Chapter 19

Terms	Definitions
A protein that acts as a catalyst for a bichemical reaction.	Enzyme
An enzyme can increase the speed of a reaction by _____ to ______ times faster.	hundreds to billions
A pocket in an enzyme with the specific shape and chemical makeup necessary to bind a substrate and where the reaction takes place.	Active Site
A reactant in an enzyme catalyzed reaction.	Substrate
The molecule produced.	Product
Acetylcholinesterase breaks down 10,000 _____ molecules per second.	Acetylcholine
_______ transfer phosphate groups from one molecule to another at the speed of 1,000 per second.	Kinases
Many enzymes are conjugated proteins that require nonprotein portions known as ______	cofactors
Some cofactors are metal ions, others are nonprotein organic molecules called _______.	coenzymes
Many coenzymes are _______, which must be ingested in our diet since we can't produce them.	vitamins
Iron, zinc, copper, selenium...Nutritionists call these ____ _________.	Trace minerals
Enzymes are divided into ____ main classes.	six
Catalyze oxidation-reduction reactions. Addition or removal of oxygen or hydrogen. Hydrogenation and dehydrogentaion are included in this category.	Oxidoreductase
Catalyze transfer of a group from one molecule to another.	Transferase
Catalyze the hydrolysis of substrate- the breaking of bond with addition of water.	Hydrolase
Catalyze the isomeration (rearrangement of atoms) of a substrate in reactions that have one substrate and one product.	Isomerase
Catalyze the bonding of 2 substrate molecules. Usually this is accomplished by dehydration synthesis.	Synthetase
Removes CO2	Decarboxylase
When nonprotein portion of an enzyme is an organic compound, it is called a (an) ________. (It usually fits into the active site.)	coenzyme
The molecule that is comes out of the active site at the end of the reaction is refered to as the _______.	product
What class of enzyme would convert a disaccharide to monosaccharides?	Hydrolase
What class of enzyme would move an hydroxyl group from one molecule to another?	Transferase
What class of enzyme would combine two amino acids to make a dipeptide?	Synthetase
What class of enzyme would convert an amide into a carboxylic acid and an amine?	Hydrolase
What class of enzyme would convert an aldehyde into a carboxylic acid?	Oxidoreductase
What class of enzyme would move the hydroxyl group on 2-hydroxypentane to form 3-hydroxypentane?	Isomerase
Aldehyde
Amide
Carboxylic Acid
Ketone
Classify the enzyme that changes 2-pentanol to 2-pentanone.	Oxidoreductase
Changes 1 big molecule to 2 small molecules	Hydrolase
Moves things around internally	Isomerase
Changes 2 small molecules to 1 big molecule	Synthetase
Adds or removes hydrogen or oxygen	Oxidoreductase
Classify the enzyme that changes 2-pentanol to 3-pentanol. (Major class)	Isomerase
Classify the enzyme that changes 2-pentene to 1-pentene.	Isomerase
Classify the enzyme that takes fatty acids and glycerol and makes triglycerides. (Major class)	Synthetase
Classify the enzyme that adds an acetic acid to the hydroxyl group at the end of choline to make acetylcholine.	Synthetase
Classify the enzyme that would convert a triglyceride into 3 fatty acids and glycerol.	Lipase
Classify the enzyme that would remove a phosphate ion from ATP and put it on glucose, resulting in ADP and glucose-6-phosphate. (Subclass)	Kinase
A significant increase in temperature of an enzyme catalyzed reaction will reduce the reaction rate because the _______________.	protein is partially or completely denatured
In an enzyme catalyzed reaction that usually occurs in the stomach, if the pH is changed from 2 to 7.4, how would it effect the reaction rate?	Stop the activity
In an enzyme catalyzed reaction, if enzyme concentration is tripled, how would it effect the reaction rate? (Assuming unlimited substrate.)	Triples the reaction rate
Classify the enzyme that changes octanoic acid to heptane and carbon dioxide.	Decarboxylase
Classify the enzyme that breaks peptide bonds. (Subclass)	Protease
Classify the enzyme that changes 2-amino-2-pentanol and cyclohexanol to 2-pentanol and 3-aminocyclohexanol. (Subclass)	Transaminase
Classify the enzyme that changes 2-pentanone to pentanal.	Isomerase
Noncompetitive inhibition is always irreversible (True/False)	False
competitive inhibition is often reversible (True/False)	True
At constant enzyme concentration, it is possible to achieve maximum enzyme rate when which of the following conditions occur? (The amount of enzyme is constant, but other factors can change.) A. there is no inhibitor present B. a competitive inhibitor is present C. a noncompetitive inhibitor is present D. none of the above	A, B
An allosteric regulator can _________. A. increase enzyme rates B. decrease enzyme rates C. bind with the active site D. If it is inhibitory, has it's effects minimized by adding large amounts of substrate E. bind somewhere other than the active site	A, B, E
Under what conditions can the effects of competitive inhibition can be reversed (allowing the reaction rate of the enzyme to increase to its normal maximum)? A. it can never be reversed B. at high subststrate concentrations C. it is irreversible if the inhibitor binds covalently or permanently D. it can be reversed but can never attain the maximum rate of the enzyme alone	B, C
Indicate which of the following characteritics are exhibited by a KINASE? A. They have a small piece of them cliped off by another enzyme to make them active. B. They add or remove a phosphate from an enzyme C. They are turned on or off by the addition of a phosphate group. D. They are an enzyme that regulates the activity of other enzymes. E. They are an inactive form of an enzyme that is made so that it doesn't work until it is turned on.	B, D
Which type of enzyme regulation can be used when you need an enzyme to be turned on instantly?	Proenzymes, Kinases
Which type of enzyme control must be influenced by hormones?	Genetic Control
Which type of enzyme control is used in blood clotting?	Proenzymes, Feedback Control
Which type of enzyme control is used when making most digestive enzymes?	Proenzymes
When determining how an inhibitor might affect the reaction rate of an enzyme, You need to know the relative difference in concentration between two factors. For non-comptetitive inhibiton, you need to know the difference in concentration between the inhibitor and the ________.	Enzyme
When determining how an inhibitor might affect the reaction rate of an enzyme, You need to know the relative difference in concentration between two factors. For competitive inhibiton, you need to know the difference in concentration between the inhibitor and the ________.	Substrate
In the cascade of proteins that results in a blood clot, the final protein, that actually forms the mesh of the clot, circulates in an inactive form in the blood. This protein is called __________ and it is (soluble/insoluble) in water.	Fibrinogen/Soluble
In the cascade of proteins that results in a blood clot, the final protein, that actually forms the mesh of the clot is called __________ and it is (soluble/insoluble) in water.	Fibrin/Insoluble
Drugs that slow the natural formation of angiotensin II (thus lowering blood pressure), are known as	angiotensin converting enzyme inhibitor
In the cascade of proteins that results in a blood clot, the final protein, that actually forms the mesh of the clot, needs to be converted from an inactive form to an active form. The enzyme that causes this conversion is called __________ .	Thrombin