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Anatomy & Physiology 12 > ENZYMES AND HOMEOSTASIS UNIT TEST > Flashcards

ENZYMES AND HOMEOSTASIS UNIT TEST Flashcards

1
Q

Characteristics of enzymes (3):

A
  • Proteins with a 3-degree level of structure
  • Biological catalysts. Catalysts are substances that increase rate of chemical reaction without undergoing any permanent chemical change
  • Recycled or reused even after chemical reactions
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2
Q

Naming structure of enzymes and examples

A

Always ends with “ASE”. Ex. Maltase works on maltose, sucrase works on sucrose, ATPase works on ATP

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3
Q

Significance of enzymes

A

Speeds up chemical reactions by up to 100,000 times faster by lowering energy of activation of chemical reaction

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4
Q

Enzyme catalase

A

Breaks down hydrogen peroxide into hydrogen and oxygen gas

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5
Q

Activation energy/energy of activation

A

Barrier to chemical reactions. Minimum amount of energy required to start a reaction

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6
Q

How do catalysts work to speed up chemical reactions

A

Lowering the energy of activation

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7
Q

Non-catalyzed/no enzyme

A

Higher energy of activation needed to activate the reactants. Therefore, the rate of reaction is slower

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8
Q

Catalyzed/with enzyme

A

Lower energy of activation needed to activate the reactants. Therefore, the rate of reaction is faster

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9
Q

Protein portion of enzyme

A

Apoenzyme. Inactive on its own

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10
Q

Cofactor

A

Enzymes require a cofactor (helper molecule) which can be either an inorganic ion or vitamin molecule so that an enzyme can properly function

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11
Q

Examples of inorganic co factors

A

Metals such as copper, zinc, iron, magnesium, selenium, etc. MINERALS

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12
Q

Examples of organic non-protein factors

A

Vitamins, such as riboflavin, niacin. COENZYMES

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13
Q

Active site

A

Where the substrate attaches to enzyme to create a product

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14
Q

How is an active site created

A

When an apoenzyme is attached with a cofactor

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15
Q

What is it called when a cofactor is attached with apoenzyme

A

Holoenzyme, a functional enzyme

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16
Q

Simple equation in word form of enzyme composition

A

Apoenzyme (protein portion) + Co factor (in organic minerals or organic vitamin) = Holoenzyme (active enzyme)

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17
Q

Lock and key theory

A

Theory where an enzyme has a specific shape which allows the substrate to fit. Believed that an active enzyme substrate complex holds a substrate that fits like a lock and key to active site.

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18
Q

What reactions do enzymes work in

A

Hydrolysis or synthesis reactions

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19
Q

What happens when a random collusion occurs with an active site and substrate

A

Creates reaction and produces new product

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20
Q

Induced fit model

A

Some active sites are known to undergo a slight change in shape in order to accommodate a substrate. Enzyme is induced to a slight alteration to achieve a fit of substrate

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21
Q

Metabolism

A

Series of chemical reactions occurring in body

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22
Q

What chemical reactions do not occur haphazardly in cells and

A

Cellular respiration, photosynthesis, protein, and lipid synthesis digestion, etc. It is because they are usually part of a metabolic pathway which is a series of reactions

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23
Q

Metabolic pathways

A

Begin with substrate/reactant and terminate with an end product. Specific enzymes control each step of metabolic pathway so if an enzyme is missing then no reaction occurs

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24
Q

Easiest way to gain metabolic energy

A

In small increments rather than all at once

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25
Q

Example of simplified metabolic pathway

A

Starch – E1 (Analase)  Maltose – E2 (Hactase)  Glucose

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26
Q

8 things that affect enzyme activity:

A
  • Heavy metal
  • Surface area
  • Temperature
  • pH
  • Concentration of enzyme
  • Concentration of substrate
  • Concentration of product
  • Presence/absence of inhibitors
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27
Q

Heavy metal

A

Things like lead or mercury can attach to allosteric site of enzyme which disrupts normal distribution of electrons affecting the ionic bonds on active site. Enzyme becomes denatured

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28
Q

Surface area

A

Increasing the surface area of a solid will increase the amount of reactant that can react

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29
Q

Temperature (3):

A
  • Heat increases kinetic energy which increases reaction rate. For every 10 degrees Celsius, the reaction rate doubles
  • Proteins denature if temperature is above optimal temp (37). It will lose the level 3 shape and function of protein. High fever can also kill someone
  • If temp is cool, the protein will not denature but molecules will move slower and have less kinetic energy = less collisions with enzymes and substrates
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30
Q

Temperature of denaturation in animal enzymes

A

40-44 degrees Celsius

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31
Q

pH

A

Enzymes have a pH for optimum activity. Most enzymes are best near pH 7 (neutral)

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32
Q

Stomach pH

A

2-3

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33
Q

Small intestine pH

A

8-9

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34
Q

Mouth pH

A

7

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35
Q

Blood pH

A

7.2-7.4

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36
Q

Substrate concentration in enzyme activity (3):

Adding substrate to an enzyme-catalyzed reaction will increase reaction rate until all..

