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BCH 4053 > Exam #3 Material > Flashcards

Exam #3 Material Flashcards

1
Q

In transforming the Michaelis-Menten equation into a straight line equation, y = mx+b, the Lineweaver-Burk double reciprocal plot, which is not a true representation?

A

X-intercept is 1/Km

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2
Q

The Km can be considered to be the same as the disassociation constant Kd for E+S binding if:

A

k2 &laquo_space;k-1

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3
Q

Fetal hemoglobin (Hb F) has an intrinsically greater affinity for O2 than adult hemoglobin (Hb A) because:

A

Hb F has a diminished capacity to bind BPG compared to Hb A.

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4
Q

The cause of cell sickling in sickle cell anemia is…

A

Oligomerization of deoxy-Hb S into long, chain-like fibers.

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5
Q

Name the tropism being described:

A)
Carbon source: CO2 energy source: light

B) Carbon source: CO2
energy source: redox reactions

C) Carbon source: organic compounds energy source: light

D) Carbon source: Organic compounds energy source: redox reactions

A

A) Photoautotroph

2) Chemoautotroph
3) Photoheterotroph
4) Chemoheterotroph

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6
Q

What is a characteristic difference between FAD and NAD+?

A

NAD+ transfers two electrons while FAD can transfer one or two.

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7
Q

For the first five steps of glycolysis, the appropriate sequence of the enzymes is:

A. Phosphofructokinase-1 (PFK-1)

B. Hexokinase /glucokinase

C. Fructose biphosphate adolase

D. Phosphoglucoisomerase

E. Triose Phosphate isomerase (TPI)

A 
D
B
A
C
E
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8
Q

The step that commits glucose to glycolysis is catalyzed by:

A

Phosphofructokinase

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9
Q

In the second half of the glycolytic pathway, __ ATP molecules are produced and with the offset of __ ATPs consumed in the first half, the net yield is __ ATPs per glucose

A

4, 2, 2

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10
Q

Which of the following amino acids would NOT provide a nucleophilic center for covalent catalysis?

Cysteine
Serine
Alanine
Lysine
Glutamic Acid
A

Alanine

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11
Q

In the chymotrypsin reaction mechanism, ___ is involved in covalent catalysis.

A

Ser 195

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12
Q

In the catalytic triad common to many serine proteases, ___ increases the basicity of ___, thus allowing deprotonation of ___ to serve as a nucleophile.

A

Asp-His-Ser

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13
Q

Which of the following is false regarding serine proteases?

A) they employ metal ion catalysis
B) They contain a catalytic triad of His, Ser, and Asp residues
C) They cleave simple organic ester bonds near larger residues
D) They employ general acid-base catalysis

A

A) they employ metal ion catalysis

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14
Q

An enzyme that has the maximum activity at pH 4 may indicate the involve of ___ amino aid in acid-base catalysis.

A

Glutamic acid

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15
Q

All are characteristics of allosteric enzymes except:

A) They obey Michaelis-Menton kinetics
B) Effectors may show stimulatory or inhibitory activity.
C) They have multiple subunits
D) The regulatory effect by altering conformation and interaction of subunits
E) Binding one subunit impacts the binding of substrate to other subunits

A

A) They obey Michaelis-Menton kinetics

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16
Q

Proinsulin is converted to insulin by:

A

Proteolytic excision of a specific peptide.

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17
Q

Heme is a porphyrin prosthetic group that coordinates __ at four positions.

A

Fe 2+

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18
Q

Which of the following is generally true for catabolism, but not anabolism?

A

A net production of energy results from degradation of large molecules.

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19
Q

All are coenzymes with an adenine nucleotide portion except:

A) NADH
B) FADH2
C) Coenzyme A
D) ATP
E) FMNH2
A

E) FMNH2

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20
Q

What does not contribute to a large negative delta G of ATP?

A

All of the above contribute:
Phosphate hydrolysis

Resonance
Stabilization

Electrostatic repulsion

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21
Q

__ can bypass the regulatory step at 3-FTK to enter glycolysis which may be a contributing factor to obesity.

A

Fructose

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22
Q

All are allosteric regulators of phosphofructokinase-1 except:

A

glucose-6-phosphate by inhibition

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23
Q

All are true for 2,3-bisphosphoglycerate (2,3-BPG) except:

A

A kinase converts 2,3-BPG to 3-phosphoglycerate

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24
Q

Which step in metabolism produces a 3-C aldose and a 3-C ketose from a 6-C sugar?

