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Biochemistry/Physiology > Quiz 6 - Glycolysis, Citric Acid Cycle, Oxidative Phosphorylation > Flashcards

Quiz 6 - Glycolysis, Citric Acid Cycle, Oxidative Phosphorylation Flashcards

1
Q

Cellular respiration

A

Cellular pathways that synthesize ATP by moving electrons from glucose to O2.
Gives off CO2, requires O2, has both anaerobic and aerobic processes

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2
Q

Glycolysis

A

Anaerobic ATP and electron carrier reduction.

NAD+ is electron acceptor, must be maintained

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3
Q

When/where is glycolyis alone the source of energy?

A

Erythrocytes (lack mitochondria)
Cancer cells
Anaerobic bacteria

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4
Q

Glycolysis preparatory phase

A

Glucose + Hexokinase + ATP > G6P + phosphohexose isomerase > F6P + Phosphofructokinase-1 > F16BP + Aldolase > G3P + DHaP

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5
Q

Triose phosphate isomerase

A

Converts Dihydroxyacetone Phosphate into Glyceraldehyde 3 phosphate

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6
Q

Glycolysis Payoff phase

A

G3P + G3P dehydrogenase + NAD+ > (NADH) 13BPG + Phosphoglycerate Kinase + ADP > (ATP) 3 PG + Phosphoglycerate mutase > 2 PG + Enolase > PEP + pyruvate kinase + ADP > (ATP) Pyruvate

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7
Q

Net balance of glycolysis

A

2 Pyruvate
2 ATP
2 NADH + H+

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8
Q

Other sources of Glycolysis molecules

A

Different sugars can be modified to become different steps of glycolysis

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9
Q

Diabetes mellitus types

A

Type 1 - lack of cells that produce insulin

Type 2 - cellular insensitivity to insulin

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10
Q

How do insulin and glucagon balance cell glucose levels?

A

Insulin leads to synthesis of glycolytic enzymes, brings glucose into cells
Glucagon increases enzymes that cause gluconeogenesis and glycogen synthesis
Interplay between these processes balances

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11
Q

Possible fates of pyruvate

A

Aerobic conditions - Conversion into Acetyl-CoA

Anaerobic conditions - conversion into lactate or ethanol via fermentation

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12
Q

Purpose of Fermentation

A

Regenerates NAD+ in anaerobic conditions to allow glycolysis to continue
Lactate is electron acceptor of NADH

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13
Q

Cori Cycle

A

Lactate from muscles enters bloodstream, goes to liver, where it is converted to glucose via gluconeogenesis

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14
Q

Pentose phosphate pathway

A

Lack of NADPH leads to this pathway to create more NADPH and ribose sugars

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15
Q

Ribose sugars

A

Nucleotides, ATP, FAD, Coenzyme A

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16
Q

NADPH

A

Necessary for reductive biosynthesis and free radical protection.

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17
Q

Where do steps of respiration occur

A

Glycolysis - cytoplasm

Pyruvate&raquo_space; Electron transport chain - Mitochondria

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18
Q

How do mitochondria affect apoptosis?

A

DNA damage, developmental signals, stress and reactive oxygen species lead to disruption of mitochondria membrane, releasing cytochromes and other contents that activate a chain of proteins. Activation of Caspase proteins lead to cell death.

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19
Q

Pyruvate conversion to Acetyl-CoA

A

Pyruvate + Pyruvate Dehydrogenase Complex + NAD+ > Acetyl-CoA + CO2 + NADH

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20
Q

Citric Acid Cycle net production per turn

A

3 NADH
2 CO2
1 GTP (ATP)
1 FADH2

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21
Q

Citric acid cycle

A

OxA + Acetyl-CoA + Citrate Synthase > Citrate + aconitase > Isoscitrate + Isocitrate dehydrogenase > (CO2 + NADH) alpha ketoglutarate + akg dehydrogenase > (CO2 + NADH) Succinyl-CoA + Succinyl-CoA synthase > (GTP) Succinate + succinate dehydrogenase > (FADH2) Fumarate + fumarase > malate + malate dehydrogenase > (NADH) OxA

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22
Q

Synthetic pathway

A

Different substrates along the pathway can be pulled to create other products like amino acids, nucleic acids, fatty acids, gluconeogenesis, neurotransmitters, hemes

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23
Q

Oxidative Phosphorylation

A

Occurs in between inner mitochondrial membrane and the matrix. Electrons from glycolysis and citric acid cycle are moved through proteins to phosphorylate ADP (create ATP)

