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PHM 532 Exam2 > FINAL ALL CHAPTERS > Flashcards

FINAL ALL CHAPTERS Flashcards

1
Q

What is maltose composed of?

A

Two glucose molecules (α-1,4 glycosidic bond).

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2
Q

What is isomaltose composed of?

A

Two glucose molecules (α-1,6 glycosidic bond).

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3
Q

What is sucrose composed of?

A

Glucose and fructose (α-1,2 glycosidic bond).

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4
Q

What is lactose composed of?

A

Glucose and galactose
(β-1,4 glycosidic bond).

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5
Q

What causes lactose intolerance?

A

Deficiency in lactase, leading to improper digestion of lactose.

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6
Q

What symptoms arise from lactose intolerance?

A

Bloating, diarrhea, and gas due to fermentation in the colon.

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7
Q

How are peptide bonds counted in multiple polypeptides linked by disulfide bonds?

A

Each chain contributes n−1n−1 peptide bonds; disulfide bonds stabilize structure but are not peptide bonds.

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8
Q

What distinguishes essential amino acids from non-essential?

A

Essential must be obtained from diet; non-essential can be synthesized by the body.

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9
Q

Are most amino acids chiral or achiral?

A

Most are chiral, except glycine, which is achiral.

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10
Q

What happens to lactose when it is not digested?

A

It ferments in the colon, causing symptoms.

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11
Q

What is the formula for the number of peptide bonds in multiple polypeptides?

A

Each contributes n-1 n-1 peptide bonds.

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12
Q

What is an example of a metabolic property of amino acids?

A

Some act as precursor for neurotransmitters.

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13
Q

What distinguishes an essential amino acid?

A

It cannot be synthesized by the body and must be obtained from the diet.

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14
Q

What type of amine group do amino acids possess?

A

A primart amine group.

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15
Q

Which amino acid is achiral?

A

Glycine.

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16
Q

What is the role of disulfide bonds in proteins?

A

They stabilize the overall structure of multiple polypeptides.

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17
Q

Why is glycine considered unique among amino acids?

A

It is the only achiral amino acid.

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18
Q

How do amino acids function as neurotransmitter precursors?

A

They are converted into neurotransmitters, such as serotonin from tryptophan.

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19
Q

What dietary adjustments are often made by those with lactose intolerance?

A

Reduction or elimination of lactose-containing foods.

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20
Q

What are common gastrointestinal symptoms of lactose intolerance?

A

Bloating, diarrhea, gas, and abdominal pain.

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21
Q

What enzyme is responsible for breaking down lactose?

A

Lactase.

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22
Q

What are the basic components of an amino acid?

A

An amino group, carboxyl group, hydrogen atom, R group (side chain).

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23
Q

How is a peptide bond formed?

A

Condensation reaction between the carboxyl group of one amino acid and the amino group of another, releasing water.

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24
Q

What role do enzymes play in biochemical reactions?

A

They act as catalysts, lowering the activation energy and speeding up reactions.

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25
Q

What does enzyme specificity refer to?

A

The ability of an enzyme to selectively catalyze a particular reaction for specific substrates.

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26
Q

Why is pH important for enzyme function?

A

Enzymes have optimal pH ranges; deviations can denature the enzyme or affect its activity.

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27
Q

What are cofactors?

A

Non-protein molecules that assist enzymes in catalyzing reactions, often metal ions or organic molecules (coenzymes).

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28
Q

What is competitive inhibition?

A

When an inhibitor competes with the substrate for binding to the active site of the enzyme, increasing Km but not affecting Vmax.

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29
Q

What is non-competitive inhibition?

A

When an inhibitor binds to an enzyme regardless of whether the substrate is present, decreasing Vmax without affecting affecting Km.

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30
Q

What is the primary function of the TCA cycle?

A

To generate energy through the oxidation of acetyl-CoA and produce NADH and FADH2 for the ETC.

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31
Q

What is acetyl-CoA’s role in metabolism?

A

It serves as a key substrate in energy production and synthesis of fatty acids and ketone bodies.

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32
Q

What us a significant function of glutamine?

A

It serves as a nitrogen donor in the synthesis of nucleotides and amino acids.

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33
Q

What biochemical property determines the solubility of free fatty acids in water?

A

The degree of saturation (number of double bonds) and the length of the carbon chain.

