Lecture 15: Fundamentals Of Nutrition Flashcards

1
Q

What major metabolic processes occur in the cytosol?

A
  • Glycolysis
  • Pentose Phosphate Pathway
  • Fatty Acid Synthesis
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2
Q

What major metabolic processes occur in the mitochondrial matrix?

A
  • Citric Acid Cycle
  • Oxidative Phosphorylation
  • Beta-oxidation of Fatty acid chains
  • Ketone Body Formation
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3
Q

Where is the only place in the body where all metabolic pathways can occur?

What are the 3 major junctions of all these processes?

A

The Liver

  • Glucose-6-Phosphate, Pyruvate, Acetyl-CoA
  • Note: Gluconeogenesis and Urea Synthesis occur in a mix between cytosol and mitochondria.
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4
Q

Loosely Describe What occurs during the fed state in your body

A

1-3: Intestines release Glucose, Amino Acids, and Chylomicrons into the blood stream from food.
4-6. In response to the glucose, blood increases insulin content and decreases glucagon content, causing blood to be converted into glycogen and acetyl-coA in the liver (excess acetyl-CoA goes to the brain)
7, 12, 13 - Excess triglycerides from Acetyl-CoA are released from the liver as VLDL and merge with chylomicrons to form adipose tissue.

Else: Muscle tissue utilizes acetyl CoA for needed energy while red blood cells convert pyruvate into lactate.

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5
Q

What is different that occurs in the fasting state rather than the Fed state?

A
  • Triglycerides are broken down into glycerol, muscle proteins are broken down into amino acids, and lactate is taken from red blood cells into the liver to produce glucose and ATP (glycogen is also broken down into the liver)
  • In response to the glucose-deficient state, blood decreases insulin and releases glucagon to activate the previous stuff in the last bullet.
  • Urea byproducts from amino acid breakdown are converted to urine in the kidneys.
  • I “think” only glucose can enter the brain.
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6
Q

VERY briefly describe where most of our ATP comes from

A
  • Glucose, Amino Acids, and Fatty Acids are all utilized in the production of Acety-CoA. Acetyl-CoA is used to trigger a rotation of the TCA cycle, generating electrons, CO2, and some other stuff.
  • The electrons are converted into ATP via the Electron transport chain.
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7
Q

What are proteins (at least pertaining to this lecture)?

A
  • Biomolecules constructed from Amino Acids
  • Critically important in Cell Life
    • As a fuel supply (TCA Cycle -> ATP Production)
    • Structural Support (Keratin, Collagen, Elastin)
    • Activity (Enzymes, Cell Signaling, Motion)
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8
Q

Describe amino acids

A
  • Nitrogen containing carboxylic acids
  • Proteinogenic Amino Acids serve as the basic building blocks of peptides and proteins
  • Essential amino acids (10) must be obtained from diet.
  • Amino acids function as precursors of biologically important molecules.
    • Acetyl CoA is produced from pyruvate, which can be generated from amino acids; TCA cycle intermediates can also be generated from amino acids.
    • Precursors of nitrogen-containing molecules such as heme, amines, melanin, and other genetic materials
    • Hormones such as insulin and glucagon.
    • Essential amino acids are crucial for maintaining health. If not taking them sufficiently, patient Will have a negative nitrogen balance.
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9
Q

Describe Carbohydrates (Pertaining to this chapter)

A
  • Organic molecules made up of C, H, and O. Usually something like C4H2O6 or whatever. (I just made that one up)
  • Important fuel stores, and a critical molecule in the control of human metabolism; catabolic in nature
  • Carbon Skeletons are used for synthesis of the other important biomolecules, so also highly anabolic when needed.
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10
Q

List the 4 common sources of dietary carbohydrates

A
  1. Starches:
    - The nutritional reservoir of CH in plants and a polysaccharide of glucose.
    - Amylose is the unbranched form
    - Amylopectin is the branched form
  2. Sucrose: Natural sweetener found in fruits and vegetables
    - These are disaccharides of glucose and fructose
  3. Dietary Fiber: Plant Origin
  4. Lactose: The major dietary carbohydrates of animal origins.
    - These are disaccharides of Glucose and Galactose
    - Lactose intolerance is the body’s inability to digest lactose
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11
Q

Describe the 4 types of Carbohydrates

A
  1. Monosaccharides: Simplest Form
    - Glucose, Fructose, galactose, ribose
  2. Disaccharides: Two monosaccharides
    - Maltose, lactose, sucrose
  3. Oligosacchardies: 3-10 Monosaccharides
    - Glycolipids and glycoproteins (attached to membrane lipids and proteins respectively)
  4. Polysaccharides: Over 10 monosaccharides
    - Glycogen, starch, cellulose
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12
Q

What are epimers?