A

B. All active sites on enzymes are saturated with substrates

  • C. More enzymes are added to increase rate of activity and give more opportunities for enzymes to attach with substrates and active site
  • D. Until it has denatured, and no active sites collude with substrate
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37
Q

How to increase rate of activity

A

Add more enzymes to increase opportunity for enzymes to attach with substrate and active site

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38
Q

Concentration of enzymes (4):

Increasing ENZYMES will result in products being made until…

A
  • A. All substrates are acted upon
  • B. Have enzymes and many active sites but limited substrates for enzymes active sites to collide with = productivity shows no progress
  • C. Add more substrate = productivity increases
  • D. Number of products produced decreases because no more substates added
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39
Q

Inhibitors

A

Substance that slows down a chemical reaction or reduces activity of particular reactant, catalyst, or enzyme

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40
Q

Two types of inhibitors

A

Competitive inhibitors (irreversible) and non-competitive inhibitors (reversible)

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41
Q

Reversible inhibitors

A

Binds to enzyme non-covalently. Does not form chemical bonds or reaction with enzyme so they can be easily removed

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42
Q

Irreversible inhibitors

A

Binds to enzyme covalently. They form a chemical bond and cannot be removed. The inhibitor out competes the substrate to attach to active site

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43
Q

2 examples of irreversible inhibitors:

A
  • Poisons such as cyanide which inhibits essential enzyme called cytochrome c oxidase involved in cellular respiration
  • Penicillin, an antibiotic derived from fungi. They inhibit enzyme needed for bacteria to build cell wall during growth and cell division
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44
Q

Significance of genes with enzymes

A

Genes are necessary to increase or to decrease concentration of enzyme (gene expression)

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45
Q

Another way to control enzyme activity

A

Inhibiting or deactivating an enzyme

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46
Q

When does enzyme inhibition occur

A

When an active enzyme is prevented from combining with its substrate.

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47
Q

Feedback inhibition

A

Something that regulates every activity of an enzyme in a cell

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48
Q

Negative feedback inhibition

A

When the concentration of an end-product in a metabolic pathway increase, the end product binds to an enzyme in pathway

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49
Q

Significance of negative feedback

A

Mechanism involved in maintaining equilibrium/homeostasis (EQUAL)

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50
Q

Why does a negative feedback have that name

A

The binding of the end product to an allosteric (non-active site) causes change in tertiary shape of enzyme’s active site

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51
Q

How to determine if it is a reversible inhibitor

A

If it can unbind from allosteric site and follow the active site to be used again

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52
Q

What is activation energy

A

Minimum amount of energy required to activate molecules to which then they can undergo a chemical reaction

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53
Q

How does activation energy determine reaction rate

A

Higher the activation energy, the slower the chemical reaction because molecules can only complete reaction once they reached the top of activation energy barrier

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54
Q

How do catalysts work to speed up chemical reactions

A

Catalysts increase the reaction rate by lowering the activation energy needed

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55
Q

What do all enzymes names end with

A

ASE

56
Q

What components make up a holoenzyme

A

An apoenzyme (protein part) and a cofactor

57
Q

Apoenzyme

A

Protein portion of an enzyme

58
Q

Co enzyme

A

Substance that enhances action of an enzyme. They are organic non-proteins (vitamins) that bind with active site of enzyme for substrate recruitment

59
Q

Cofactor

A

Non-protein like vitamins or minerals that attach to apoenzyme and are necessary for enzyme function to work as catalyst. Co factors are inorganic while co enzymes are organic

60
Q

Co enzyme examples

A

Vitamins like riboflavin, or niacin

61
Q

Co factor examples

A

Inorganic stuff like metals, copper, zinc, iron, magnesium, selenium, or vitamins

62
Q

Metabolism

A

Series of chemical reactions occurring in body that change food to energy

63
Q

Metabolic pathway

A

Set of actions or interactions between genes and their products that result in change of some component of system that is essential for correct functioning

64
Q

Metabolic energy

A

Process of generating energy (ATP) from nutrients

65
Q

Allosteric site

A

Non-active site that causes change in tertiary shape of enzyme’s active site

66
Q

Lock and key theory

A

Theory that explains how enzymes are specific for their substrate. Each enzyme is specific for its substrate like a key for its lock