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24
Q

Regulation of Phosphofructokinase-1

A

Presence of ATP and/or Citrate inhibits PFK-1
Presence of ADP and/or AMP promotes PFK-1
Insulin promotes synthesis of PFK-1
Glucagon inhibits synthesis of PFK-1

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25
Q

Pyruvate dehydrogenase complex

A

3 cooperative proteins that convert Pyruvate into Acetyl-CoA. Utilizes an internal acyl lipolysine to transfer acetyl group from pyruvate to the CoA

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26
Q

Regulation of citric acid cycle

A

Allosteric regulation of enzymes. Regulated at most exergonic steps. Presence of ADP promotes, Presence of ATP inhibits
Mass action regulates function - too much product slows, not enough speeds up

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27
Q

Ubiquinone

A

Coenzyme Q - carries both electrons and protons (QH2)

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28
Q

Cytochromes

A

Only accepts electrons

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29
Q

Iron-Sulfur proteins

A

Only accepts electrons, found within complexes

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30
Q

Regulation of Respiratory chain

A

Allosteric regulation. Too much ATP or NAD+ inhibits

Excess ADP promotes

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31
Q

Reactive Oxygen species formation

A

Buildup of ubiquinone can cause transfer of electrons onto O2, creating free radicals.
Mitochondria not making ATP due to lack of O2 or ADP, or excess of NADH promotes formation of ROS

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32
Q

Pepsin

A

Active form of pepsinogen. A protease that hydrolyzes Phe, Trp, Tyr polypeptide bonds

33
Q

Secreten

A

Stimulates release of bicarbonate from the pancreas

34
Q

Trypsin, Chymotrypsin, Carboxypeptidase

A

Proteases that break down proteins

35
Q

Three fates of dietary amino acids

A
  1. Used for synthesis within cells
  2. Catabolized for energy within cells
  3. Transported to the liver and excreted
36
Q

Deamination

A

Amino acids from ingested protein, alanine from muscle and glutamine from muscle and tissues enter cycle to become glutamate. NH4+ then removed to urea

37
Q

Amine group carriers

A

Glutamate
Aspartate
Glutamine
Alanine

38
Q

Ammonia Toxicity

A

Ammonia disregulates K+. Is a diffusible gas that can cross the blood brain barrier, disrupts astrocyte K+ uptake and prevents GABA inhibition. This causes neuronal hyperactivity, seizures, oxidative stress, death

39
Q

Transaminase reactions

A

Amino acid catabolism. Important for oxidation and uric acid cycle. Amine group transferred from amino acid to alpha-ketoglutarate to create glutamate

40
Q

One-Carbon Transfers

A

Amino acid catabolism. Puts carbons back on to put molecules back into the citric acid cycle.

41
Q

How is intracellular ammonia buffered?

A

By converting glutamate to glutamine. Done by glutamine transport or glucose-alanine cycle

42
Q

Glutamine transport

A

Glutamate turned into glutamine, moved from body cells to liver, then converted back into glutamate. NH4+ excreted in urea

43
Q

Glucose-Alanine Cycle

A

Like Cori cycle. Primarily used by muscle. Pyruvate is given the amino group, brought to liver as Alanine, then converted back into pyruvate. NH4+ excreted as urea

44
Q

Urea Cycle

A

Prep phase: Glutamate, Glutamine, provide NH+ to Carbamoyl phosphate, Oxaloacetate takes NH+ to become Aspartate
Cycle: Carbamoyl phosphate passes N to Ornithine to become citrulline. Aspartate adds another N to become arginosuccinate. Fumarate removed to become arginine, then urea removed to become ornithine.

45
Q

Urea cycle regulated

A

Increased synthesis of enzymes

Allosteric carbonyl posphate synthetase 1 regulation

46
Q

Aspartate-arginino-succinate shunt

A

Ties citric acid cycle and urea cycle at aspartate

47
Q

Ketogenic amino acids

A 
Leucine
Lysine
Phenylalanine
Tryptophan
Tyrosine
Isoleucine
Threonine
48
Q

Glucogenic

A 
Arginine
Glutamine
Histidine
Proline
Glutamate
Isoleucine
Methionine
Threonine
Valine
Phenylalanine
Tyrosine
Alanine
Cysteine
Glycine
Serine
Tryptophan
Asparagine
Aspartate
49
Q

CoFactors for one-carbon transfer reactions

A 
Biotin
Tetrahydrofolate
adoMet
- One-carbon group donors or recipients
- Vitamins
50
Q

Which 6 amino acids are degraded to pyruvate

A 
Tryptophan
Alanine
Cysteine
Serine
Glycine
Threonine
- energy-rich AAs
SGT CAT is a PYRat
51
Q

Which 7 amino acids are degraded to Acetyl-CoA?