A

Fructose bisphosphate aldolase

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25
Q

In alcohol fermentation from glucose, the two oxidation-reduction reactions are catalyzed by:

A

Glyceraldehyde-3-phosphate dehydrogenase and alcohol dehydrogenase

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26
Q

Pyruvate dehydrogenase is a multi-enzyme complex homologous to:

A

Alpha-ketoglutarate dehydrogenase

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27
Q

Order the coenzymes according to their involvement in the pyruvate dehydrogenase complex:

A) NAD+
B) CoA-SH
C) TPP
D) Lipoate (lipoamide)
E) [FAD]
A

C D B E A

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28
Q

Allosteric inhibitors of isocitrate dehydrogenase include __ and __, wheras __ acts as an allosteric activator, __ the Km for isocitrate.

A

ATP; NADH; ADP; lowering

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29
Q

List the names of 5 enzymes that are regulated in the glycolysis and TCA cycle.

A

__

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30
Q

All are true statements for the glyoxylate pathway except:

A

Glyoxysomes contain all of the enzymes for the glyoxylate cycle.

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31
Q

Name two investigators who were awarded the Nobel Prize for their work on the structures of hemoglobin and myoglobin.

A

Perutz, Kendrew

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32
Q

What is the Michaelis-Menton equation formula?

A

Vo= Vmax [S] / Km + [S]

Where Km = (k-1 + k2)/k1

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33
Q

Km is often interpreted as…

A

The affinity of enzyme for substrate.

Km is similar to the dissociation constant (Kd) for the ES complex. If k-1&raquo_space; k2, then Km ~ Kd

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34
Q

Kcat =

A

Kcat = Vmax / [E] total

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35
Q

Catalytic efficiency =

A

Catalytic efficiency = Kcat/Km

Where Kcat = Vmax / [E] total and Km = (k-1 + k2)/k1

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36
Q

Rates of enzyme catalyzed reactions generally ___ with temperature, however, at temps above 50-60 deg. celsius, enzymes show a ___ in activity.

A

Increase; decline.

Enzymes typically double in rate for every 10 deg. celsius rise in temperature.

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37
Q

As [S] increases, kinetic behavior changes from 1st order to ___ order kinetics.

A

Zero

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38
Q

The Lineweaver-Burk plot equation is the Michaelis-Menton rearranged to make it linear. The equation is…

A

(1/vo) = (Km/Vmax) (1/[S]) + (1/Vmax)

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39
Q

___-___ plot solves the problem of uneven sampling.

A

Hanes-Woolf

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40
Q

The three main categories of reversible enzyme reactions are:

A

Competitive
Uncompetitive
Mixed (Noncompetitive): inhibitor binds to sites on E that influence both S binding and catalysis

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41
Q

Explain the double displacement (ping pong) mechanism.

A

The first substrate is converted to product before the second substrate adds.

This requires two forms of “free” enzyme

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42
Q

Catalytic power is the ratio of the enzyme…

A

catalyzed rate / uncatalyzed rate

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43
Q

Enzymes often have cofactors such as ___, ___, ___, and ___.

A

Metal ions, coenzymes, cosubstrates, and prosthetic groups.

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44
Q

In enzymes, an apoenzyme refers to the ___ form ___ the cofactor.

A

Inactive form; without

45
Q

In enzymes, a holoenzyme refers to the ___ form ___ a cofactor.

A

Active; with

46
Q

Enzymes catalyze reactions by ____ and ___ the activation energy of the reaction.

A

Stabilizing the transition state; lowering

47
Q

How does destabilization of ES affect enzyme catalysis?

A

Raising the energy of ES raises the catalyzed rate.

This is accomplished by a loss of entropy due to formation of ES and destabilization of ES by strain, distortion, and desolvation.

48
Q

Catalysis via preferential transition state binding is when…

A

Some enzymes bind the transition state of the reaction with greater affinity than its substrates or products.

Thus, enzymes may mechanically strain substrates to TS geometry.

49
Q

A transition state analog is a stable molecule that is chemically ___ to the transition state. They often make good ___, since they can make ideal enzyme inhibitors.

A

Similar; drugs

50
Q

Specific acid-base catalysis is when…

A

H+ or OH- is transferred FROM solution

51
Q

General acid-base catalysis is when…

A

H+ or OH- is generated in the transition state

52
Q

___ is often a general acid or base because its side chain is near pKa of 7.

A

Histidine

53
Q

Metal ions participate in catalysis in three major ways:

A
  • Binding to substrates to orient them
  • Mediating redox reactions through reversible changes in oxidation state
  • Electrostatically stabilizing or shielding negative charge
54
Q

Enzymes facilitate formation of near-attack conformations

Near-attack conformations (NACs) are ___ to reaction transition states. In NACs, reacting atoms are in Van der Waals contact and at an angle resembling the bond to be formed in the transition state.

