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Nutrition 1 (Semester I) > 4a. Biochemistry - Proteins, Enzymes > Flashcards

4a. Biochemistry - Proteins, Enzymes Flashcards

1
Q

What are the building blocks for proteins?

A

Amino acids

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2
Q

What four elements do amino acids contain?

A

Carbon
Hydrogen
Oxygen
Nitrogen

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3
Q

Which element distinguishes proteins from fats and carbs?

A

Nitrogen

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4
Q

How many different amino acids does the body need to create the proteins needed to function?

A

20

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5
Q

Which functional groups make up amino acids?

A

Carboxyl
Amino
Side chain of R that determines characteristics

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6
Q

What are the bonds that join amino acids together?

A

Peptide bonds

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7
Q

How do amino acids join together?

A

Dehydration synthesis

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8
Q

What are 2 amino acids joined together called?

A

Dipeptide

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9
Q

What are 3 amino acids joined together called?

A

Tripeptide

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10
Q

What type of peptide is aspartame?

A

Dipeptide

Neurotoxin

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11
Q

What type of peptide is glutathione?

A

Tripeptide

Antioxidant

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12
Q

Which three amino acids make up glutathione?

A

Cysteine
Glutamate
Glycine

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13
Q

Why do we need to ensure a good supply of cysteine in our diets?

A

We don’t have enough in the body which can impair glutathione production

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14
Q

Which foods are a good source of cysteine?

A

Legumes
Eggs
Sunflower seeds

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15
Q

What are the two types of amino acids?

A

Acidic side chains

Basic side chains

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16
Q

What do amino acids with acidic side chains do?

A

Release hydrogen ions

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17
Q

What do amino acids with basic side chains do?

A

Bind to hydrogen ions

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18
Q

What determines whether or not the amino acids release H+ or bind to hydrogen?

A

The pH of the surrounding fluid

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19
Q

What effect does the pH of the surrounding fluid do to a protein?

A

Effects its 3D structure and function

i.e. ceviche - raw fish - starts off soft, then goes hard when lemon juice squeezed on it

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20
Q

What characteristic do non-polar amino acids have?

A

Hydrophobic

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21
Q

How does a non-polar, hydrophobic amino acid react in a watery environment?

A

It folds to be on the inside of the protein structure, away from water

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22
Q

Example of a non-polar, amino acid

A

Tryptophan

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23
Q

What characteristic do polar amino acids have?

A

Hydrophilic

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24
Q

How does a polar, hydrophilic amino acid react in a watery environment?

A

It folds to be on the outside of the protein structure, interacting with the polar water molecules

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25
Q

Example of a polar, hydrophilic amino acid

A

Tyrosine

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26
Q

Examples of functions of proteins

A 
Fluid balance in blood e.g. albumin
Alternative energy source
Clotting mechanisms e.g. clotting factors
Enzyme production
Storage molecule e.g. ferritin
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27
Q

What is the 3D structure of a protein key to?

A

Its function

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28
Q

What is the process whereby a protein’s structure changes?

A

Denaturing

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29
Q

How can proteins become denatured?

A

Heat - cooking (e.g. egg whites)

Heavy metals e.g. lead, mercury

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30
Q

What is needed to digest proteins?

A

Enzymes

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31
Q

How are proteins digested?

A

Mouth - mechanically broken down

Stomach - pepsin enzyme breaks down peptide bonds between the amino acids

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32
Q

What is pepsin?

A

Enzyme

Released by gastric cells

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33
Q

What is the inactive form of pepsin called?

A

Pepsinogen

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34
Q

What activates pepsinogen into pepsin?

A

HCl

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35
Q

What is required for pepsin to function properly?

A

Fluid pH of 2

Adequate stomach acid

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36
Q

What happens when protein-rich chyme enters the small intestine?

A

Hormone CCK is released

Triggers release of pancreatic enzymes

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37
Q

What are the pancreatic enzymes?

A

Trypsin

Chymotrypsin

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38
Q

What happens to proteins once the pancreatic enzymes are released?

A

Broken down further into tripeptides, dipeptides and single amino acids by pancreatic juices and brush border enzymes
Absorbed into blood

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39
Q

What are nucleic acids?

A

Largest molecules in the body

Used to store genetic information

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40
Q

What are the most common nucleic acids?

A 
Deoxyribonucleic acid (DNA)
Ribonucleic acid (RNA)
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41
Q

What are the building blocks of nucleic acids called?

A

Nucleotides

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42
Q

What do nucleotides consist of?

A

Phosphate group
Sugar
Nitrogenous base

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43
Q

What are the functions of nucleic acids?

