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CHM 432 > Exam Three > Flashcards

Exam Three Flashcards

1
Q

What is required for enzymatic reactions?

A

Formation of an ES complex

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2
Q

What is the equation for a first order reaction?

A

rate = k[A]

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3
Q

What is the equation for a second order reaction?

A

rate = k[A][B]

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4
Q

What order reaction occurs when the amount of substrate has no effect on the rate?

A

zero

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5
Q

True or False: the higher the concentration of S, the faster the reaction

A

False, it is dependent on the amount of enzyme present

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6
Q

True or False: the higher the concentration of E, the faster the reaction

A

True, although technically there is normally a limited amount of enzyme

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7
Q

________ is an indicator of affinity for a substrate (binding efficiency)

A

Km

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8
Q

Does a smaller or larger Km indicate better affinity?

A

smaller

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9
Q

What is Vmax?

A

The maximum velocity the enzyme can achieve at a given enzyme concentration

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10
Q

What is the kcat equation?

A

kcat = Vmax / total Enzyme concentration

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11
Q

What value can be thought of as frequency of the reaction?

A

kcat

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12
Q

what is the measure of both binding and catalytic events?

A

kcat/Km

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13
Q

Does a larger or smaller value of kcat/Km indicate a better enzyme?

A

larger

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14
Q

What limits kcat/Km?

A

time for electron rearrangement, turnover number, and collision

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15
Q

What is the number of kcat/Km that is considered catalytic perfection?

A

10e8 - 10e9 1/(M*s)

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16
Q

Generally, efficient enzymes have (high/low) Vmax, Km, kcat, kcat/Km?

A

high Vmax, low Km, high kcat, high kcat/Km

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17
Q

With a lineweaver-burk plot equation, what is the Vmax equal to?

A

1/y-intercept

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18
Q

With a lineweaver-burk plot equation, what is the Km equal to?

A

slope/y-intercept

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19
Q

What makes an irreversible inhibitor, irreversible?

A

it covalently modifies the enzyme so that it cannot return to its active form

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20
Q

What is an example of an irreversible inhibitor?

A

Serine Protease

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21
Q

Kinetics don’t affect which kind of inhibitor?

A

irreversible

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22
Q

What are the effects of reversible inhibitors interacting with an enzyme?

A

lower overall reaction rate, reaction kinetics are changed, and the inhibitor can be released from the enzyme

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23
Q

What kind of inhibitor am I describing: the inhibitor competes with the substrate for the active site

A

competitive inhibitor

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24
Q

Which inhibitor is considered mutually exclusive?

A

competitive

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25
Q

For competitive inhibition, what occurs if [s] is much greater than [I]?

A

no inhibition is observed

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26
Q

What values do competitive inhibitors affect?

A

Km, not Vmax
(increase in Km)

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27
Q

What kind of inhibitor am I describing: inhibitor binds at a site other than the active site and changes the conformation of the enzyme

A

mixed inhibitor

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28
Q

What values do mixed inhibitors affect?

A

Vmax (decreases) and Km (increase or rarely decrease)

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29
Q

What kind of inhibitor is a noncompetitive inhibitor?

A

mixed

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30
Q

What values do noncompetitive inhibitors affect?

A

Vmax (decreases), no change in Km

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31
Q

What kind of inhibitor affects only the catalytic activity and not substrate binding?

A

Uncompetitive inhibitor

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32
Q

What values do uncompetitive inhibitors affect?

A

Km (decreases) and Vmax (decreases)

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33
Q

What kind of inhibitor is Tamiflu?

A

competitive inhibitor

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34
Q

What NSAID is irreversible inhibition of both COX-1 and COX-2?

A

Aspirin

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35
Q

What NSAID is reversible inhibition of both COX-1 and COX-2?

A

ibuprofen

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36
Q

What NSAID is selective inhibition of just COX-2?

A

Vioxx and Celebrex

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37
Q

What is the term for the sequential reaction where the order of the substrate matters?

A

Ordered

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38
Q

What is the term for the sequential reaction where it doesn’t matter which substrate goes first/the order doesn’t matter?

A

Random

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39
Q

If you have more than one substrate, is there one Km, or does each substrate have its own Km?

