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Clinical Chemistry Spring 2023 > Protein Metabolism > Flashcards

Protein Metabolism Flashcards

1
Q

Define non-essential amino acids

A

Amino acids that are produced by the body therefore they aren’t essential.

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2
Q

Define essential amino acids

A

Amino acids that cannot be produced by the body and are obtained through diet.

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3
Q

Make flash cards based on slide 2

A

Could not make while at work w/o notes

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4
Q

What are the two groups important in forming a peptide bond for an amino acid?

A

NH2 group & COOH group to form a peptide bond. Assume the R group will attach eventually.

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5
Q

List the essential amino acids

A
  1. Histidine
  2. Isoleucine
  3. Leucine
    4.Lysine
    5.Methionine
  4. Phenylalanine
    7.Threonine
    8.Tryptophan
    9.Valine
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6
Q

What are the two ionizable groups on an amino acid?

A

The Nitrogen group (NH3) and COOH group

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7
Q

If the pH is lower than the isoelectric point (pI) which group on the amino acid will have a charge?

A

The NH3 group. It’ll be a positive charge.

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8
Q

At neutral pH what group on the amino acid will have a charge?

A

Both

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9
Q

When pH is higher than the isoelectric point which group (on amino acid) will have a charge?

A

The COOH group. It’ll be a negative charge.

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10
Q

Define the isoelectric point.

A

pH at which overall net charge is neutral.

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11
Q

What are the different kinds of protein made in protein synthesis?

A
  1. Plasma proteins
  2. Intracellular proteins
  3. Structural Proteins
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12
Q

How much energy is expended in amino acid metabolism?

A

12 - 20% of total energy supply

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13
Q

Amino acids are used to create what non protein nitrogenous compounds?

A
  1. Purine
  2. Pyrimidine
  3. Porphyrins
  4. Creatine
  5. Urea
  6. Histidine
  7. Thyroxine
  8. Epi
  9. Coenzyme NAD+
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14
Q

Cysteine, glycine, serine, alanine, and threonine can all be converted to what chemical before entering the TCA cycle?

A

Pyruvate then Acetyl - CoA

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15
Q

Tryptophan and lysine are converted to what chemical before entering the TCA cycle?

A

Alpha - Ketoadipate

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16
Q

Phenylalanine, Leucine and tyrosine can be converted into what chemical to eventually enter the TCA cycle

A

Acetoacetate, then acetoacetyl - CoA and finally Acetyl - CoA

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17
Q

Tyrosine can be converted to not just acetoacetate but also what other two chemicals to contribute to the TCA cycle?

A

Fumarate or Oxaloacetate

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18
Q

Asparagine and aspartate can be converted to what two materials to contribute to the TCA cycle?

A

Oxaloacetate or Fumarate

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19
Q

Arginine, Proline, Histidine, Glutamate, and Glutamine can be converted to what chemical to be funnel into the TCA cycle?

A

Alpha - Ketoglutarate

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20
Q

Isoleucine can be converted to what two chemicals to contribute to the TCA cycle?

A

Acetyl - CoA or Succinyl CoA

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21
Q

Methionine, Isoleucine, and Valine can be converted to what chemical

A

Succinyl CoA

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22
Q

The enzyme methylmalonyl CoA mutase requires ______ to convert L-Methylmalonyl - CoA to succinyl-CoA.

A

Vitamin B12

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23
Q

What is the name of the disorder for inborn error of phenylalanine metabolism?

A

PKU, Phenylketonuria

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24
Q

What enzyme is defective in PKU?

A

Phenylalanine hydroxylase. The defective enzyme prevents conversion of phenylalanine to tyrosine.

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25
Q

In PKU the accumulation of phenylalanine and/or phenylpyruvic acid leads to…

A

Severe metabolic acidosis & neurological problems however it can be controlled by monitoring diet.

26
Q

Describe tyrosinemia

A

A disorder that leads to the accumulation of tyrosine because of the absence/defective enzyme that catabolize tyrosine in liver.

27
Q

What enzyme is effected in Type 1 Tyrosinemia?

A

Fumarylacetoactetate hydrolase

28
Q

What are some symptoms for a patient with type 1 tyrosinemia.