A

DNA - template for protein synthesis

RNA - copies specific sub-sections of DNA (genes) and translates it into proteins

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44
Q

What do the nucleotides in DNA contain?

A

5-carbon sugar deoxyribose

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45
Q

DNA contains which four nucleotide bases?

A

Adenine
Cytosine
Guanine
Thymine

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46
Q

Which nucleotide bases are purines?

A

Adenine

Guanine

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47
Q

Which nucleotide base pairs with adenine?

A

Thymine

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48
Q

Which nucleotide base pairs with cytosine?

A

Guanine

49
Q

What is the structure of DNA?

A

Two strands wound together like a twisted ladder

Double helix

50
Q

What are the ‘sides of the DNA ladder’ formed from?

A

Sugar-phosphate bonds which are covalent bonds

51
Q

What are the ‘rungs of the DNA ladder’ made from?

A

Hydrogen bonds

52
Q

What is the structure of RNA?

A

Single strand of nucleotides containing ribose

53
Q

When DNA is condensed down, what does it form?

A

Chromosomes

54
Q

What are the ends of chromosomes called?

A

Telomeres

55
Q

What affect does ageing have on telomeres?

A

Shortens them

56
Q

What can accelerate the shortening of telomeres?

A 
Stress
Poor nutrition
Poor sleep
Lack of exercise
Chemical agents
57
Q

What is mutation?

A

A change in the DNA sequence

58
Q

How can a mutation affect protein synthesis?

A

Can cause a change in the sequence of amino acids in the protein
This can cause the protein to be a slightly different shape

59
Q

How may a shape change affect a protein?

A

May affect its functionality

60
Q

How does a mutation cause sickle cell anaemia?

A

Mutation in gene that codes for the production of haemoglobin proteins
The haemoglobin becomes abnormally shaped and makes the RBCs defective

61
Q

How does a mutation cause haemophilia?

A

Affects genes associated with clotting factors 8 and 9

Results in problems clotting

62
Q

How can a mutation cause cancer?

A

Affects the genes that code for the proteins involved in regulating cell division

63
Q

What is gene expression?

A

The process by which the instructions in our DNA are converted into a functional product, such as a protein

64
Q

What can influence gene expression?

A

Environment the genes are bathed in
e.g. amount of toxins we’re exposed to
Certain nutrients

65
Q

Which nutrients can influence gene expression?

A 
Vit A
Vit D
EFAs
Fibre
Zinc
66
Q

Can gene mutations affect enzyme activity?

A

Yes

67
Q

What is MTHFR?

A

Enzyme necessary for converting folate (B9) into a form used for methlylation

68
Q

What is the active form of folate called?

A

Methylfolate

69
Q

What is methylfolate used for?

A

Metabolising homocysteine

associated with heart disease and dementia

70
Q

How can people with MTHFR mutations be affected?

A

Higher homocysteine levels which could lead to heart disease and/or dementia

71
Q

What may people with a MTHFR mutation benefit from?

A

Taking methylfolate

Avoiding excessive fortified folic foods e.g. cereals

72
Q

What are enzymes?

A

Biological catalysts made from protein

73
Q

What do enzymes do?

A

Create a lower energy way for starting materials to meet and react
Allows reactions to happen quicker in mild conditions within the body

74
Q

Can enzymes be reused?

A

Yes, they don’t get damaged during a reaction process so can be used again

75
Q

What are the molecules at the start of a reaction process called?

A

Substrates

76
Q

What does an enzyme convert a substrate to?

A

A product

77
Q

Example of enzyme, substrate, product

A

Enzyme - pepsin
Substrate - a protein e.g. food
Product - shorter protein chains

78
Q

What happens when a substrate binds to an enzyme?

A

The enzyme stresses the bond in the substrate
Weakens it
Allows body to more easily break bond

79
Q

What conditions do enzymes need to work correctly?

A

Correct temperate - 37C

Correct pH - could be acid or alkaline

80
Q

Does an enzyme reaction need more or less energy than a reaction without an enzyme?

A

Less

81
Q

What is the area on an enzyme where the substrate binds called?

A

Active site

82
Q

What are enzyme co-factors?

A

Usually vitamins or minerals that are needed to activate an enzyme

83
Q

Examples of enzyme co-factors

A

Zinc

Selenium

84
Q

How is zinc an enzyme co-factor?

A

Required to activate the enzyme ‘alcohol dehydrogenase’ that breaks down alcohol

85
Q

Why is selenium an enzyme co-factor?

A

Required for the antioxidant enzyme ‘glutathione peroxidase’

86
Q

What can a lack of co-factor lead to?

A

A reduction in enzyme activity

87
Q

What can affect the speed of enzyme reaction?

A

Substrate concentration

88
Q

What is substrate concentration?