A

Precursors

55
Q

Low barrier hydrogen bonds (LBHB) stabilize the ___ ___. They can be used to lower the ___ barrier.

A

Transition state; activation

56
Q

Quantum Mechanical Tunneling

Tunneling provides a path “around” the usual ___ of activation for steps in chemical reactions. Tunneling probably contributes to most ___ transfer reactions.

A

energy; hydrogen

57
Q

The most well characterized serine proteases are ___, ___, and ___.

A

Chymotrypsin; trypsin; elastase

58
Q

Serine is part of a “catalytic triad” composed of ___, ___, ___.

A

Ser, His, Asp

59
Q

Serine proteases differ in their specialties:

Trypsin: Cleaves after ___ amino acid

Chymotrypsin: Cleaves after ___ amino acid

Elastase: Cleaves after ___ ___ residues.

A

Basic; aromatic; small neutral

60
Q

Serine proteases serve as enzymes that ___. Serine serves as the ___ amino acid at the enzyme’s active site.

A

Cleave peptide bonds; nucleophilic

61
Q

Serine proteases display ___ kinetics, meaning that there are at least 2 steps.

A

Burst

62
Q

DIPF, or Diisopropylphosphofluoridate, irreversibly ___ serine proteases.

A

Inactivates

63
Q

There are three key residues for the catalytic triad, and each’s function is:
Asp-102:
His-57:
Ser-195:

A

Asp-102: functions to orient and polarize His-57

His-57: acts as a general acid base

Ser-195: forms a covalent bond with peptide to be cleaved

64
Q

The oxyanion hole is part of the enzyme that forms hydrogen bonds with the O- in the tetrahedral intermediate. It facilitates ___ of the transition state.

A

Binding

65
Q

Bovine Pancreatic Trypsin Inhibitor (BPTI) prevents trypsin synthesized in pancreas from ___ that organ. It prevents H2O from reaching the active site.

A

Digesting

66
Q

The aspartic proteases, pepsin, chymosin, cathepsin D, renin and HIV-1 protease all involve two __ residues at the active site. These two residues work together as general acid-base catalysts.

A

Asp

67
Q

Enzymes are regulated in multiple ways, such as:

A
  • Genetic regulation of enzyme synthesis and decay
  • Allosteric regulation
  • Covalent modification
  • Availability of substrates and cofactors
68
Q

Typical enzymes show hyperbolic increase in velocity with respect to [S], while cooperative enzymes exhibit the ___ curve.

A

Sigmoid

69
Q

Positive cooperativity implies ___ binding.

A

Allosteric

70
Q

In the Monod, Wyman, and Changeux allosteric model, there are two conformational states of the enzyme: ___ and ___. Also, allosteric proteins are oligomers.

It states that S binds ___, because as it shifts the equilibrium to the R state, it opens up more S binding sites.

A

Relaxed (R); Taut (T); Cooperatively

R: has affinity for S
T: low to no affinity to S

71
Q

The sequential model for allostery (KNF) says that:

  • Protein is ___.
  • Does not require all subunits to be in either the R or T state, differing with the ____ model.
  • Ligand-induced changes in one subunit lead to conformation changes in adjacent subunits.
A

Oligomeric; MWC (Monod, Wyman and Changeux)

72
Q

Covalent Modification Regulation of Enzymes:

-Enzyme activity can be regulated through reversible ___ by protein kinases.

A

Phosphorylation

73
Q

In regulation by phosphorylation, protein kinases phosphorylate ___, ___, and ___ residues in target proteins.

Kinases are often regulated by ____ control.

A

Ser, Thr, Tyr

Intrasteric

74
Q

An example of allosteric regulation is ___ ____, also called GPase.

It works by breaking down glycogen highly expressed in muscle, and can be phosphorylated at Ser 14. Phosphorylation shifts equilibrium towards R state.

Glycogen n + Pi gives Glycogen n-1 + G1P

A

Glycogen phosphorylase

75
Q

Allosteric regulators that influence the R/T equilibrium are called ___.

A

Effectors

76
Q

Allosteric regulators that influence the R/T equilibrium are called ___, which can be positive or negative.

A

Effectors

77
Q

In regulation by proteolytic activation/inactivation,

___ are inactive precursors of enzymes, and proteolytic cleavage produces the ___ product.

A

Zymogens; active

78
Q

Isozymes are enzymes with slightly different ___.