A
  1. Failure to thrive, jaudice, cabbage like odor, and nose bleeds
  2. Liver & kidney failure, neuropathy, and hepatic tumors
29
Q

What enzyme is effected in Type 2 tyrosinemia?

A

Deficiency of tyrosine aminotransferase

30
Q

What are some symptoms for a patient with type 2 tyrosinemia.

A

Excessive tearing, photophobia, eye pain, lesions, and mental retardation.

31
Q

What enzyme is effected in Type 3 tyrosinemia?

A

Deficiency of 4-hydroxyphenylpyruvate dioxygenase

32
Q

What are some symptoms for a patient with type 3 tyrosinemia?

A

Mild retardation, seizures, and intermittent ataxia (slurred speech, stumbling, falling, and incoordination in other words degeneration of the nervous system)

33
Q

What are other names for alkaptonuria?

A

Black urine disease or black bone disease

34
Q

What enzyme is defective in alkaptonuria?

A

Homogentisate oxidase

35
Q

What are some long term problems patients with alkaptonuria run into?

A

Kidney, prostate calculi, and heart problems

36
Q

If homogenisate oxidase is defective what will happen in the body?

A
  1. Increased homogentisic acid (HGA), its an intermediate breakdown product
  2. HGA is deposited in connective tissue, cartilage, and skin leading to darkening of skin, urine and arthritis
  3. Urine turns to black when exposed to air
  4. Patient may develop kidney, prostate calculi, and heart problems.
37
Q

Maple syrup urine disease has what defective enzyme?

A

Alpha ketoacid dehydrogenase

38
Q

The defective alpha ketoacid dehydrogenase leads to what symptoms in the body?

A
  1. Poor feeding, vomiting, lethargy, seizures, and developmental delays
  2. Urine smells like maple syrup
39
Q

What amino acids cannot be broken down in the body with maple syrup urine disease?

A

Valine, Isoleucine, and Leucine

40
Q

What enzyme is defective in isovaleric acidemia?

A

Isovaleryl-CoA dehydrogenase (IVD) enzyme

41
Q

What enzyme is unable to be broken down

42
Q

What are the two amino acids you cannot use for gluconeogenesis?

A

Leucine and lysine

43
Q

What are left over amino acids turned into ?

A

Ammonia then goes through the urea cycle

44
Q

What is the rate limiting enzyme in the urea cycle?

A

Carbamoyl phosphate synthetase

45
Q

Where is urea reabsorbed in the nephron?

A

Distal tubule

46
Q

How much urea is excreted?

47
Q

What is used to transport citrulline out and ornithine in the mitochondria?

A

A symporter

48
Q

Define zwitterion

A

Amino acid with an equal number of opposing charge

49
Q

What pH is there ionizable groups?

50
Q

A cation has a pH ______ pI.

51
Q

A anion has a pH ____ pI

A

greater than

52
Q

What organ is involved in plasma protein synthesis and secretion?

A

Liver with albumin being the most abundant protein.

53
Q

What makes intracellular proteins?

A

Cytoplasmic free ribosomes

54
Q

List non protein nitrogen compound synthesis

A

Purine, Pyrimidine, porphyrins, creatine, Urea, Hisitidine, Thyroxine, Epi, Coenzyme NAD+

55
Q

Energy substrates such as carbs, fat, and protein are what percentage of total energy supply?

56
Q

What are the amino acids broken down into pyruvate then acetyl-coa?

A

Threonine, glycine, serine, cysteine, and alanine.

57
Q

What are the amino acids used to make alpha-ketoadipate, acetoacetate, acetoacetyl-coa and then acetyl-coa?

A

Lysine, tryptophan, phenylalanine, tyrosine, and leucine

58
Q

What are the amino acids used to make alpha-ketoglutarate?

A

Arginine, proline, histidine, glutamine, and glutamate

59
Q

What are the amino acids used to make succinyl CoA?

A

Methionine, Isoleucine, and valine

60
Q

What is the enzyme used to convert L-methylmalonyl-CoA?

A

Methylmalonyl CoA mutase. It is a B12 dependent enzyme

Clinical Chemistry Spring 2023 (6 decks)

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