A protein that acts as a catalyst for a bichemical reaction.
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.
A reactant in an enzyme catalyzed reaction.
The molecule produced.
Acetylcholinesterase breaks down 10,000 _____ molecules per second.
_______ transfer phosphate groups from one molecule to another at the speed of 1,000 per second.
Many enzymes are conjugated proteins that require nonprotein portions known as ______
Some cofactors are metal ions, others are nonprotein organic molecules called _______.
Many coenzymes are _______, which must be ingested in our diet since we can't produce them.
Iron, zinc, copper, selenium...Nutritionists call these ____ _________.
Enzymes are divided into ____ main classes.
Catalyze oxidation-reduction reactions. Addition or removal of oxygen or hydrogen. Hydrogenation and dehydrogentaion are included in this category.
Catalyze transfer of a group from one molecule to another.
Catalyze the hydrolysis of substrate- the breaking of bond with addition of water.
Catalyze the isomeration (rearrangement of atoms) of a substrate in reactions that have one substrate and one product.
Catalyze the bonding of 2 substrate molecules. Usually this is accomplished by dehydration synthesis.
When nonprotein portion of an enzyme is an organic compound,
it is called a (an) ________. (It usually fits into the active site.)
The molecule that is comes out of the active site at the end of the
reaction is refered to as the _______.
What class of enzyme would convert a disaccharide to monosaccharides?
What class of enzyme would move an hydroxyl group from one molecule to another?
What class of enzyme would combine two amino acids to make a dipeptide?
What class of enzyme would convert an amide into a carboxylic acid and an amine?
What class of enzyme would convert an aldehyde into a carboxylic acid?
What class of enzyme would move the hydroxyl group on 2-hydroxypentane to form 3-hydroxypentane?
Classify the enzyme that changes 2-pentanol to 2-pentanone.
Changes 1 big molecule to 2 small molecules
Moves things around internally
Changes 2 small molecules to 1 big molecule
Adds or removes hydrogen or oxygen
Classify the enzyme that changes 2-pentanol to 3-pentanol. (Major class)
Classify the enzyme that changes 2-pentene to 1-pentene.
Classify the enzyme that takes fatty acids and glycerol and makes triglycerides. (Major class)
Classify the enzyme that adds an acetic acid to the hydroxyl group at the end of choline
to make acetylcholine.
Classify the enzyme that would convert a triglyceride into 3 fatty acids and glycerol.
Classify the enzyme that would remove a phosphate ion from ATP and put it on glucose, resulting in ADP and glucose-6-phosphate. (Subclass)
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.
Classify the enzyme that breaks peptide bonds. (Subclass)
Classify the enzyme that changes 2-amino-2-pentanol and cyclohexanol to 2-pentanol and 3-aminocyclohexanol. (Subclass)
Classify the enzyme that changes 2-pentanone to pentanal.
Noncompetitive inhibition is always irreversible (True/False)
competitive inhibition is often reversible (True/False)
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
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
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.
Which type of enzyme regulation can be used when you need an enzyme to be turned on instantly?
Which type of enzyme control must be influenced by hormones?
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?
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 ________.
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 ________.
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.
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.
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 __________ .