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34
Q

How does saturation affect the solubility of fatty acids?

A

Saturated fatty acids are less soluble in water than unsaturated fatty acids.

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35
Q

What factors influence the melting point of unbranched fatty acids?

A

The length of the carbon chain and the degree of saturation.

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36
Q

How do longer chains and saturation affect the melting point?

A

Longer chains and higher saturation increase melting points, while unsaturation lowers them.

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37
Q

Are most fatty acids essential or non-essential?

A

Most fatty acids are non-essential; however, linoleic and alpha-linolenic acids are essential.

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38
Q

How are fatty acids classified as omega-3 or omega-6?

A

Based on the position of the first double bond from the methyl end (omega-3: third carbon; omega-6: sixth carbon)

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39
Q

What are the full names of three omega-3 fatty acids?

A
  1. Alpha-linolenic acid (ALA)
  2. Eicosapentaenoic acid (EPA)
  3. Docosahexaenoic acid (DHA)
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40
Q

What is a gene?

A

A segment of DNA that contains instructions for synthesizing proteins or RNA molecules; it is basic unit of heredity.

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41
Q

What type of bonds from between complementary nitrogen bases in DNA?

A

Hydrogen bonds.

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42
Q

How many hydrogen bonds form between adenine and thymine (A-T)?

A

2 hydrogen bonds.

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43
Q

How many hydrogen bonds form between cytosine and guanine (C-G)?

A

3 hydrogen bonds.

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44
Q

Why do phosphodiester bonds connect in a DNA molecule?

A

They connect the sugar and phosphate backbone, linking adjacent nucleotides.

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45
Q

Name the purine nitrogen bases.

A

Adenine (A) and Guanine (G).

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46
Q

Name the pyrimidine nitrogen bases.

A

Cytosine (C), Thymine (T), Uracil (U in RNA).

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47
Q

What is a high anion gap associated with?

A

Accumulation of unmeasured anions (lactic acidosis, ketoacidosis).

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48
Q

What typically causes a normal anion gap?

A

Loss of bicarbonate (diarrhea, renal tubular acidosis).

49
Q

What does the turnover number (k_cat) indicate about an enzyme?

A

The number of substrate molecules converted to product per enzyme molecule per unit time.

50
Q

What happens to enzyme activity if temperature exceeds the optimal range?

A

Enzymes may denature, losing their functional shape and activity.

51
Q

What is the enzyme-substrate complex?

A

The intermediate formed when an enzyme binds to its substrate, facilitating the reaction.

52
Q

Name the two main types of enzyme inhibition.

A

Competitive inhibition and non-competitive inhibition.

53
Q

What role do all allosteric sites play in enzyme regulation?

A

Allosteric sites allow molecules to bind, causing conformational changes that can enhance or inhibit enzyme activity.

54
Q

What is a key difference between NADH and FADH2 in cellular respiration?

A

NADH produces more ATP per molecule than FADH2 when oxidized in the ETC.

55
Q

How does insulin affect glucose metabolism?

A

Insulin promotes the uptake of glucose by cells and stimulates glycogen synthesis.

56
Q

When is the lactic acid threshold?

A

It is the exercise intensity at which lactate starts to accumulate in the blood, indicating anaerobic metabolism.

57
Q

What is the role of coenzymes in enzyme reactions?

A

Coenzymes assist enzymes by carrying chemical groups or electrons during reactions.

58
Q

What is the main product of beta-oxidation?

A

Acetyl-CoA, which enters the TCA cycle for energy production.

59
Q

How are glycolysis and the TCA cycle interconnected?

A

Pyruvate from glycolysis is converted to acetyl-CoA, which enters the TCA cycle.

60
Q

What does the turnover number (k_cat) indicate?

A

It indicates the maximum number of substrate molecules an enzyme converts to product per unit time when fully saturated.

61
Q

How is enzyme activity typically measured?

A

By monitoring the rate of product formation or substrate consumption over time.

62
Q

What happens to enzyme activity at high temperatures?

A

Enzyme activity generally increases with temperature up to a certain point, after which it may denature and lose activity.

63
Q

What are coenzymes?

A

Organic molecules that assist enzymes in catalyzing reactions, often derived from vitamins (e.g., NAD+, FAD).

64
Q

What is a metabolic pathway?

