___ catalyze group-transfer reactions. ___ catalyze hydrolysis. ___ catalyze ligation or joining of two substrates.

___ catalyze lysis of a substrate. ___ catalyze oxidationreduction reactions.

___ catalyze structural change within a single molecule.
___ is an allosteric inhibitor of PFK-1 while ___ is an allosteric activator of PFK-1.

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

A ___ is the protein part of the holoenzyme.

A high Kcat would be consistent with a ___ (fast, slow) reaction.

apoenzyme/apoprotein

fast

African sleeping sickness is caused by ___.

Do allosteric enzymes exhibit typical Michaelis-Menten kinetics?

Trypanosomes

No

Do you want a high or low Km?

For the unimolecular reaction S --> P, the rate equation is ___.
If there is no spermine or spermidine then the cells cannot ___.

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.

stays the same, increases

decreases, stays the same

In uncompetitive inhibition the Vmax ___ and Km ___.

Irreversible inhibition is bound ___ while reversible inhibition is bound ___. Is regulation by covalent modification faster or slower than allosteric regulation?

decreases, decreases

covalently, noncovalently

slower

Michaelis-Menten Kinetics is a ___ or ___ order reaction.

More substrate would create a ___ (faster, slower) reaction.

zero, first

faster

Sigmoidal has ___ (one, more than one) binding site.

Spermine and spermidine have ___ (negative, positive) charges.

more than one

positive

The ___ is the energy difference between the ground state and the transition state.

energy of activation (Eact)

The ___ is the starting point for either the forward or reverse reaction.

ground state

The formation of E + P is the ___ step.

Trypanosomes are ___ (eukaryotes, prokaryotes) and ___ (multicellular, unicellular).

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