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Foundations of Medicine > Skildum/ Prunuske Week 1 > Flashcards

Skildum/ Prunuske Week 1 Flashcards

1
Q

Which are the nonpolar, aliphatic amino acids?

A 
Glycine (G, R= H)
Alanine (A, R= CH3)
Proline (P, R= ring structure)
Valine (V, R= CH with 2 CH3 groups)
Leucine (L, R= CH2-CH with 2 CH3 groups)
Isoleucine (I, R= C bound to a CH3 and CH2-CH3)
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2
Q

Which are the aromatic amino acids?

A

Phenylalanine (F, R= Ch2-benzene)
Tyrosine (Y, R= CH2- benzene with para OH)
Tryptophan (W, R= big structure with 2 rings)

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3
Q

Which are the polar, uncharged amino acids?

A

Asparagine (N, R= CH2- C=O-NH2)
Glutamine (Q, R= CH2-CH2-C=O-NH2)
Serine (S, R=CH2OH)
Threonine (T, R= CH bonded to OH and CH3)

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4
Q

Which are the sulfur containing amino acids?

A

Methionine (M, R= CH2-CH2-S-CH3)

Cysteine (C, R= CH2-SH)

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5
Q

Which are the negatively charged (acidic) amino acids?

A

Aspartate (D, R= CH2, COO-)

Glutamate (E, R= CH2-CH2-COO-)

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6
Q

Which are the positively charged (basic) amino acids?

A

Arginine (R, R= CH2-CH2-CH2-NH-C=NH2+ and NH2 on last carbon
Lysine (K, R= CH2-CH2-CH2-CH2-NH3+)
Histidine (H, R= CH2- ring structure)

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7
Q

What is a peptide bond and how is it formed?

A

bond in amino acids between carbonyl carbon and nitrogen

-formed through dehydration reaction (releases H2O)

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8
Q

What are the 2 main structures in secondary proteins?

A

Alpha helix- R groups stick on outside

beta sheets- R groups stick up and down

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9
Q

What is Creutzfeldt Jakob’s disease caused by?

A

prion disease, increases in protein beta sheets which leads to amyloid fibers
Normal = PrP^c
Abnormal = PrP^sc

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10
Q

Where does ubiquitin tag bring misfolded proteins?

A

To the proteasome to be destroyed

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11
Q

What are the components of hemoglobin?

A

2 beta and 2 alpha subunits

Cooperatively binds oxygen (sigmoidal curve)

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12
Q

What are hemoglobin T and R states?

A

T state- promoted by 2,3-BPG (allosteric modulator) promotes O2 dissociation
R state- relaxed, easier for O2 to bind

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13
Q

What is the blood test to test for diabetes? (glycosylation on hemoglobin)

A

HbA1C

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14
Q

The base pair mutation of what to what amino acid causes sickle cell anemia?

A

From glutamate (negatively charge) to valine (nonpolar) on position 6 of beta subunit

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15
Q 
What do these problems with Hb mean?
HbS
HbSS
HbAA
HbSA
HbC
A 
HbS- glu6val, sickle cell 
HbSS- alpha 2 beta 2^s- sickle cell 
HbAA- alpha2 beta 2^a normal
HbSA- sickle cell trait 
HbC- Glu6Lysine -lysine in the spot of glutamate
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16
Q

What is thalassemia?

A

altered ratio of alpha beta hemoglobin, usually 1 is not produced

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17
Q

What is deltaS in the Gibbs free energy equation and what does increase or decrease mean?

A

Entropy.
deltaS > 0 is order decreasing (more randomness)
deltaS < 0 is order increasing (less randomness)

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18
Q

What does it mean if the Michaelis-Menten constant (Km) decreases?:

A

Takes less concentration for enzyme to reach Vmax so:

The enzyme is more active

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19
Q

What is a competitive inhibitor and does Km or Vmax change?

A

It competes at substrate binding sites

-increases Km but does not change Vmax

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20
Q

What is a noncompetitive inhibitor and does Km or Vmax change?

A

Molecules which bind an enzyme and inhibit its activity without inhibiting substrate binding (ex: suicide inhibitors)
-decreases Vmax but does not change Km

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21
Q

What is an allosteric inhibitor?

A

a molecule that binds an enzyme away from active substrate binding site and causes conformational change to prevent substrate binding

  • cannot be described by Michaelis- Menten
  • hyperbolic to sigmoidal curve)
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22
Q

Why do people with sickle cell have jaundice?

A

Sickle red blood cells turnover faster than normal RBCs

-heme breaks down into bilirubin and liver is overwhelmed–> causes discoloration

23
Q

What are treatments for sickle cell?

A

only cure is a bone marrow transplant

  • Hydroxyurea- drug that increases production of fetal (gamma) Hb subunits
  • blood transfulsion
24
Q

What are the oxidation/ reduction cofactors?

A

NADH, NADPH, PAD, metals, ascorbic acid

25
Q

What are the activation transfer reaction cofactors?

A

TPP, Biotin, Lipoate, PLP, Cobalamin, Coenzyme A

26
Q

What is the difference between an apoenzyme and holoenzyme?