A

A series of interconnected biochemical reactions that convert substrates into products through enzyme activity.

65
Q

What does the Michaelis-Menten equation describe?

A

The relationship between reaction rate (v), maximum velocity (Vmax), substrate concentration ([S]), and Km.

66
Q

How can you distinguish between competitive and non-competitive inhibition?

A

Competitive inhibition affects Km by increasing it, while non-competitive inhibition does not change Km but reduces Vmax.

67
Q

How does lactic fermentation benefit muscles during exercise?

A

It allows for ATP production when oxygen is limited by regenerating NAD⁺ for glycolysis.

68
Q

What is the primary use of ketone bodies in tissues?

A

They are converted back to acetyl-CoA for energy production, particularly in the brain and muscles.

69
Q

What role does the heme group in hemoglobin play?

A

Each subunit contains a heme moiety that binds to iron (Fe²⁺), enabling oxygen transport.

70
Q

What are the two primary functions of hemoglobin?

A
  1. Oxygen transporter (carries O₂ to tissues, CO₂ back to lungs).
  2. Buffer (maintains pH by binding protons and regulating CO₂ levels).
71
Q

What does the oxygen dissociation curve measure?

A

The percentage of hemoglobin bound to oxygen (O₂ saturation).

72
Q

What promotes O₂ release from hemoglobin in peripheral tissues?

A

Low partial pressure of O₂.

73
Q

What factors produce the Bohr effect?

A

Increased CO₂, H⁺ concentration, and temperature enhance O₂ release.

74
Q

What is the Rapoport-Luebering cycle?

A

A pathway that shunts 1,3-bisphosphoglycerate from glycolysis to generate 2,3-bisphosphoglycerate (2,3-BPG), lowering hemoglobin’s affinity for O₂.

75
Q

What is the purpose of the HbA1c glycation test?

A

It measures average blood glucose levels over 2-3 months, useful for diagnosing and monitoring diabetes.

76
Q

How does calcium function in muscle contraction?

A

It binds to troponin, causing a conformational change in tropomyosin that exposes myosin-binding sites on actin.

77
Q

What is the role of ATP in muscle function?

A

Provides energy for muscle contraction and relaxation, crucial for cross-bridge cycling between actin and myosin.

78
Q

What is rigor mortis?

A

Stiffening of muscles post-mortem due to ATP depletion, causing myosin heads to remain bound to actin.

79
Q

What is the average lifespan of red blood cells?

A

Approximately 120 days; aged cells are removed by the spleen and liver.

80
Q

Describe the metabolic degradation of heme to bilirubin.

A

Heme → Biliverdin → Bilirubin (unconjugated) → Conjugated bilirubin in the liver.

81
Q

What is jaundice?

A

Accumulation of bilirubin in the blood leading to yellowing of skin and eyes.

82
Q

What are the types of jaundice?

A

Pre-hepatic (hemolytic), hepatic (liver dysfunction), and post-hepatic (obstruction of bile flow).

83
Q

Define oxidants.

A

Substances that can oxidize other molecules, often producing free radicals.

84
Q

Define antioxidants.

A

Molecules that neutralize free radicals and prevent oxidative damage.

85
Q

What is oxidative stress?

A

An imbalance between oxidants and antioxidants, leading to cellular damage.

86
Q

Name some reactive oxygen species (ROS).

A

Superoxide (O₂⁻), hydrogen peroxide (H₂O₂), hydroxyl radical (*OH), nitric oxide (NO).

87
Q

What enzyme converts superoxide radicals into hydrogen peroxide?

A

Superoxide dismutase (SOD).

88
Q

What are some enzymatic antioxidants?

A

Superoxide dismutase (SOD), glutathione peroxidase, glutathione reductase.

89
Q

What are some non-enzymatic antioxidants?

A

Vitamins (e.g., C, E), minerals (e.g., selenium, zinc).

90
Q

What are the biochemical components of glutathione?

A

Cysteine, glutamine, and glycine.

91
Q

What is the function of glutathione in the body?

A

Acts as a major antioxidant, reducing oxidative stress.

92
Q

What does glutathione reductase do?

A

Converts GSSG back to reduced glutathione (GSH) using NADPH.

93
Q

What is the biochemical importance of the pentose phosphate pathway?

A

Generates NADPH for reductive biosynthesis and ribose-5-phosphate for nucleotide synthesis.

