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Biochemistry > Unit 2 - Amino Acids > Flashcards

Unit 2 - Amino Acids Flashcards

1
Q

What are carbohydrates used for?

A

Energy
Some storage
Structure

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2
Q

What are lipids used for?

A

Energy
Storage
Structure

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3
Q

What are proteins used for?

A

Energy when caloric intake low
NO STORAGE
Structure

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4
Q

What chemicals are used for energy?

A

Carbs
Lipids
Some Proteins (low calories)

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5
Q

What chemicals are used for storage?

A

Some Carbohydrates
Lipids

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6
Q

What chemicals are used for structure?

A

Carbs
Lipids
Proteins

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7
Q

What chemicals are used for regulation?

A

Proteins

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8
Q

What are proteins made up of?

A

20 amino acid combinations

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9
Q

How many acids are “essential”

A

9

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10
Q

What are “essential” amino acids?

A

Not synthesized
From diet

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11
Q

How many amino acids are synthesized?

A

11

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12
Q

What organ synthesizes amino acids?

A

Liver and kidney

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13
Q

How do the liver and kidney synthesize amino acids?

A

Transamination
Deamination

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14
Q

What is transamination?

A

Converting one amino acid group into another

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15
Q

What is deamination?

A

Degrading amino acid to change it

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16
Q

What organs conserve amino acids?

A

Kidney
GI

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17
Q

What is the LAST CHOICE for energy use?

A

Amino Acids

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18
Q

Which organ reabsorbs amino acids?

A

Kidney

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19
Q

Which organ absorbs amino acids? How?

A

GI tract
Digested proteins

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20
Q

What is the basic structure of an amino acid?

A

Carboxyl Group
Amino Group
Alpha Carbon
R Group
Hydrogen

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21
Q

Why are amino acids named such?

A

Amino (NH2)
Acid (COOH)

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22
Q

What is the pH of the carboxyl group?

A

Weakly acidic

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23
Q

Alpha Carbon

A

Carbon at center of amino acid

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24
Q

Amino Group (Basic structure)

A

NH2

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25
Q

Carboxyl Group (Basic structure)

A

COOH

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26
Q

R group

A

Variable, changes with each a.a.

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27
Q

Amino acids contain both…

A

NH2 (Amino group)
COOH (Carboxyl group)

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28
Q

In an acid environment, what is in excess?

A

H+

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29
Q

What happens to the amino and carboxyl groups in an amino acid in Low pH environment?

A

Both protonated
- COOH retains H+
-NH2 gains H+ –> NH3+

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30
Q

Under acid conditions, how does the entire amino acid behave? (Why?)

A

As a cation, Net pos. charge
NH2 gains H+ = NH3+

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31
Q

What is physiological pH?

A

7.37 to 7.47

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32
Q

How does the structure of amino acid in physiological pH differ from the basic structure?

A

Carboxyl group has no H (COO-)
Amino group has extra H (NH3+)
is an Ampholyte

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33
Q

Ampholyte

A

Both Pos and Neg charges

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34
Q

What is another word for Ampholyte?

A

Dipolar ion

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35
Q

What is the charge on amino acid groups in physiological pH?

A

No Net Charge

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36
Q

What is the charge on amino acid groups in acidic pH?

A

Net Positive Charge

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37
Q

Amphoteric definition

A

Able to act as acid and base
Is a buffer

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38
Q

Why are amino acids at physiological groups good buffers?

A

They can accept or donate H+
(COO- and NH3+)

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39
Q

What is in excess in a high pH environment?

A

OH-

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40
Q

What happens to the basic structure of an amino acid in alkaline conditions?

A

COOH loses H (COO-)
NH2 loses H (NH2)
DEprotonated

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41
Q

What is the charge of the amino acid in acidic conditions?

A

Net NEGATIVE charge
Anion

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42
Q

What is a peptide bond

A

Bond between AMINO end of one a.a. and CARBOXYL end of one a.a.

