthosteric site has on the binding of the ligand to a second (and successive) orthosteric site
What does the ratio between Kcat/Km measure?
It's the ratio of catalytic efficiency
What is allosterism?
Unión de una molécula en un sitio diferente al sitio activo, conocido como el sitio alostérico. La unión de un regulador alostérico puede facilitar o inhibir la unión del sustrato al sitio activo, afectando así la velocidad de la reacción química que catalizan