Enzymes
Kinetics
Regulation Strategies
Catalytic Strategies
Extra
100

These make enzymes powerful catalysts

What is lowers activation energy and creates a more stable transition state? What is highly specific?

100

This is the minimum amount of kinetic energy that reactant molecules must possess in order to overcome their mutual electron cloud repulsions to break/weaken their bonds

What is activation energy?

100

This is reversible, noncovalent binding of regulatory molecules at dedicated allosteric sites

What is allosteric control?

100

This is the method used in enzymes that have more than one substrate or two substrates that are bound close together/at adjacent sites in the active sites.

What is catalysis by approximation?

100

These are enzymes that differ in amino acid sequence but catalyze the same reaction. 

What are isozymes or isoenzymes?

200

Holoenzymes are an enzyme plus this molecule

What is a cofactor?

200

This is the value of reaction rate when an enzyme is fully saturated

What is Vmax?

200

This is zymogens or proenzymes that have to be trimmed in order to be turned on and become active

What is proteolytic cleavage?


200

This is the enzyme that catalyses hydrolysis reactions that cleave covalent peptide bonds. 

What are proteases?

200

These are protein phosphatases.

What is catalyzing the removal of phosphate groyps from proteins?

300

This is the function of active sites of enzymes

What is the location of the substrate binding and undergoing a chemical reaction?

300

This is the number of substrate molecules converted into product per unit of time at a single catalytic site when the enzyme is fully saturated with substrate

What is Kcat?

300

This is the quaternary structure of ATCase

What is 2 catalytic trimers and 3 regulatory dimers?

300

This is the enzyme that is active in digestion in the duodenum and is produced in the pancreas.

What is chymotrypsin?

300

This is the class that protein kinase A is part of. 

What is serine/threonine kinases?

400

This is the model that describes the active site not being a perfect match for the substrate but undergoes a conformational change as the substrate interacts with the enzyme

What is induced fit?

400

This is how the rate of a forward reaction is measured

What is measuring amount of substrates compared to the amount of products?

400

This is PALA

What is a bisubstrate analog that resembles the reaction intermediate and is exogenous?
400

These are the physiological purposes of carbonic annhydrase

What is converting toxic gas waste into HCO3-? What is turning bicarbonate into carbon dioxide if the carbon dioxide levels are too low?

400

These are the catalytic strategies that chymotrypsin uses. 

What is covalent catalysis, approximation catalysis, and acid-base catalysis?

500

These are examples of how enzymes transform energy into a different form of energy

What is photosynthesis and ATP synthesis?

500
This is E + S <--> ES --> E + P

What is Michaelis-Menten Model?

500

This is the allosteric enzyme that can only exist in T and R states; binding of the ligand shifts the equilibrium between the 2 states.

What is the concerted model of cooperativity?

500

This is the relationship between methylases and restriction endonucleases.

What is methylases add methyl groups to host's own matching DNA prevent restriction endonucleases from digesting it?

500

These are the effects zinc has on water in carbonic anhydrase's active site.

What is reducing the pKa of water, generating OH- from H2O at ph of 7, and holds OH- rigidly in place?

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