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43
Q

Use “polymer” to describe protein formation

A

Proteins are polymers of a.a. joined at alpha carbon

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44
Q

Protein synthesis

A

DNA –> Gene –> m-RNA –> Ribosomes –> Protein

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45
Q

What is the Isoelectric point? (or PI)

A

the pH at which a.a. has net neutral charge

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46
Q

What determines an a.a. isoelectric point?

A

R group

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47
Q

How does R group determine an a.a. shape and behavior?

A

R group can be polar (hydrophilic, outside) or non polar (hydrophobic, inside)

48
Q

What happens when amino acids bind?

A

Peptide bond forms
Water released

49
Q

Why does a peptide bond form water?

A

OH released from carboxyl group
H released from Amino group
H2O

50
Q

Dipeptides

A

2 a.a.
1 peptide bond

51
Q

Tripeptides

A

3 a.a.
2 peptide bond

52
Q

Oligopeptides

A

UP TO 5 a.a.

53
Q

Oligo- definition

A

Few

54
Q

Polypeptides

A

6 to 30 a.a.

55
Q

How many a.a. constitutes a protein?

A

<40 a.a.
with complex organic compounds (C, H, O, N, S)

56
Q

Proteome

A

All the proteins an organism can make depending on their genetics

57
Q

Most a.a. diseases are due to..?

A

Genetic defects

58
Q

Renal aminoaciduria

A

Normal blood/plasma levels
Kidney CAN’t reabsorb a.a.

59
Q

Overflow aminoaciduria

A

Transport system overwhelmed
High blood/plasma levels
Renal threshold exceeded, reabsorption threshold exceeded

60
Q

Aminoacidopathies

A

Defect in handling parent a.a.
Parent a.a. in excess

61
Q

Organic acidemias

A

Issue in catabolic pathway of a.a. (transamination/deamination)
organic acid metabolites in excess
(parent a.a. may or may not accumulate)

62
Q

What is the main treatment of Inborn errors of metabolism?

A

Dietary avoidance of amino acid

63
Q

When do primary aminoacidopathies appear and why?

A

Early in life because its genetic

64
Q

When do secondary aminoacidopathies appear and why?

A

Later in life because acquired

65
Q

Liver disease causes…

A

a.a. overflow due to accumulation

66
Q

Phenylalanine levels that constitute phenylketonuria

A

> 2mg/dL
phenylalanine:tyrosine ratio high
(inc phenylalanine, dec tyrosine)

67
Q

How is tyrosine produced?

A

Adding OH to phenylalanine

68
Q

phenylketonuria has a deficiency of what enzyme

A

phenylalanine hydroxylate`

69
Q

What is formed in place of tyrosine in phenylketonuria?

A

Toxic phenylpyruvate

70
Q

Enzyme levels in classic PKU

A

Virtually absent

71
Q

End products and where they build up in Classic PKU

A

Phenylpyruvate/Phenylketoacids
Builds up in blood, urine, csf

72
Q

How to manage classic PKU?

A

Diet
no milk, dairy products or aspartame

73
Q

When is newborn screening done for classic PKU?

A

After sufficient milk feedings

74
Q

What is important to know about pregnant women with PKU?

A

Toxic products can cross the placenta

75
Q

PKU signs/symptoms

A

Normal at birth
Failure to thrive, babies
Urine has musty/mousy odor
Phenylalanine inc in blood, urine, CSF

76
Q

PKU Urine

A

Smells mousy/musty
Turns blue/green with ferric chloride (no longer done in US because genetic screening at birth)

77
Q

What does high levels of phenylalanine do?

A

Toxic to brain tissue
Irreversible mental retardation

78
Q

Why are PKU patients normally fair skinned?

A

Tyrosine needed to form melanin

79
Q

Inborn errors of metabolism

A

Aminoacidopathies
Organic acidemias

80
Q

What is the proportion of inborn errors seen between boys and girls?

