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Transferases
Hydrolases
Ligases
Lyases
Oxidoreductases
Isomerases
PEP, ADP
___ is the affinity of the substrate for the enzyme. ___ is the slowest step and the turnover number.
___ is when there are no ways of intermediates and everything takes place because the enzyme acts as one complex without entering the bulk solvent.
Km
Kcat
Metabolite channeling
A ___ is a coenzyme or metal ion that is tightly or covalently bound to the enzyme.
prosthetic group
A ___ is a complete active enzyme with its bound coenzyme and/or metal ions.
holoenzyme
A ___ is a compound that binds to an enzyme and interferes with its activity.
inhibitor
apoenzyme/apoprotein
fast
Trypanosomes
No
Low
V = k[S]
divide
In competitive inhibition the Vmax ___ and Km ___. In noncompetitive inhibition the Vmax ___ and Km ___.
In the absence of a substrate the enzyme is in the ___ state.
decreases, decreases
covalently, noncovalently
slower
zero, first
faster
positive
The ___ is the energy difference between the ground state and the transition state.
The ___ is the starting point for either the forward or reverse reaction.
ground state
rate-limiting
eukaryotes, unicellular
Vo vs. [S] curve is ___ (hyperbolic, sigmoidal). When ES is kept at a constant rate, it is called the ___ state.
When ES is still being formed, it is called the ___ state. With an activator Km ___ and with an inhibitor Km ___.
sigmoidal
steady
pre-steady
decreases, increases