What is the major difference between a Ketose and an Aldose?

A
  • Epimers are diastereomers that differ in configuration of only one stereogenic (chiral center). For example, D-Glucose and D-Galactose are epimers.
  • Ketoses have alcohols on the bottom, and Ketone groups at the top (But still with the alcohol endpiece). Aldoses simply end in aldehydes.
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13
Q

Should Learn how to Draw Dihydroxyacetone, Fructose, Ribulose, Glyceraldehyde, Ribose, Glucose, Manose, and galactose.

A

Fuck My Life.

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14
Q

When an open chain fructose folds into a cyclic form of fructose, which stand out carbons/oxygens are connected.

A
  • Carbonyl C=O group at C2 becomes the C connector of the pentagon ring. The associated O becomes an additional OH side group.
  • OH group at C5 becomes the O connector of the pentagon. The respective H joins the aforementioned OH side-chain.
  • Monosaccharides exist in solution mainly as ring structures and are more stable.
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15
Q

Describe what constitutes a glycosidic bond and give an example of each type.

A

Sucrose - Alpha1-Beta2 Bond (Hexagon to pentagon)
Lactose - Beta1-4 Bond (Lactose)
Maltose: Alpha1-4 Bond

  • These are all joined by O-glycosidic bond
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16
Q

Describe Amylose

Describe Amylopectin

A

Amylose is a type of polysaccharide of glucose residues linked with an alpha1-4 glycosidic bonds.

Amylopectin is an amylose with the addition of alpha-1,6 glycosidic branch points

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17
Q

Describe Cellulose

A
  • A major plant polysaccharide
  • Unbranched polymer of glucose residues are joined by a Beta1-4 linkage, allowing to form very long and straight chains
  • Bent is favored because bent is more suitable for storage.
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18
Q

What are 5 chemically modified derivatives of monosaccharides

A
  1. Deoxyaldose: A major component of DNA
  2. Acetylated amino sugars: They are components of glycoproteins and glycolipids [cell signaling, cell adhesion, immunoresponse]
  3. Acidic Sugars: Glycosaminoglycans and proteoglycans. Present in cell membrane and in the extracellular matrix.
  4. Sugar esters: Constituted the gangliosides in oligodendrocyte of the nervous system.
  5. Sugar alcohols: Food additives, gains importance in uncontrolled diabetetes leading to cataracts and peripheral neuropathy used in synthesis of lipids.
    - See Slide 30
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19
Q

Why is High Fructose Corn Syrup believed to be so fattening?

A

It bypasses a major regulatory step in glycolysis, enteriing at step 5. This disrupts fuel metabolism and increases productions of lipids since DAG can be converted to glycerol-3-phosphate and then into triacylglycerols.
- See Slides 33-35

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20
Q

What is a lipid?

A
  • Water insoluble biomolecules that are highly soluble in organic solvents
  • Membrane constituents
  • Fatty Acids are key constituents of lipids
  • The hydrophobic properties of lipids are due to the fatty acids
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21
Q

Describe fatty acids

A
  • Contains a hydrocarbon chain, and a carboxylilc acid group.
  • Building Blocks of phospholipids and glycolipids, components of biological membranes.
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22
Q

Fatty acids are oxidized in the mitochondria to generate ATP. What is the important enzyme needed in lipid digestion?

A

Lipase enzyme: inefficient expression of this enzyme leads gastrointestinal problems

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23
Q

Where are saturated acids usually found?

A

Animal fats. Holds more energy than unsaturated, but an cause problems because it’s harder to break apart.
- Note: Introduction of the double bond reduces the potential energy of the fatty acid.

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24
Q

Be able to draw, or at least recognize Vitamin A, Vitamin D, Vitamin E, and Vitamin K.

A

DO IT!