A

Affect them both equally because autosomal recessive

81
Q

Aminoacidopathies are a defect in what?

A

The handling of parent amino acid
Increase a.a.

82
Q

Organic acidemias are a defect in what?

A

The catabolic pathway of an amino acid

83
Q

What accumulates in an organic acidemias?

A

Organic acid metabolites

84
Q

What amino acid becomes an essentiatal a.a. in PKU patients?

A

Tyrosine

85
Q

Difference between PKU and Tyrosnemia?

A

PKU can’t form tyrosine
Tyrosinemia can’t convert tyrosine

86
Q

What is tyrosine a precursor for?

A

Thyroxine/Thyroid hormones
Melanin
Adrenal hormones

87
Q

Which form of tyrosinemia is more severe?

A

1

88
Q

What is the enzyme that is deficient in tyrosinemia 1?

A

Fumarylactoacetate hydrolase at end of pathway

89
Q

What is the enzyme that is deficient in tyrosinemia 2?

A

Tyrosine aminotransferase at the beginning of pathway

90
Q

How to manage tyrosinemia?

A

Minimize phenylalanine and tyrosine in diet

91
Q

Why is Tyrosinemia 1 so detrimental?

A

Because at the end of the pathway, increase of tyrosine and its metabolic products

92
Q

Why is Tyrosinemia 2 less severe?

A

Because at the start of pathway, only tyrosine is increased, not metabolic products

93
Q

Diseases of Tyrosinemia 1

A

Cirrhosis
Acute hepatic failure

94
Q

S/S of Tyrosine 1

A

Hepatosplenomegaly
Photophobia
Ricketts
Tyrosine crystals in urine

95
Q

Diseases of Tyrosinemia 2

A

Eyes, skin, mental development problems

96
Q

Mousy urine

A

PKU

97
Q

What enzyme is deficient in Alkaptonuria?

A

Homogentisic Acid (HGA)

98
Q

What is alkaptonuria?

A

Dark urine caused by increase of HGA

99
Q

What is the clinical presentation of alkaptonuria?

A

Dark urine
Arthritis
Pigment cahnges

100
Q

What is a quick way to test for alkaptonuria?

A

Adding a base to fresh urine

101
Q

What is melanuria?

A

Malignant melanoma that increases melanogen that is present in urine and causes a dark color upon oxidation

102
Q

Types of Branched Chain Amino Acid Disorders?

A

Maple syrup urine disease
Organic Acidemia

103
Q

Burnt sugar urine smell

A

Maple syrup urine disease

104
Q

Sweaty feet urine smell

A

Organic acidemia

105
Q

What is in accumulation in maple syrup urine disease

A

Leucine
Isoleucine
Valine

106
Q

What are branched cahin a.a. disorders

A

Methyl group branches of a.a. chain

107
Q

What a.a. disorder is seen later in life?

A

Alkaptonuria

108
Q

What is not an amino acid disorder taht affects urine color?

A

Melanuria

109
Q

Why are branched chain a.a. disorders seen early in life?

A

Acute ketoacidosis episodes
- Failure to thrive
- Mental retardation and death

110
Q

Diagnostic findings for branched chain a.a. disorder

A

Inc ketones
Smells

111
Q

What is the most common inborn error of metabolism

A

Cystinuria

112
Q

What causes cystinuria

A

Cystine not reabsorbed by the kidney tubule because of lack of enzyme

113
Q

What is elevated in cystinuria?

A

Cystine
Lysine
Arginine
Ornithine
IN URINE

114
Q

What is the treatment for cystinuria?

A

Keep urine in alkaline pH to prevent crystal formation

115
Q

What is the best practice for detecting a.a. disorder?

A

High performance liquid chromatography tandem mass spectrometry (HPLC-MS-MS)

116
Q

Guthrie Test

A

Biochemistry (26 decks)

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