67
Q

Induced fit theory

A

Theory that the binding of a substrate to an enzyme causes change in shape of enzyme to enhance its activity

68
Q

Negative feedback inhibition

A

When too much of a substance results in decreased production of the same or different substance

69
Q

Body reaction when too hot (3):

A
  • Sweat
  • Blood dilates
  • SA increases to release heat
70
Q

Homeostasis

A

Maintenance of equilibrium of the body’s internal environment in the fact of changing conditions

71
Q

Examples of homeostasis (5):

A
  • Body temperature
  • Blood pressure
  • Blood pH
  • Blood glucose levels (0.1%)
  • Blood salt level (0.9%)
72
Q

Body reaction when too cold (3):

A
  • Shiver
  • Goosebumps
  • blood vessel constriction
73
Q

Body when blood pressure is too high

A

Arteries can dilate and lower the heart rate

74
Q

Body when blood pressure is too low

A

Arteries can constrict and increase heart rate

75
Q

How is blood pH maintained

A

Buffer which absorbs excess acid or base

76
Q

How is blood glucose levels maintained

A

Insulin and glucagon (hormones)

77
Q

How is blood salt level maintained

A

Kidney

78
Q

Importance of constant environment (2):

A
  • Chemical reactions occur within a narrow range of pH, temperature, and concentration
  • Cells need constant supply of nutrients
79
Q

What types of nutrients do cells constantly need

A

O2, amino acid, glucose, vitamin/minerals

80
Q

What needs to be constantly removed from cell

A

Nitrogenous wastes such as ammonia, urea

81
Q

What is toxic for a cell

A

Nitrogenous waste

82
Q

What do humans and animals have that eliminate urea from the blood

A

Kidneys

83
Q

Where was urea produced

A

Liver from nitrogenous waste

84
Q

Maintaining homeostasis

A

Feedback mechanisms

85
Q

Why is homeostasis important

A

Important because chemical reactions in cells occur within fine temp, pH, and concentration ranges

86
Q

Examples of stimuli (5):

A
  • Chemicals
  • Light
  • Sound waves
  • Motion
  • Touch
87
Q

4 main types of receptors:

A
  • Chemoreceptor
  • Photoreceptor
  • Mechanoreceptor
  • Thermoreceptor
88
Q

Chemoreceptor

A

Responds to chemical substances including taste, smell, blood pH, and pain

89
Q

Pain receptors in relation to chemoreceptors

A

Pain receptors are a type of chemoreceptors because they respond to chemicals released by damaged tissue

90
Q

Photoreceptor

A

Respond to light energy

91
Q

Mechanoreceptor

A

Respond to mechanical forces which result in pressure change

92
Q

Example of mechanoreceptor

A

Soundwaves converted to fluid-pressure to be detected by mechanoreceptor in the inner ear

93
Q

Pressure receptor in relation to mechanoreceptor

A

Certain arteries detect changes in blood pressure

94
Q

Stretch receptor in relation to mechanoreceptor

A

Stretch receptors in the lungs detect the degree of lung inflation, bladder, stomach, and rectum

95
Q

Thermoreceptor

A

Respond to warm and cold and are in skin and hypothalamus

96
Q

Sensory receptor significance

A

Respond to environmental stimuli by generating nerve impulses to the nervous system. Then the appropriate part of your body will generate impulses to the appropriate part of body for a response

97
Q

Negative feedback

A

Decreases the effect of stimulus

98
Q

Negative feedback mechanisms in blood

A

Blood pressure, blood pH, blood glucose levels are all maintained by negative feedback

99
Q

Hypothalamus

A

Thermostat for body temperature located in part of brain and maintains/controls homeostasis

100
Q

Positive feedback

A

Mechanism that makes the original stimulus more intense and does not restore homeosis so it takes it further away from equilibrium

101
Q

2 examples of positive feedback

A

Women giving birth and nursing a baby

102
Q

Positive feedback (women giving birth) in DETAIL steps (3):

A
  • Head of baby presses against cervix and stimulates mechanoreceptors
  • When nerve impulses reach brain, the brain causes pituitary gland to secrete oxytocin (hormone)
  • Oxytocin travels in blood to uterus and causes uterus to contract and push fetus
103
Q

How is the cervix stimulated when giving birth

A

Mechanoreceptors sends nerve impulses to brain and stimulates posterior pituitary glands to secrete oxytocin

104
Q

Positive feedback (nursing a baby) in DETAIL steps (3):

A
  • Sucking on a nipple cause nerve impulses to travel to hypothalamus
  • Oxytocin released by posterior pituitary gland
  • The lobules in mammary glands to contract, releasing milk
105
Q