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25
Q

Describe Vitamin A

A
  • Precursor Beta-Carotene is found in spinach, carrots, dark green leafy vegetables, and yellow vegetables
  • Vitamin A derivative retinol is found in the liver, cod liver oil, dairy products, and eggs.
  • Synthetic Derivatives of Vitamin A include the drugs tretinoin and isotretinoin.
26
Q

Describe Vitamin D

A
  • D2 (ergocalciferol) and Vitamin D3(Cholecalciferol) are found in liver, eggs, fish, plants, and vitamin D-fortified foods such as milk and cereal.
  • D3 is also produced in the skin via a mechanism that requires sunlight exposure
  • Calcitriol, the bioactive form of D, is derived from Vitamin D2 and D3.
  • D can be defined as fatty acids that are converted to a form of cholesterol that is converted to D3 in the skin by UV…and is also made by the intestines
  • Liver makes calciferol and kidney finally make the active form, calcitriol
27
Q

Describe Vitamin E

A

Tocopherols, which are members of the vitamin E family, are found in vegetables oils, seeds, nuts, and green leafy vegetables.

28
Q

Describe Vitamin K

A
  • Vitamin K1 is obtained from green leafy vegetables

- Vitamin K2 is synthesized by bacteria in the large intestine and colon

29
Q

Describe the location of every Vitamin D conversion

A
  • Within the Skin, 7-Dehydrocholesterol is converted to Cholecalciferol by D3 by UV light
  • Within the intestines Ergocalciferol (D2) is converted back and forth from cholecalciferol (D3)
  • Within the liver, cholecalciferol is coverted by 25-Hydroxylase into 25-Hydroxylcholecalciferol
30
Q

Describe the Vitamin K Cycle

A

Vitamin K exists in 3 forms. One of which is a cofactor for gamma-carboxylase, involved in clotting. Warfarin inhibits.

  1. Vitamin K starts out in the form of phylloquinone.
  2. Vitamin K-reductase reduces in down to Hydroquinone(K)
  3. CO2, and O2 join the clotting factor precursor and are enzymated by gamma-carboxylase, which shape it into Epoxide (K) (Note: CO2/O2 precursors bind to matured clotting factors) (may need to know that it includes a “Glu” connected to a carboxylate, which helps with coagulation)
  4. Vitamin K-Epoxide is reduced by V. K-Epoxide reductase back into phylloquinone. Also inhibited by warfarin.
31
Q

List the name and functional form for all of the Vitamins involved in redox reactions

A
  • C: Ascorbic Acid - Ascorbate
  • B2: Riboflavin - Flavin Adenine dinucleotide (FAD)
  • B3: Niacin - N+ and NADP+
32
Q

List all of the names and functional forms for vitamins involved in nonredox reactions

A
  • B1: Thiamin; Thiamine Pyrophosphate(TPP)
  • B5:Pantothenic Acid; Coenzyme A
  • B6: Pyridoxine; Pyridoxal Phosphate
  • B12: Cobalamin; Adenosylcobalamin Methylcobalamin
  • Biotin; Biotin
  • Folate: Tetrahydrofolate
33
Q

List known disorders associated with vitamin Deficiencies (in vitamins involved in redox reactions)

A
  • B2: Cheilosis, Angular Stomatitis
  • B3: Pellagra with diarrhea, dermatitis, dementia
  • C: Scurvy w/ petechiae, ecchymoses, bleeding gums
34
Q

List known disorders associated with vitamin Deficiencies (in vitamins involved in nonredox reactions)

A
  • B1: Beriberi, polyneuritis, Wernicke-Korsakoff Syndrome
  • B5: Deficiencies are rare
  • B6: Nasolateral seborrhea, glossitis, peripheral neuropathy
  • B12: Pernicious Anemia, neurologic disorders, pallor
  • Biotin: Fatigue, Depression, Nausea, Dermatitis, Muscle Pain
  • Folate: Megaloblastic Anemia, Mental status changes, glossitis, palor
35
Q

Name the 3 minerals commonly regarded as electrolytes

A

Sodium, Potassium, Chlorine

36
Q

Name the 5 most essential minerals (apart from electrolytes)

A

Calcium, Phosphorous, Magnesium, Iron, Sulfur

37
Q

Name the 2 Enzymes associated with Zinc

A

Carbonic anhydrase, and carbodypeptidase

38
Q

What do coenzyme A, NAD+, FAD, Lipoic Acid, and Thiamine Pyrophosphate

A

They are found in the metabolically important enzyme complexes: Alpha-Ketoglutarate Dehydrogenase, Branched-Chain alpha-keto acid dehydrogenase, and Pyruvate Dehydrogenase

39
Q

What form is iron in in the intestinal lumen?

A
  • Fe2+ usually in the heme iron. Enters the apical membrane of an enterocyte
  • Fe3+ in nonheme iron (from plant products) where it’s usually reduced to Fe2+ by ferric reductase (activated further by Vitamin C)
40
Q

What form is iron in in the enterocyte cell?

