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BCHM Exam 3 > Metabolism > Flashcards

Metabolism Flashcards

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
Q

Vitamin C deficiency

A

Scurvy

26
Q

What is vitamin B1

A

Thiamine

27
Q

What is thiamine

A

A cofactor for the pyruvate dehydrogenase complex and a-ketoglutarate dehydrogenase

28
Q

What is thiamine

A

A cofactor for the pyruvate dehydrogenase complex and a-ketoglutarate dehydrogenase

29
Q

What is a B1 deficiency

A

Beriberi: Weakness and leg swelling

30
Q

What is a B1 deficiency

A

Beriberi: Weakness and leg swelling

31
Q

What is B3

A

Niacin

32
Q

Niacin

A

Precursor for NADP+ and NADPH

33
Q

What does a B3 deficiency lead to?

A

Pellagra: 4 D’s (diarrhea, dermatitis, dementia and death)

34
Q

Nicotinamine adenine dinucleotide (NAD+/NADH)

A

Water soluble 2 e- carrier

35
Q

What is the significance of the phosphorylated form (NADP+/NADPH)

A

Used as a redox cofactor in biosynthetic pathways (NADP+ is oxidized and NADPH is reduced)

36
Q

Ubiquinone (Coenzyme Q)

A

Mobile electron carrier that receives e- from a prosthetic group; Lipid soluble 1 e- (GH) or 2 e- (QH2) carrier

37
Q

What is B2

A

Riboflavin

38
Q

Riboflavin

A

Precursor to forming flavins

39
Q

Flavins

A

Prosthetic group that can carry 1 e- or 2 e-

40
Q

How are fatty acids stored

A

As triglycerides

41
Q

How is glucose stored

A

In the liver and muscles as glycogen

42
Q

What bonds store energy in reduced cofactors?

A

Phosphoanhydride bonds (ATP) or thioester bonds (acetyl CoA)

43
Q

What happens to excess Amino Acids?

A

Can be broken down and converted to carbohydrate to be stored as glycogen or as acetyl units and stored as fat

44
Q

How does the liver break down glycogen to release glucose?

A

Catalyzed by glycogen phosphorylase ; phosphate removed before the release in the blood

45
Q

Catabolism involves doing what to carbon

A

Oxidizing carbon; replaces C-H with C-O

46
Q

Anabolism involves doing what to carbon

A

Reducing carbon; replacing C-O with C-H

47
Q

How are electrons passed in oxidation?

A

Passed as an H atom (proton and 1 e-) or as a H- (hydride; proton and 2 e-)

48
Q

Oxidation

A

Loss of electrons

49
Q

Reduction

A

Gain of electrons

50
Q

Cofactors

A

Temporary carriers of e- such as NAD+ or NADP+ (oxidized form)

51
Q

Metabolites

A

2-3 carbon intermediates that are products of catabolic pathways and precursors for anabolic pathways

52
Q

What occurs at equilibrium

A

No net chance in the concentration

53
Q

What occurs when the system is not at equilibrium?

A

Reactants move to reach equilibrium values

54
Q

Delta G^o’

A

Standard free energy for a reaction in STP;

55
Q

Delta G with no superscripts

A

Actual change in the living cell

56
Q

What is the purpose of ATP hydrolysis?

A

Products of hydrolysis are more stable than reactants because the negative charges are dispersed; products have higher resonance stabilization (greater deloactization of electrons)

57
Q

How are metabolic pathways often regulated

A

At steps with very negative delta G (irreversible)

58
Q

What occurs at steps with a delta G near zero

A

They are reversible and the direction of the net rxn depends on the concentration of reactants and products

59
Q

When are irreversible steps most likely to occur?

A

Early in a metabolic pathway to commit a metabolite to the pathway

60
Q

What is used in chemical rxns to make the overall process favorable

A

Energy currency

BCHM Exam 3 (7 decks)

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