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Cell Biology Term 1 > Proteins & Enzymes > Flashcards

Proteins & Enzymes Flashcards

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1
Q

What makes an amino acid Essential?

A

It cannot be synthesized and must be obtained from the diet

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2
Q

List the essential Amino Acids

A
  • Histidine
  • Methionine
  • Threonine
  • Valine
  • Isoleucine
  • Phenylalanine
  • Leucine
  • Lysine
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3
Q

What is an aliphatic compound?

A

=Non-aromatic

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4
Q

Where are AA’s with non-polar side chains commonly located?

A
  • Interior of proteins which reside in an aqueous environment
  • The exterior of proteins that reside in a cell membrane
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5
Q

Which amino acid has a polar uncharged side chain and is found in the active site of many enzymes?

A

Cysteine (-SH)

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6
Q

What mutation is present in the DNA of patients with Sickle Cell Anemia?

A
  • Point mutation
  • At position 6 in Hemoglobin chain
  • Glutamate is replaced by valine
  • Beta subunits of Hg polymerize inside of RBC’s distorting the shape to resemble a sickle
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7
Q

Why does the gene for sickle cell persist?

A
  • Life cycle of RBC’s in carriers is less than normal (120 days)
  • life cycle of malaria parasite is 120 days, so not enough time to reproduce
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8
Q

What stereoisomer is the most prevalent in life on Earth?

A

L-isomers

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9
Q

What is the average pH of arterial blood in humans?

A

7.35-7.45

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10
Q

Disease of which organs can disrupt pH homeostasis?

A
  • Lungs

- Kidneys

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11
Q

What molecular interaction stabilize the 3’ structure of proteins?

A
  • Disulfide bonds
  • Hydrophobic interactions
  • Hydrogen bonds
  • Ionic bonds
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12
Q

What protein is involved in protein folding quality control?

A

Chaperones

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13
Q

What organelle is involved in maintaining proteostasis?

A

Proteasome

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14
Q

Contrast Globular vs. Fibrous proteins.

A

Globular: Round to ovoid. Have active sites. Transporters and enzymes.

Fibrous: Long rods. Structural proteins.

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15
Q

What is the molecular cause of Alzheimer’s disease?

A
  • Amyloid Precursor Protein is cleaved
  • Small portion of Precursor is released
  • if not degraded, forms Beta sheets and stick together
  • Accumulate and form Amyloid plaques
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16
Q

What is the most common prion disease in humans?

A

Creutzfeldt-Jakob Disease

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17
Q

When is hemoglobin in its T (Taught) state?

A

When it is deoxygenated

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18
Q

When is hemoglobin in its R (Relaxed) state?

A

When it is oxygenated

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19
Q

Which state of hemoglobin has a higher affinity for O2?

A

R

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20
Q

In which direction does the Bohr Effect shift the oxygen binding curve?

A

To the right

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21
Q

What physiological condition causes the Bohr Effect?

A

Low blood pH

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22
Q

In which direction does 2,3-BPG shift the oxygen binding curve?

A

To the right

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23
Q

How is 2,3-BPG produced?

A

It is an intermediate of Glycolysis

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24
Q

How many molecules of 2,3-BPG bind to a hemoglobin molecule?

A

one

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25
Q

In what direction will a decrease in temperature shift the oxygen binding curve?

A

To the left

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26
Q

How does hemoglobin become glycosylated? What is high levels of glycosylated hemoglobin a sign of?

A
  • when red blood cells are in a solution with a high concentration of glucose
  • Diabetes
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27
Q

What is ascorbate (vitamin C) important for?

A
  • it is required for the post-translational modification of collagen
  • used for hydroxylation of proline and lysine
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28
Q

What disease results from vitamin C deficiency?

A

Scurvy

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29
Q

Which molecule binds oxygen more tightly, myoglobin or hemoglobin?

A

Myoglobin

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30
Q

Why does blood become acidotic during hypoxia or ischemia?

A

The energy production is mostly being done by glycolysis, producing lactic acid

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31
Q

In what state (T/R) does 2,3-BPG stabilize in hemoglobin?

A

T

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32
Q

What are the letters that represent glycosylated hemoglobin?

A

HbA1c

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33
Q

In what state (T/R) does carbon monoxide stabilize in hemoglobin?

A

R

34
Q

what disease does Hb C represent?

A

hemolytic anemia

35
Q

What are the symptoms of Hb SC?

A
  • Decreased solubility in deoxy form
  • polymer formation
  • vascular occlusion
  • Pain
36
Q

What is the basic repetitive amino acid sequence of the alpha-chain of collagen?

A

Gly-X-Y

37
Q

How do we know when a generic drug is a protease inhibitor?

A

The generic name ends in -navir

38
Q

What is the turnover number?

A

The number of substrates turned into product divided by unit time

39
Q

High turnover numbers are associated with reactions in which Delta-G is negative or positive?

A

Negative

40
Q

Why do allosteric enzymes show a sigmoidal reaction curve?

A

The substrate alters the enzyme conformation to increase activity, though sometimes binding can decrease activity

41
Q

What is the significance of Km?