94
Q

What is favism?

A

A genetic condition where consumption of fava beans leads to hemolytic anemia due to glucose-6-phosphate dehydrogenase (G6PD) deficiency, causing oxidative stress in red blood cells.

95
Q

What hormone promotes glucose uptake and storage in the fed state?

A

Insulin; it also stimulates lipogenesis and enhances protein synthesis.

96
Q

What are the effects of insulin on lipids in the fed state?

A

Increases fatty acid synthesis and storage in adipose tissue; promotes storage of triglycerides.

97
Q

What hormone is prominent in the fasting state?

A

Glucagon; it increases mobilization of fatty acids and promotes gluconeogenesis.

98
Q

How does glucagon affect lipid metabolism?

A

Enhances lipolysis (breakdown of fats) and increases ketogenesis for energy supply.

99
Q

List biochemical signs of metabolic syndrome.

A

Elevated blood glucose, dyslipidemia (high triglycerides, low HDL), hypertension, central obesity.

100
Q

What are the pathophysiological manifestations of metabolic syndrome?

A

Increased risk of cardiovascular diseases, development of type 2 diabetes, chronic inflammation, and endothelial dysfunction.

100
Q

What is the role of acetyl CoA in fatty acid biosynthesis?

A

It serves as a precursor for the synthesis of fatty acids.

101
Q

What is the biochemical role of malonyl CoA in fatty acid biosynthesis?

A

It acts as a building block and provides carbon units for fatty acid synthesis.

102
Q

How does biotin function in the biosynthesis of fatty acids?

A

It acts as a coenzyme for acetyl CoA carboxylase, essential for converting acetyl CoA to malonyl CoA.

103
Q

Describe the initial step in vitamin D biosynthesis in the skin.

A

UVB radiation converts 7-dehydrocholesterol to previtamin D3.

104
Q

What occurs to previtamin D3 in the liver?

A

It is converted to 25-hydroxyvitamin D (calcidiol).

104
Q

What is the final activation step of vitamin D in the kidney?

A

Conversion of 25-hydroxyvitamin D to 1,25-dihydroxyvitamin D (calcitriol).

105
Q

How does vitamin D affect calcium absorption?

A

It increases intestinal absorption of calcium by enhancing expression of calcium-binding proteins.

106
Q

What are the structural differences between vitamin D3 and D2?

A

Vitamin D3 (cholecalciferol) is produced in the skin; D2 (ergocalciferol) is derived from yeast and fungi and is less potent.

106
Q

What are the five types of lipoproteins?

A

Chylomicrons, VLDL, LDL, HDL, IDL.

107
Q

What does potency refer to in terms of vitamin D?

A

Potency indicates how effectively a vitamin raises serum levels of 25-hydroxyvitamin D; D3 is generally more potent than D2.

108
Q

How is the relationship between volume and density characterized in lipoproteins?

A

Larger lipoproteins (e.g., chylomicrons) are less dense; smaller lipoproteins (e.g., HDL) are more dense.

109
Q

What is the difference between exogenous and endogenous pathways of lipoproteins?

A

Exogenous: Transport dietary lipids from intestines to tissues (chylomicrons). Endogenous: Transport synthesized lipids from liver to tissues (VLDL, LDL).

110
Q

What is the role of Apo-B48?

A

It is crucial for intestinal lipid transport and is present in chylomicrons.

111
Q

What role does Apo-CII play in lipid metabolism?

A

It activates lipoprotein lipase, facilitating the hydrolysis of triglycerides.

111
Q

What is the function of Apo-B100?

A

It is important for lipid metabolism and receptor binding, found in VLDL and LDL.

112
Q

What does Apo-A1 do?

A

It activates lecithin-cholesterol acyltransferase (LCAT) and is a major protein in HDL.

113
Q

What is the reverse transport of cholesterol?

A

The process by which HDL collects excess cholesterol from tissues and transports it back to the liver.

113
Q

Why do LDL particles have a longer circulation time than other lipoproteins?

A

Due to their size and affinity for receptors, allowing prolonged delivery of cholesterol.

114
Q

Why is HDL referred to as “good cholesterol”?

A

It reduces the risk of atherosclerosis by transporting excess cholesterol for excretion or recycling.

PHM 532 Exam2 (5 decks)

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