A 
Tryptophan
Lysine
Phenylalanine
Tyrosine
Leucine
Isoleucine
Threonine
TTT PILL
All ketogenic
52
Q

Which 5 amino acids are degraded to alpha-ketoglutarate?

A 
Glutamate
Glutamine
Proline
Arginine
Histidine
Go get Harry potters altoids
53
Q

Which 4 amino acids are degraded to Succinyl-CoA?

A 
Methionine
Isoleucine
Valine
Threonine
Sucks that mother is very talkative
54
Q

Which 2 amino acids are degraded to Oxaloacetate?

A

Asparagine
Aspartate
Oxen or Asses

55
Q

Which 9 amino acids are essential?

A 
Histidine
Isoleucine
Leucine
Lysine
Methionine
Phenylalanine
Threonine
Tryptophan
Valine
PVT TIM HaLL
56
Q

What are the 7 source molecules for amino acids?

A 
3-Phosphoglycerate
Phosphoenolpyruvate
Pyruvate
Ribose 5-phosphate
Erythrose 6-phosphate
Oxaloacetate
Alpha-Ketoglutarate
- All parts of glycolysis, pentose phosphate pathway and citric acid cycle
57
Q

Intron

A

Non-coding segments of genes, spliced from mRNA

58
Q

Exon

A

Encodes for amino acid sequence

59
Q

How much DNA codes for proteins?

60
Q

How many genes are in human DNA

A

about 25,000

61
Q

Which strand is the mRNA created from

A

The template strand, 3’ to 5’

62
Q

RNA polymerase I

A

Synthesizes rRNA

63
Q

RNA polymerase II

A

Synthesizes mRNA

64
Q

RNA polymerase III

A

Synthesizes tRNA

65
Q

Transcription of mRNA

A

DNA binds to DNA polymerase, separates DNA strands, RNA polymerization begins after CTD is phosphorylated. Once RNA complete, elongation factors and Phosphates removed

66
Q

Negative Regulation

A
  1. Molecular signal causes dissociation of repressor from DNA, inducing transcription
  2. Molecular signal causes binding of repressor to DNA, inhibiting transcription
67
Q

Positive Regulation

A
  1. Molecular signal causes dissociation of activator from DNA, inhibiting transcription
  2. Molecular signal causes binding of activator to DNA inducing transcription
68
Q

RNA processing

A

5’ Cap addition - stabilizes 5’ end
Splicing - Spliceosome proteins remove introns, keep exons
Termination and tail - Polyadenylation factors add poly-A talk that stabilizes RNA for splicing and translation

69
Q

Splicing variability

A

Exons can be rearranged, spliced different ways to create different products

70
Q

Nuclear Export

A

Poly-A stabilizes RNA, export factors and proteins bind to poly-A, complex moves out to nuclear pore complex, out into cytosol

71
Q

Codons

A

Triplets of nucleotides that specify amino acid in polypeptide chain
AUG codes for Met, start codon
Third base has variability (“Wobble”) to resist mutation

72
Q

Aminoacylation

A

Addition of amino acid to tRNA

73
Q

Eukaryotic Ribosome

A

60S + 40S subunits = 80S ribosome

74
Q

Initiation

A

ATP/GTP hydrolysis drives initiation, Ribosome subunits come together around 5’ end of mRNA

75
Q

Elongation

A

Growing chain attached to middle (P) site, incoming tRNA binds to A site, tRNA exits from E site.
GTP hydrolysis dependent
Reads mRNA 5’ to 3’, creates polypeptide N terminus to C terminus

76
Q

Termination

A

End codon triggers eukaryotic releasing factor and GTP to release polypeptide from tRNA

77
Q

Nuclear localization sequence

A

Sequence in protein that triggers Importin (alpha and beta subunit) to bind to protein and bring it into the nucleus though the nuclear pore complexes, allow nuclear effects

78
Q

Signal Recognition Peptide

A

Recognizes signal sequence on developing protein, binds to ribosome, brings ribosome to ER membrane. Protein is extruded into ER lumen for future packaging and processing.

79
Q

Degradation of proteins

A

Ubiquitin is post-translational modification. Polyubiquitination will be tag for further processing
Proteosome will digest poly-ubiquitinated proteins in the cytoplasm
Lysosome will digest proteins that reach the late endosome stage of the endocytic pathway

Biochemistry/Physiology (10 decks)

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