A

Each substrate has a distinctive Km

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40
Q

Does allosteric regulation inhibit or enhance enzyme activity?

A

It does both! Depends if it’s a positive or negative effector

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41
Q

What is the allosteric effect?

A

binding of an effector to one subunit affects the active sites of all subunits

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42
Q

What is the negative effector of PFK?

A

PEP: almost a final product of of the pathway that PFK is regulating

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43
Q

What is the positive effector of PFK?

A

ADP

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44
Q

Why is ADP the positive effector of PFK?

A

High concentration of ADP would indicate a need for ATP, which is the product of glycolysis

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45
Q

What form are the majority of natural carbohydrates in?

A

D form

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46
Q

What are the left and right symbols for D-Glucose?

A

RLRR

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47
Q

What are the left and right symbols for D-Galactose?

A

RLLR

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48
Q

Pyran is a ___ - membered ring

A

6

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49
Q

Furan is a _____ - membered ring

A

5

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50
Q

Is Beta together or opposite?

A

together

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51
Q

is Alpha together or opposite?

A

opposite

52
Q

Anomeric carbon forms a covalent bond with an alcohol - what is this called?

A

glycosidic bond

53
Q

What is a reducing sugar?

A

sugars with anomeric carbons that have not formed glycosides

54
Q

What is polymerized by glycosidic bonds?

A

carbohydrate monomers

55
Q

Sucrose make up:

A

alpha-glucose + beta-fructose

56
Q

Maltose make up:

A

alpha-glucose + beta-glucose

57
Q

Lactose make up:

A

beta-galactose + beta-glucose

58
Q

Isomaltose make up:

A

alpha-glucose + alpha-glucose

59
Q

Cellobiose make up:

A

beta-glucose + beta-glucose

60
Q

Which polysaccharide has a linear make up?

A

cellulose

61
Q

Which polysaccharide has a branched make up?

A

starch

62
Q

Which polysaccharide has a highly branched make up?

A

glycogen

63
Q

What cleaves glycogen?

A

glycogen phosphorylase / glycogen debranching enzyme

64
Q

What is a glycoprotein?

A

protein that has some type of carbohydrate attached to it

65
Q

What kind of carbohydrate is attached to a glycoprotein?

A

oligosaccharide

66
Q

At what amino acids are the oligosaccharides attached to the glycoprotein?

A

Asn (N-glycosidic), Ser (O-glycosidic), or Thr (O-glycosidic)

67
Q

What is the purpose of the oligosaccharide added to the glycoprotein

A

helps stabilize the protein and the helps the organism recognize its own protein vs. foreign proteins

68
Q

Which fatty acids have double bonds?

A

unsaturated

69
Q

Which fatty acids don’t have any double bonds?

A

saturated

70
Q

What is the saturated 18 C fatty acid

A

stearic acid CH3(CH2)16COOH

71
Q

What is the monounsaturated 18 C fatty acid

A

oleic acid CH3(CH2)7CH=CH(CH2)7COOH

72
Q

What is the polyunsaturated 18 C fatty acid with two double bonds?

A

linoleic acid CH3(CH2)4CH=CHCH2CH=CH(CH2)7COOH

73
Q

What is the polyunsaturated 18C fatty acid with three double bonds?

A

linolenic acid CH3CH2CH=CHCH2CH=CHCH2CH=CH(CH2)7COOH

74
Q

What is the common name for 18:1n9, trans?

A

Elaidic Acid

75
Q

What causes trans unstaturation?

A

hydrogenation

76
Q

What makes omega 6 and omega 3 fatty acids “essential”

A

our body needs them, but cannot make them so we must take them from food

77
Q

What is the 12 C saturated fatty acid called?

A

Lauric Acid

78
Q

What is the 14 C saturated fatty acid called?

A

Myristic Acid

79
Q

What is the 16 C saturated fatty acid called?

A

Palmitic Acid

80
Q

What is a triacylglycerol?

A

3 fatty acids on a glycerol backbone

81
Q

The more double bonds, the ________ the melting point

A

lower

82
Q

The longer the acyl chain, the ________ the melting point

A

higher

83
Q

What are the 4 kinds of membrane bilayers?

