Metabolism Flashcards

(60 cards)

1
Q

Catabolism def

A

Breaking down larger molecules to release free energy and small molecules

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2
Q

What is the energy from catabolism used for (2)

A
  1. Drive cellular processes
  2. Build molecules
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3
Q

Anabolism def

A

Using energy to build cell components

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4
Q

Anabolism role in disorder

A

Reduce entropy to create order

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5
Q

Metabolism def

A

Balance between catabolism and anabolism

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6
Q

What 4 biomolecules make up the human diet

A

Proteins, nucleic acid, polysaccharides and fats

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7
Q

Digestion reduces these 4 biomolecules to what monomers

A

Amino acids, nucleotides, monosaccharides, fatty acids

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8
Q

Amylases

A

Starch enzymes that are Hydrolases

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9
Q

How do amylases work?

A

break the bond connecting glucose polymers to monomeric carbohydrates

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10
Q

What digests starch

A

Amylases

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11
Q

What digests proteins

A

Proteases

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12
Q

How do proteases work?

A

Hydrolysis peptide bonds to release AA’s

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13
Q

What are Fatty acids digested by?

A

Lipases

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14
Q

How are proteins degraded inside the cell

A

By lysosome

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15
Q

What is a lysosome

A

Organelle constraining proteases and hydrolytic enzymes

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16
Q

Why do proteins need to be degraded?

A

Because the are abnormal or because their concentration must be regulated

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17
Q

What type of proteins do lysosomes degrade?

A

Extracellular or degradative enzymes

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18
Q

How are proteins degraded inside the cells?

A

By the proteasome core

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19
Q

What is a proteasome?

A

Barrel shaped multisubunit protein complex (protease) in the cytoplasm that targets intracellular proteins

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20
Q

What is ubiquitin

A

A small protein that is transferred to the Lys side chain of the target protein so it can be degregated

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21
Q

How do ubiquitins degrade proteins

A

Once 4 ubiquitins are added, the polypeptide is unfolded and enters the proteasome; active sites than cleave into small pepetides

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22
Q

What assists ubiquitins in unfolding the protein

A

ATP hydrolysis (ATP —> ADP +P)

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23
Q

Role of Vitamin C

A

Antioxidant and a cofactor for the enzyme that hydroxylates proline residues in collagen

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24
Q

Vitamin C deficiency

A

Scurvy

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25
Vitamin C deficiency
Scurvy
26
What is vitamin B1
Thiamine
27
What is thiamine
A cofactor for the pyruvate dehydrogenase complex and a-ketoglutarate dehydrogenase
28
What is thiamine
A cofactor for the pyruvate dehydrogenase complex and a-ketoglutarate dehydrogenase
29
What is a B1 deficiency
Beriberi: Weakness and leg swelling
30
What is a B1 deficiency
Beriberi: Weakness and leg swelling
31
What is B3
Niacin
32
Niacin
Precursor for NADP+ and NADPH
33
What does a B3 deficiency lead to?
Pellagra: 4 D’s (diarrhea, dermatitis, dementia and death)
34
Nicotinamine adenine dinucleotide (NAD+/NADH)
Water soluble 2 e- carrier
35
What is the significance of the phosphorylated form (NADP+/NADPH)
Used as a redox cofactor in biosynthetic pathways (NADP+ is oxidized and NADPH is reduced)
36
Ubiquinone (Coenzyme Q)
Mobile electron carrier that receives e- from a prosthetic group; Lipid soluble 1 e- (GH) or 2 e- (QH2) carrier
37
What is B2
Riboflavin
38
Riboflavin
Precursor to forming flavins
39
Flavins
Prosthetic group that can carry 1 e- or 2 e-
40
How are fatty acids stored
As triglycerides
41
How is glucose stored
In the liver and muscles as glycogen
42
What bonds store energy in reduced cofactors?
Phosphoanhydride bonds (ATP) or thioester bonds (acetyl CoA)
43
What happens to excess Amino Acids?
Can be broken down and converted to carbohydrate to be stored as glycogen or as acetyl units and stored as fat
44
How does the liver break down glycogen to release glucose?
Catalyzed by glycogen phosphorylase ; phosphate removed before the release in the blood
45
Catabolism involves doing what to carbon
Oxidizing carbon; replaces C-H with C-O
46
Anabolism involves doing what to carbon
Reducing carbon; replacing C-O with C-H
47
How are electrons passed in oxidation?
Passed as an H atom (proton and 1 e-) or as a H- (hydride; proton and 2 e-)
48
Oxidation
Loss of electrons
49
Reduction
Gain of electrons
50
Cofactors
Temporary carriers of e- such as NAD+ or NADP+ (oxidized form)
51
Metabolites
2-3 carbon intermediates that are products of catabolic pathways and precursors for anabolic pathways
52
What occurs at equilibrium
No net chance in the concentration
53
What occurs when the system is not at equilibrium?
Reactants move to reach equilibrium values
54
Delta G^o’
Standard free energy for a reaction in STP;
55
Delta G with no superscripts
Actual change in the living cell
56
What is the purpose of ATP hydrolysis?
Products of hydrolysis are more stable than reactants because the negative charges are dispersed; products have higher resonance stabilization (greater deloactization of electrons)
57
How are metabolic pathways often regulated
At steps with very negative delta G (irreversible)
58
What occurs at steps with a delta G near zero
They are reversible and the direction of the net rxn depends on the concentration of reactants and products
59
When are irreversible steps most likely to occur?
Early in a metabolic pathway to commit a metabolite to the pathway
60
What is used in chemical rxns to make the overall process favorable
Energy currency