A
  • it is the concentration of substrate at which an enzyme has reached one half of its maximum velocity
  • lower Km = higher affinity to enzyme
42
Q

What does it mean for a reaction velocity to be zero order?

A

the velocity of the reaction is constant and independent of substrate concentration

43
Q

What does it mean for a a reaction velocity to be first order?

A

The velocity of the reaction is proportional to the the substrate concentration

44
Q

Illustrate the difference between first order zero order kinetics with two clinical examples:

A
  1. Metabolism of aspirin. Low dose = 1st order, high dose = zero order.
  2. Alcohol intoxication. Zero order kinetics regardless of substrate concentration
45
Q

What are isoenzymes/isozymes?

A

Enzymes that have a different sequence but still catalyze the same reaction.

46
Q

What kind of enzymes do drugs that end in -navir inhibit?

A

Protease

47
Q

Where is cholesterol synthesized in the cell?

A

Smooth ER

48
Q

Analysis of a patient’s blood showed elevated levels of Aspartate Amino Transferase/Alanine Amino Transferase. You suspect that pathology is in which organ?

A

Liver

49
Q

Glucokinase vs. Hexokinase?

A
  • glucokinase: in liver/pancreas. High Km. High Vmax.

- Hexokinase: All tissues. Low Km. Low Vmax.

50
Q

A competitive inhibitor will alter an enzyme’s ________ but not its ________.

A

Km, Vmax

51
Q

What kind of drugs are competitive inhibitors of HMG-CoA reductase?

A

Statins

52
Q

What do statins do for us?

A

Reduce cholesterol

53
Q

A noncompetitive inhibitor will alter an enzyme’s ________ but not its ________.

A

Vmax, Km

54
Q

What’s an example of a drug that is a noncompetitive (irreversible) inhibitor?

A

Aspirin

55
Q

How can allosteric activators alter enzyme kinetics?

A
  • Alter Km

- Alter Vmax

56
Q

What serum protein levels increase after Liver damage?

A

ALT/AST

57
Q

What serum protein levels increase after Heart muscle damage?

A
  • MB Creatine phosphokinase (CPK)
  • Cardiac Troponin (Specific and most common)
  • Lactate dehydrogenase (LDH) -not very Specific
58
Q

What serum protein levels increase after skeletal muscle damage?

A

MM creatine phosphokinase

59
Q

What serum protein levels increase after Brain damage?

A

BB Creatine Phosphokinase

60
Q

What is the most specific and commonly used serum marker for monitoring cardiac muscle damage?

A

Cardiac Troponin

61
Q

What are the 3 ways in which enzymes can be activated or inactivated?

A

1) Proteolysis
2) Allosteric changes
3) Covalent modification

62
Q

What is an example of an enzyme that is activated by proteolysis?

A

Angiotensinogen–>Angiotensin I–>Angiotensin II

63
Q

What enzyme converts angiotensin I to angiotensin II?

A

Angiotensin Converting Enzyme (ACE)

64
Q

What enzyme converts Angiotensinogen to angiotensin I?

A

Renin

65
Q

What does Glycogen Phosphorylase do?

A

Converts Glycogen to Glucose-1-Phosphate

66
Q

What are the activators of Glycogen Phosphorylase?

A

AMP/ADP-CA2+-Glucagon-Epinephrine

67
Q

What are the inhibitors of Glycogen Phosphorylase?

A
  • ATP
  • Glucose-6-Phosphate
  • Insulin
68
Q

How do you treat a patient who is overdosed on beta blockers?

A

Glucagon

69
Q

What does G-alpha-s protein do?

A

Stimulatory G protein that increases Adenyl cyclase activity

70
Q

What does G-alhpa-i do?

A

Inhibitory G protein that inhibits Anenyl Cyclase activity

71
Q

What does G-alpha-q protein do?

A

Queer G protein that activates phospholipase C (increases IP3 and Calcium)

72
Q

What does adenyl cyclase do?

A

converts ATP to cAMP

73
Q

What are the most common second messengers?

A
  • cAMP
  • cGMP
  • CA2+
  • IP3
  • DAG
74
Q

What second messenger activates Protein Kinase A (PKA)?

A

cAMP

75
Q

What second messenger regulates Protein kinase G (PKG)?

A

cGMP

76
Q

What second messenger regulates CaM Kinase?

A

Ca2+

77
Q 
Inhibition of cyclooxygenase by Aspirin is due to:
A.  Carboxylation
B.  Acetylation
C.  Glycosylation
D.  Hydroxylation
E.  Phosphorylation
A

B. Acetylation

78
Q

Blood clotting pathway and RAAAs (Renin-Angiotensin-Aldosterone-ADH) pathway are activated by ______

A

Proteolysis

79
Q

Wat type of glucose transporter is SLGT?

A

A sodium-glucose symporter. Transports glucose into cells from intestine and renal tubules

80
Q

What type of glucose transporter is GLUT 2?

A

A channel for facilitated diffusion of glucose

81
Q

What is Nitric Oxide’s amino acid precursor?

A

Arginine

82
Q

What is a funciton of Nitric Oxide?

A

relax smooth muscle surrounding blood vessels (vasodilator)

Cell Biology Term 1 (7 decks)

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