A

Subunits

79
Q

Hemoglobin is responsible for _____ in the blood, while Myoglobin is responsible for _____ in the muscle.

A

O2 transport; O2 diffusion in the muscle.

80
Q

Hemoglobin is a ___, and has 2 alpha subunits and 2 beta subunits. Myoglobin is a monomer.

A

Tetramer

81
Q

Both Hemoglobin and Myoglobin bind ___, which carriers O2.

A

Heme

82
Q

Myoglobin has ___ residues, with 8 helices named A-F. Myoglobin binds between helix ___.

A

153, E-F

83
Q

___, ___, and ___ can bind to heme groups with a much higher affinity than O2, and can cause toxicity.

A

CO, NO, and H2S

84
Q

Oxygen binding by Myoglobin is ___.

A

Hyperbolic

85
Q

When interpreting hyperbolic plots of myoglobin, the steepness of the plot indicates ___ ___.

A

higher affinity

86
Q

Hemoglobin undergoes conformational change upon binding ___.

It has two conformations, T state, in which it is ___, and R state, in which it is oxyhemoglobin.

A

O2

deoxyhemoglobin

87
Q

Hemoglobin has cooperative binding which is ____, and increases the effectiveness of O2 delivery.

Myoglobin has hyperbolic bindining.

A

Sigmoid

88
Q

Hemoglobin binds oxygen in the ___ and releases it in the ___.

A

Lungs; capillaries

89
Q

Hemoglobin effectors:

-H+ can promote ___ of oxygen from hemoglobin, called the Bohr effect. This works by a pH influence on T to R transition. (decreased pH leads to increased ___ of O2 from hemoglobin).

A

Dissociation

90
Q

Deoxy-hemoglobin has a higher affinity for H+ than ___.

A

Oxy-Hemoglobin

91
Q

CO2 also promotes the ___ of O2 from hemoglobin. Most of the CO2 is transported in the blood in the form of bicarbonate, and hydration of CO32 in tissues leads to proton production. These protons are taken up by hemoglobin as oxygen dissociates.

A

Dissociation

92
Q

___ is a negative allosteric effector of hemoglobin. When it is present, it will bind in the sigmoid curve.

A

2,3-Bisphosphoglycerate

93
Q

Fetal hemoglobin has a ___ affinity for O2 because it has a ___ affinity for BPG (bisphosphoglycerate).

A

Higher; lower

94
Q

Fetal hemoglobin has a ___ affinity for O2 because it has a ___ affinity for BPG (bisphosphoglycerate).

A

Higher; lower

95
Q

Sickle cell anemia is caused by a single amino acid ___ in hemoglobin (Glu to Val). This causes hemoglobin to form a filament.

A

Substitution

96
Q

An organism with:

Carbon source: CO2
Energy source: light

Is a…

A

Photoautotroph

97
Q

An organism with:

Carbon source: CO2
Energy source: light

Is a…

A

Photoautotroph

98
Q

An organism with:

Carbon source: CO2
Energy source: light

Is a…

A

Photoautotroph

99
Q

An organism with:

Carbon source: Organic compounds
Energy source: light

Is a…

A

Photoheterotroph

100
Q

An organism with:

Carbon source: Organic compounds
Energy source: light

Is a…

A

Photoheterotroph

101
Q

An organism with:

Carbon source: Organic compounds
Energy source: light

Is a…

A

Photoheterotroph

102
Q

An organism with:

Carbon source: Organic compounds
Energy source: light

Is a…

A

Photoheterotroph

103
Q

An organism with:

Carbon source: CO2
Energy source: redox reactions

Is a…

A

Chemoautotroph

104
Q

An organism with:

Carbon source: organic compounds
Energy source: redox reactions

Is a…

A

Chemoheterotroph

105
Q

In the cytosol, what metabolic pathways occur?

A

Glycolysis, pentose phosphate pathway, fatty acid biosynthesis, etc.

106
Q

In the mitochondria, what metabolic pathways occur?

A

TCA cycle, oxidative phosphorylation, fatty acid oxidation, amino acid breakdown

107
Q

In the smooth ER, what metabolic pathways occur?

A

Lipid and steroid biosynthesis

108
Q

Enzymes at key steps in metabolic pathways are regulated by…

1.
2.
3.

A
  1. Allosteric control- feedback inhibition, products inhibit earlier reactions
  2. Covalent modification- phosphorylation/dephosphorylation can change enzyme kinetics
  3. Genetic control- control transcription of metabolic enzymes
109
Q

Phosphocreatine is a high-energy compound used to generate ___ during intense activity. It acts as an ___ buffer.

A

ATP

BCH 4053 (5 decks)

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