A
  • Iron is reduced or oxidized as needed in the enterocyte (But remember it can only enter the cell through the apical membrane as Fe2+).
  • The Fe3+ is used in ferritin production as storage and degrades into hemosiderosis
  • Iron as Fe2+ often exits cell through the basolateral membrane through a Ferroportin Channel
41
Q

What form is iron in in the blood?

A
  • Fe2+ that enters the blood through the ferroportin channel is oxidized into Fe3 and used in the production of Transferin, which is a transporter activated by low storages of iron, and inhibited by high storages of iron.
  • The Transferrin helps transport iron to liver, spleen, and bone marrow.
42
Q

What is Basal Metabolic Rate?

A

BMR - Energy required to maintain life

  • The functioning of lungs, kidneys, and brain
  • The pumping of the heart
  • Maintenance of ionic gradients across membranes
  • Reactions of biochemical pathways
  • Obviously increased with more strenuous activity
43
Q

Define Metabolism?

A
  • A linked series of chemical reactions that begins with a particular molecule and converts it into some other molecule or molecules in a carefully defined fashion
  • Pathways are interdependent and their activity is coordinated by sensitive means of communication in which allosteric enzymes are predominant.
  • Short Version: Glucose is converted to pyruvate. In anaerobic conditions, Pyruvate becomes lactate. In aerobic conditions, pyruvate becomes acetyl-CoA.
44
Q

If you’re struggling so much with the nucleotide bases, then for fuck’s sake, learn to at least draw adenine now.

A

Since it’s a part of ATP. It’s a purine crown with Two Nitrogens and an unshared double bond on the left side, a paired double bond between it’s other half, and two nitrogens with neighboring double bonds on the hexa side. And an amine branching off for the fuck of it.

45
Q

How much energy can a mol of ATP produce?

A

Somewhere between 7-11 kcalories per mol.

46
Q

What is the “thing” about ATP that makes it such a good energy holder.

A
  • Phosphoryl transfer potential, good for cell energy transferring.
  • Also found in PEP (phosphoenolpyruvate), Creatine phosphate, and 1,3-Biphosphoglycerate. (1,3-BPG)
47
Q

What is the drawback of using ATP

A

It has to be used “immediately” upon it’s reaction. The body only has about 100 grams of ATP at any given time because it doesn’t even produce it until it’s ready.

48
Q

Don’t fuck this up:

What is the rule about potential energy based on oxidation?

A
  • The more reduced a carbon is to begin with, the more free energy is released by its oxidation (So less is more)
  • From most energy to least: Methanol, Aldehyde, Carboxylic Acid, CO2.
49
Q

What are the “Three stages” of Digestion

A
  • Stage One: Break that shit down! Degradation and absorption. No energy is extracted yet.
  • Stage Two: Sugars and fatty acids are converted to acetyl CoA. Amino acids just get used throughout. Some ATP is produced in glycolysis
  • Stage Three: Acetyl CoA is used in aerobic reaction (most ATP is produced here)
50
Q

What do NADH and NADPH carry and what are it’s vitamin precursors.

A

Carries electrons, niacin precursor

51
Q

What do FADH carry and what is it’s vitamin precursor

A

Carries electrons, Riboflavin precursor

52
Q

What does Conenzyme A carry and what is it’s vitamin precursor

A

Carries Acyl group, Pantothenate precursor.

53
Q

What does the tetrahydrofolate carrry and what is it’s precursor?

A

Carries single-carbon units, and Folate precursor

54
Q

What do nucleoside triphosphates carry?

A

Nucleotides

55
Q

Know how to draw Vitamin B2. What kind of reaction does it normally carry out as a reaction and what is it’s coenzyme?

A

Coenzyme is FAD and does oxidation-reduction reactions

56
Q

Know how to draw B3 and what coenzyme and reaction it causes

A

Conenzyme is NAD+ and performs oxidation-reduction reaction

57
Q

Know how to draw B5 and know what coenzyme and reaction it causes

A

Coenzyme is CoA and performs Acyl-group transfers

58
Q

Know how to draw B6 and know what conezyme and reaction it causes

A

Conezyme Pyridoxical Phosphate and causes group transfers to or from amino acids.

59
Q

Prepare those chegg flashcards. Know how to recognize Vitamin K1, A, E, and D2.

A

FML

60
Q

What are the 3 major ways metabolic processes are regulated?

A
  1. Controlling the amount of enzymes availbable through transcription/signaling
  2. Controlling catalytic activity through feedback inhibition - conformation/modification
  3. Controlling the accessibility of substrates through compartmentalization of pathways