A

An apoenzyme needs to be bound by a cofactor and a holoenzyme is functional
-the apoenzyme cannot bind the substrates transition state

27
Q

What is it called when a cofactor binds permanently to its enzyme?

A

prosthetic group, ex) FAD binding succinate dehydrogenase

28
Q

What is the reusable cofactor for alcohol dehydrogenase?

A

NADH

enzyme oxidizes ethanol to acetaldehyde

29
Q

What are the 3 functions of redox reactions?

A

fuel oxidation (ex: succinate dehydrogenase)
detoxification (ex: alcohol dehydrogenase)
biosynthesis (ex: HMG CoA reductase)

30
Q

Which enzyme converts pyruvate + NADH –> lactate + NAD+

A

lactate dehydrogenase

31
Q

What is niacin used for and where is it found?

A

Dietary precursor for NADH and NADPH

Found in meat, whole grains, and fortified cereals

32
Q

What is niacin deficiency?

A

Pellagra

33
Q

What are the symptoms of pellagra?

A

3Ds - dermatitis, diarrhea, and dementia (also glossitis- bright red and smooth tongue)

34
Q

What is the dietary precursor for FAD and FMN?

A

riboflavin (vitamin B2)

35
Q

What is riboflavin (vitamin B2) found in?

A

eggs, milk, organ meats, legumes, mushrooms

36
Q

What does riboflavin deficiency cause?

A

cheiosis (sores at corners of mouth), glossitis, keratitis, seborrheic dermatitis, anemia (fewer RBCs but they look normal)

37
Q

How is riboflavin deficiency diagnosed?

A

Erythrocyte glutathione reductase assay

  • collect and lyse blood, incubate with substrates (NADPH, gludathione) and +/- extra FAD
  • NADPH absorbs light at 340nm and NADP+ is lower- use to compare ratio before and after more FAD was added
  • > 1.4 indicates riboflavin deficiency
38
Q

What are the 2 functions of ascorbic acid (vitamin C)?

A

1) redox cofactor for hydroxylase enzymes in collagen synthesis, neurotransmitter synthesis, and oxygen sensing
2) non-enzymatic antioxidant

39
Q

What is the deficiency in ascorbic acid (vitamin C) called? What are the symptoms?

A

Scurvy

  • Slow wound healing, irritability/ apathy, anemia, enlarged junctions between ribs, petichiae (rash with bumps)
  • x-ray has white plate at ends of bones
40
Q

What metals are used in redox reactions? And what are their basic features?

A

iron, cobalt, copper, manganese, molybdenum

-need 2 stable oxidation states

41
Q

What are the main functions of pyruvate dehydrogenase?

A

Regulates glycolytic substrate oxidation in mitochondria

-converts pyruvate to acetyl CoA

42
Q

What main functions are associated with TPP, NAD+ and FAD, lipoate and CoASH?

A

TPP = decarboxylation
NAD+ and FAD = reduction and oxidation
lipoate and CoASH = transfer acyl groups

43
Q

What is thiamine found in? What causes deficiency?

A
  • meat, legumes, whole grains, cereals

- Deficiency from malnutrition, alcoholism, monotonous diet

44
Q

What 3 conditions are caused by thiamine deficiency?

A

Beri beri- “I can’t I can’t” headache, malaise, peripheral neuropathy, and heart failure
Wernike encephalopathy- confusion, mental status changes, abnormal eye movements, ataxia
Karsokoff psychosis- amnesia and confabulation

45
Q

What enzymes is biotin a cofactor for?

A

acetyl CoA carboxylase (FA synthesis)
pyruvate carboxylase (gluconeogenesis)
propionyl CoA carboxylase (branched chain FA metabolism)
methylcrotinyl CoA carboxylase (branched chain amino acid metabolism)

46
Q

What symptoms are from biotin deficiency?

A

Rare, but scaly dermatitis, thinning hair, and alopecia

47
Q

What protein in raw egg whites binds biotin permanently and can cause deficiency?

A

avidin

48
Q

What is the cofactor pyridoxal phosphate (PLP) used for?

A
  • enzymes that metabolize amino acids

- ex) transaminases

49
Q

What is pyridoxal phosphate deficiency?

A

in infants causes seizures, diarrhea, anemia
in adults causes peripheral neuropathy
-Diagnose by measuring erythrocyte transaminase activity with and without exogenous PLP

50
Q

What is antiquitin deficiency (PDE)?

A

epilepsy caused by sequestration of PLP so not available

in infants

51
Q

What is cobalamin (vitamin B12) used for?

A

to transfer and rearrange methyl groups

-2 forms: deoxyadenosine cobalamin and methylcobalamin

52
Q

Where can cobalamin be found in diet?

A

in bacteria

53
Q

What are the symptoms of cobalamin (vitamin B12) deficiency?

How is it diagnosed?

A

pernicious anemia, megaloblastic anemia, weakness, fatigue, seizures, sensory deficits
Diagnose- blood smear, methylmalonic acid in blood and urine

Foundations of Medicine (7 decks)

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