A

glycerophospholipids, sphingomyelins, cholesterol, and isoprenoids

84
Q

What is the make up of a glycerophospholipid?

A

glycerol-3-phosphate + 2 fatty acids

85
Q

What is a sphingosine?

A

18 carbon amino alcohol

86
Q

What is the make up of a ceramide?

A

sphingosine + N-acyl fatty acid

87
Q

What is the make up of a sphingomyelin?

A

ceramide + phosphoryl head group

88
Q

What is the make up of a cerebroside?

A

ceramide + single sugar head group

89
Q

What is the make up of a ganglioside?

A

ceramide + oligosaccharides (including sialic acid)

90
Q

What is Tamiflu an analog of?

A

Sialic acid

91
Q

What is sterol’s make up?

A

3 cyclohexanes and 1 cyclopentane

92
Q

Which vitamins are isoprenoids?

A

A, D, and K

93
Q

Vitamins A, D, and K are _______ because of their isoprenoid nature

A

fat soluble

94
Q

What is the outer leaflet of the membrane composed of?

A

sphingolipids and phosphatidyl choline

95
Q

What is the inner leaflet of the membrane composed of?

A

phosphatidyl serine

96
Q

How are the inner and outer leaflets of the membrane’s distinct compositions maintained?

A

it is thermodynamically unfavorable to flip flop

97
Q

What enzyme allows the outer and inner leaflets to flip flop?

A

flippases (or translocases)

98
Q

What is another term for the flip flop of inner and outer leaflets?

A

transverse diffusion

99
Q

What is the more common type of switching in the membrane?

A

lateral diffusion

100
Q

What kind of diffusion is the reason the membrane is so flexible?

A

Lateral Diffusion

101
Q

Membranes are _________ (structure - wise)

A

dynamic and fluid

102
Q

What is the main source of energy in the body?

A

oxidation of carbons in carbohydrates

103
Q

All reactions in vivo occur with a net ________ in free energy

A

decrease

104
Q

Are metabolic pathways reversible?

A

No, it is thermodynamically unfavorable to do so

105
Q

What is the first step of every metabolic pathway called and what is unique about it?

A

First committed step, Delta G of this step must be negative

106
Q

What is the catabolic pathway of glycolysis?

A

gluconeogensis

107
Q

What are used as energy currency in the cell?

A

reduced cofactors

108
Q

Reduced cofactors are produced as a result of what?

A

catabolic activities

109
Q

Where do glycosidic bonds have to take place?

A

at anomeric carbons

110
Q

What kind of bonds are very unstable/high energy and are therefore favorable to break?

A

phosphoanhydride

111
Q

What are the results of the breaking of phosphoanhydride bonds?

A

more resonance stabilization, more solvation in water, and less ionic repulsion

112
Q

Hydrolysis of _________ bonds also releases a large amount of free energy and is therefore a favorable reaction.

A

thioester

113
Q

What is the oxidized form of NAD?

A

NAD+

114
Q

What is the reduced form of NAD?

A

NADH

115
Q

What is the oxidized form of FAD?

A

FAD

116
Q

What is the reduced form of FAD?

A

FADH2

117
Q

What is the oxidized form of Q?

A

Q

118
Q

What is the reduced form of Q?

A

QH2

119
Q

Which reduced cofactor accepts hydrogen as an element?

A

FAD and Q

120
Q

Which reduced cofactor accepts Hydride ion?

A

NAD

121
Q

What coenzyme can carry electrons in the membrane?

A

coenzyme Q

122
Q

What is the tendency of a substrate to accept electrons/to become reduced?

A

reduction potential

123
Q

These are the major functions of which organelle: citric acid cycle, electron transport and oxidative phosphorylation, fatty acid oxidation, and amino acid breakdown

A

mitochondrion

124
Q

These are the major functions of which organelle: glycolysis, pentose phosphate pathway, fatty acid biosynthesis, and many reactions of gluconeogenesis

A

cytosol

125
Q

These are the major functions of which organelle: DNA replication and transcription, RNA processing

A

nucleus

CHM 432 (4 decks)

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