A

Enzymes work best when there is plenty of substrate
As the concentration of substrate increases, so does the rate of enzyme activity
However, a point will be reached when the enzymes become saturated and no more substrates can fit at any one time even though there is plenty of substrate available
The available substrate has to wait for enzymes to clear their active sites
(wait for a parking space to become available)

89
Q

Example of substrate concentration in nutrition

A

The same enzyme converts O6 and O3
If someone ingests a lot of O6 and small amount of O3, the O6 will occupy the active sites meaning the O3 won’t be converted

90
Q

What happens to molecules at high temperatures?

A

Move much faster
More collisions
Faster reaction time

91
Q

How can high temperatures affect enzymes?

A

Atoms in enzymes vibrate too much
The weak bonds holding the 3D structure together can break
Enzyme becomes denatured

92
Q

What effect does over-eating have on enzyme production?

A

Eating more means more enzymes are produced and used up
Eventually enzyme production can’t meet demand
Impairs digestion and the absorption of nutrients

93
Q

Why is it important not to drink whilst eating?

A

Dilutes the digestive juices containing enzymes

94
Q

Other than over-eating, what other factors can reduce digestive enzyme output?

A

Prolonged stress

Nutritional deficiencies

95
Q

What treatment can be used to promote the production of digestive enzymes?

A

Herbal bitters

Bitter greens

96
Q

Examples of enzymes in food

A 
Bromelain - pineapples
Papain - papaya
Lipase - avocado
Alliinase - garlic
Actinidin - kiwi
97
Q

How are plant enzymes different to human enzymes?

A

Tolerate a wider pH

Less likely to be denatured

98
Q

What can denature plant enzymes?

A

Heat

Microwaving food

99
Q

At what temperature do enzymes start to be destroyed?

A

Above 40C

100
Q

What are the benefits of eating raw food?

A 
More enzymes
More vitamins
More minerals
More probiotics
More antioxidants
101
Q

What decreases the antioxidant value of food?

A

Cooking

102
Q

Which compounds become more readily available during heating?

A

Lycopene - tomatoes

Beta carotene - sweet pots, carrots, mangoes

102
Q

When is it advisable not to each raw foods?

A

SIBO - can cause immediate bloating
Thyroid disorders - raw turnips/cabbage (goitrogenic foods) can disrupt the uptake of iodine in thyroid gland
Yin conditions - lethargy, anaemia, feeling cold

103
Q

Which enzymes are involved in the creation of inflammatory mediators?

A

Cyclooxygenase 1 and 2

Lipoxygenase 5

104
Q

Which inflammatory mediator is created by cyclooxygenase 1 and 2?

A

Prostaglandins

105
Q

Which inflammatory mediator is created by lipoxygenase 5?

A

Leukotrienes

106
Q

Examples of natural anti-inflammatories

A

Turmeric
Ginger
Boswellia

107
Q

Which drugs can inhibit enzymes?

A

Antibiotics

Statins

108
Q

Which enzymes do antibiotics deactivate?

A

Zonulin - the enzyme necessary for the connections of amino acids in cell walls

109
Q

Which enzyme does statins inhibit?

A

HMG-CoA reductase - used by liver to make cholesterol and CoQ10

110
Q

What is systemic enzyme therapy?

A

Taking a large dose of proteolytic enzymes on an empty stomach so that some of the enzymes are able to reach the stomach intact

111
Q

What are the functions of proteolytic enzymes?

A

Reduce inflammation

Efficient clearance of damaged tissue

112
Q

Examples of proteolytic enzymes

A

Bromelain - pineapple
Serrapeptase
Pancreatic enzymes

113
Q

What properties has bromelain shown to have?

A

Anti-inflammatory
Anti-cancer
Anti-clotting
Reduce plaques (atherosclerosis)

114
Q

What properties does serrapeptase have?

A

Anti-inflammatory

115
Q

How does serrapeptase help with reducing inflammation?

A

Thinning fluids formed from injury
Inhibits release of pain-mediating chemicals
Enhances CV health by breaking down fibrin - a by-product of blood coagulation
(dissolves blood clots/atherosclerotic plaques)
Reduces pain/swelling without inhibiting prostaglandins

116
Q

How does serrapeptase alleviate pain?

A

By inhibiting release of bradykinin from inflamed tissues

Hydrolysing histamine

117
Q

Which inflammatory mediator does serrapeptase not inhibit?

A

Prostaglandins

118
Q

What are the therapeutic uses of serrapeptase?

A 
Inflammatory mediated pain
Scar tissue
Endometriosis
Autoimmunity
Excess mucus

Nutrition 1 (Semester I) (15 decks)

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