Week 6 Flashcards
__________ are catalysts involved in biochemical reactions.
Enzymes.
Enzymes are usually __________ proteins.
Globular.
__________ is a molecule or molecules that acts as the reactant in an enzymatically catalyzed reaction.
Substrate.
_____________ is the location where the enzyme binds to the substrate and catalysis occurs.
Active site.
__________ model is when the active site is already in a configuration that can only fit 1 shape of substrate.
Lock and key.
_____________ catalyze reaction involving the gain or loss of electrons.
Oxidoreductases.
_____________ transfer on functional group to another.
Transferases.
____________ cleave a bond with water.
Hydrolases.
______________ break double bond using some other means than oxidation or hydrolysis.
Lyases.
___________ catalyze a rearrangement of the molecule.
Isomerases.
__________ join two molecules.
Ligases.
___________ is a type of transferase which specifically transfers a phosphate group from ATP to another molecule and thus also has hydrolase activity.
Kinase.
An induced fit binding model requires what to be reorganized to fit what?
The enzyme is reorganized to fit the substrate.
If there is enough substrate, the enzyme will reach full saturation this is called __________
Saturation Kinetic Curve.
The _____________ is a double reciprocal of Michaelis-Menten equation and an easier method to interpret graphical data.
Lineweaver-Burke Plot
The____________ is the number of reactions the enzyme can catalyze per unit of time. Also can be used to measure catalytic efficiency.
Turnover number.
____________ is an occurrence when rate-limiting step becomes the diffusion of enzyme and substrate together.
Diffusion controlled limit.
____________ prevent the generation of products.
Inhibitors
_____________ Covalently modifies the active site of the enzyme, irreversibly blocking its function, directly poisons the enzyme.
Suicide inhibitors.
_____________ competes directly with the substrate but can be overcome if the substrate concentration is high.
Competitive inhibition
_____________ binds to the ES complex and decreases Vmax but increases KM.
Uncompetitive inhibition
_______________ bind in the presence or absence of a substrate. Effective regardless of substrate concentration.
Mixed inhibition.
On a Lineweaver-Burke plot, the intercepts can be used to obtain which information about the reaction?
Km and Vmax.
In induced fit models, the enzymes bind substrates that favor the _______________.
Transition state.
In _______________ catalysis amino acid side chains donate or accept protons.
General acid-base.
In_____________ catalysis the active site metal can act as a redox active center.
Metal ion.
In________________ catalysis nucleophilic or electrophilic attack on an atom results in a covalent intermediate.
Covalent
______________ is an enzyme example of acid-base catalysis that is a natural antibiotic and the active site contains two negatively charged residues.
Lysozyme.
___________ is an example of metal ion catalysis.
Anhydrase.
____________ are enzymes that degrade proteins. Are important in protein maturation, blood clotting, and protein trafficking.
Proteases.
_____________ is an example of covalent catalysis and cleaves dietary protein on the C-terminus of Try,Phe, and Trp.
Chymotrypsin.
Cymotrypsin is a _____________ protease.
Serine.
The inactive for of chymotrypsin is called_____________
Chymotrypsinogen
What are the categories of proteases named after?
The catalyst responsible for generating the nucleophile
