Enzyme Elimination
Equation Equilibrium
Cameron's Conundrums
Cam's Continuum
How do you answer this?
100

What is the primary source of the energy enzymes use to reduce activation energies?

noncovalent enzyme-substrate interaction.

100

What is the steady state?

: the reaction period where [ES] is constant

100

ATCase catalyzes the conversion of carbamoyl phosphate and aspartate into N-carbamoylaspartate, a precursor in pyrimidine biosynthesis. What roles do ATP and CTP play in this reaction?

heterotropic modulators

100

A reaction where the rate depends only on the concentration of S is called a _____ reaction.

first order

100

What are the four kinds of B. Reversible- noncovalent association? 

Competitive, Uncompetitive, mixed , non-competitive inhibition

200

Which type of enzyme inhibitor repeatedly exchanges with the substrate for the active site?

Competitive

200

What does the y intercept on a Lineweaver-Burk plot represent?

1/Vmax

200

 Penicillin inhibits _____ during peptidoglycan synthesis.

the transpeptidase reaction

200

Plots of V0 versus [S] for allosteric enzymes produce _____ saturation curves.

sigmoid

200

What are the three catalytic triad amino acids? 

Ser, His, Asp

300

How is a protein's phosphorylation status regulated?

Different enzymes phosphorylate and dephosphorylate the protein such that activation and deactivation are separately regulated.

300

Consider the reaction E + S ⇌ ES ⇌ EP ⇌ E + P What do ES and EP represent in the reaction?

reaction intermediates consisting of transient complexes of the enzyme with the substrate and with the product, respectively

300

What is a cofactor?

an inorganic ion required for enzyme activity

300

At a substrate concentration that is much greater than the Km for the reaction, which statement is true (assuming the enzyme obeys Michaelis-Menten kinetics)?

The reaction velocity is equal to Vmax.

300

What are the 4 ways to regulate activity? 

Allosteric, Reversible covalent modification, Removal of peptide bonds (proteolytic cleavage), binding of separate (regulatory proteins)

400

Which type of enzyme inhibitor competes with the substrate for the active site and participates in the initial steps of the reaction before permanently inhibiting the process?

:) suicide

400

According to the Michaelis-Menten model, kcat (turnover number) can be defined as the

maximum number of product molecules generated by a single enzyme over a specified time.

400

Metal ions, such as Fe2+ and Mg2+, that are required by an enzyme for its ability to function are called? 

cofactors

400

Which enzyme mechanism involves the transfer of a proton from one molecule to another?

acid-base catalysis

400

True or False

Mixed is reversible by high [S]

False

500

Complex organic or metalloorganic molecules, such as lipoate or tetrahydrofolate, required for enzyme function are called

coenzymes.

500

What does the x intercept on a Lineweaver-Burk plot represent?

−1/Km

500

Why do allosteric enzymes display a sigmoid instead of a hyperbolic kinetics plot?

Modulator binding provokes cooperative interactions between multiple protein subunits.

500

What do isomerases do?

convert isomers

500

Name 2 features of the allosteric enzymes. 

Modulators are usually heterotropic

Modulators bind non-covalently

Large, multisubunit enzymes are often allosteric.