BCH211 - Exam 2 assesses key concepts in biochemistry, focusing on enzyme activity, metabolic processes, and the role of vitamins. It evaluates understanding of protein sensitivity to temperature, anabolism, enzyme inhibition, and optimal enzyme conditions.
True
False
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Competitive inhibition
Noncompetitive inhibition
Neither form of inhibition
Both forms of inhibition
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ATP
Acetyl CoA
Glucose
Pi
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True
False
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Proenzyme
A zymogen
A cofactor
A substrate
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Diastereomers are those compounds that can only have 6 chiral carbons
Diastereomers are all of the isomers for compounds that can have two or more chiral centers
Diastereomers are isomers that only have 1 chiral center.
Diastereomers are isomers that are mirror images of the other
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High molecular weight
Specificity
Susceptibility to denaturation
High turnover rate
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Both D and L
D
L
Neither D nor L
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Substrate site
Primary site
Active site
Substrate bond
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Entropy doesn't change.
ATP has no entropy.
Entropy increases.
Entropy decreases.
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Option 1
Option 2
Option 3
Option 4
A catalyst
An activator
A carbohydrate
A lipid
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Polysaccharides
Oligosaccharides
Disaccharides
Monosaccharides
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23
84000
480
1400
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A hemiacetal
An acetal
An amide
An ester
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Zymogen
Cofactor
Substrate
Isozyme
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Resembles the substrate
Binds at a site other than the active site
Reduces Km
Increases Vmax
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Sucrose
Glucose
Galactose
Fructose
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This is an uncompetitive inhibitor
This is a noncompetitive inhibitor
This is a competitive inhibitor
This is an irreversible inhibitor
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True
False
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Optimum conditions
Low pressure, high temperature
Room conditions
Standard conditions
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Ribose
Maltose
Galactose
Glucose
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A decrease in enzyme concentration
A decrease in substrate concentration
An increase in enzyme concentration
An increase in substrate concentration
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The active site changes its conformation to fit the transition state.
The substrate changes its conformation to fit the active site.
The active site changes its conformation to fit the product.
The active site changes its conformation to fit the substrate.
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Induced-fit theory
Physically-fit theory
Expanding-fit theory
Lock-and-key theory
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Substrates
Activators
Apoenzymes
Coenzymes
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Starch
Sucrose
Fructose
Lactose
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5.5
6.5
9.5
3.0
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Is this a reducing sugar? (YES)
1 pt for placing the beta structure
1 pt for the glycosidic linkage
2 pts for each sugar
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Enzymes can produce a reaction transition state with a reduced activation energy.
There are enzymes that interact with one enantiomer, but not the other.
Enzymes are not used up during the reaction in which they are involved
Enzymes can reduce the net energy of a reaction
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0.0254 millimolar (mM)
0.523 millimolar (mM)
5.23 millimolar (mM)
39.4 millimolar (mM)
75.3 millimolar (mM)
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Glycosides
Simple sugars
Reducing sugars
Oxidizing sugars
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B (beta)
Cis
Trans
Alpha
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Sucrose
Amylopectin
Amylose
Cellulose
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-40 Joule/mol
-15 Joule/mol
-10 Joule/mol
-2540 Joule/mol
You cannot tell from the given data
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It is easier to see whether points deviate from a straight line than from a curve
It is not affected by the presence of inhibitors
It can be used whether or not the enzyme displays Michaelis-Menten kinetics
It can work with allosteric enzymes
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Changing the value for Vmax
This type of inhibitor both changes the Km and interferes with substrate binding
Modifying the Km value
Interfering with substrate binding
All of these are correct
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Irreversible inhibitor
Noncompetitive inhibitor
Competitive inhibitor
All of these
Non of these
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A ketohexose
An aldopentose
A ketopentose
An aldohexose
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Allosteric production
Feedback control
Biofeedback
Enzyme induction
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A (1-4)
B (1-4)
B (1-6)
A (1-6)
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Glycogen
Amylopectin
Amylose
Cellulose
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A D form
Neither D nor L
Both D and L
An L form
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You cannot tell from the data given
Competetive
Irreversible inhibition
Non-competitive
More than one answer is correct
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Option 1
Option 2
Option 3
Option 4
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