What works with the nervous system to maintain homeostasis

A

Hormones and proteins

106
Q

Where are hormones secreted

A

Can be directly secreted into blood or into the ducts

107
Q

Endocrine glands

A

Glands that secrete hormones directly into blood

108
Q

Examples of endocrine glands (9):

A
  • Hypothalamus
  • Pituitary
  • Thyroid
  • Parathyroid
  • Thymus
  • Adrenal gland
  • Pancreas
  • Ovaries
  • Testes
109
Q

Exocrine glands

A

Glands that secrete hormones into ducts

110
Q

Examples of exocrine glands (2)

A

Hypothalamus and pancreas (The two are both endocrine and exocrine glands)

111
Q

Peptide hormones

A

Binds to specific receptor protein in plasma membrane

112
Q

When does protein relay end

A

Protein relay in plasma membrane ends when enzyme converts ATP to cAMP, which activates an enzyme cascade. Therefore, a metabolic pathway is activated

113
Q

Examples of peptide hormones (4):

A
  • Oxytocin
  • Insulin
  • Glucagon
  • Thyroxin
114
Q

Steroid hormone

A

After passing through cell membrane, a steroid hormone binds to receptor protein in nucleus

115
Q

Hormone-receptor complex

A

Binds to DNA. Activates certain genes and protein synthesis. Transcription and translation are also activated

116
Q

How is transcription and translation activated

A

When the hormone-receptor complex binds to DNA

117
Q

Where is the thyroid gland situated

A

In the neck in front of the trachea

118
Q

Examples of negative feedback loop in hormones

A

Thyroid gland producing peptide hormones called thyroxin which affects body cells. It increases rate of cellular respiration and metabolic rate

119
Q

What is needed to make thyroxin

A

Iodine

120
Q

Concentration of thyroxin compared to blood

A

Thyroxin is 25x greater than blood

121
Q

Good sources of iodine

A

Seaweed, seafood, ionized table salt

122
Q

Thyroxin level STIMULUS

A

Thyroxin level drops below set-point concentration, detected by osmoreceptors

123
Q

Thyroxin level REGULATORY CENTER

A

Hypothalamus releases Thyrotropin-RELEASING HORMONES (TRH) and it travels to anterior pituitary gland through a duct

124
Q

Thyroxin level ADAPTIVE RESPONSE

A

Anterior pituitary gland releases THYROID-STIMULATING HORMONE (TSH) in bloodstream. The TSH binds to receptors on plasma membrane of thyroid gland.

125
Q

If there are sufficient iodine in thyroid gland, what happens

A

Thyroxin is made and secreted into blood scream which causes an increase in thyroxin levels

126
Q

How long does negative feedback mechanism continue for

A

Continues until thyroxin levels are at/above set point and the stimulus is not detected by the hypothalamus

127
Q

Condition where you have too little thyroxin

A

Hypothyroidism

128
Q

Symptoms of hypothyroidism (9)

A
  • Fatigue
  • Weight gain
  • Low body temp
  • Hair loss
  • Slower pulse
  • Thick/puffy skin
  • Depression
  • Sensitive to cold temp
  • High risk of marriage if pregnant
  • Poor digestion
129
Q

Simple goiter

A

Enlargement of thyroid gland caused by lack of iodine in diet

130
Q

Why does the thyroid gland enlarge when you suffer from simple goiter

A

The anterior pituitary gland is constantly releasing TSH. The thyroid gland is stimulated to produce more thyroxin but since they don’t have iodine, thyroxin cannot be made.

131
Q

How is simple goiter treated

A

Iodized table salt, or eating more iodine-rich foods

132
Q

Cretinism

A

Condition when the thyroid gland fails to develop during infancy or early childhood

133
Q

Side effects or cretinism

A

Short and stocky due to skeletal growth usually inhibited and mental retardation occurs unless thyroid therapy begins in the first 2 months

134
Q

Condition where you have too much thyroxin

A

Hyperthyroidism

135
Q

What happens when you have hyperthyroidism

A

Thyroid gland becomes enlarged and overactive which causes a goiter to form and the eyes to protrude (tissue fluid increases and causes double vision)

136
Q

Symptoms of hyperthyroidism (8):

A
  • Hyperactivity
  • Nervousness
  • Irritability
  • Insomnia (sleep disorder)
  • Weight loss
  • Anxiety
  • Fast heart rate
  • Overheating
137
Q

How is enlarged thyroid gland treated in hyperthyroidism

A

Radiation or surgery

Anatomy & Physiology 12 (10 decks)

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