Module 11 Flashcards

(30 cards)

1
Q

What is catabolism vs anabolism?

A

Catabolism breaks down big molecules for energy
Anabolism is the synthesis of bigger molecules from small molecules

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2
Q

What two molecules are convergence points for sugar fatty acid, and amino acid metabolism?

A

pyruvate, Acetyl-CoA

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3
Q

What is the key chemical process that is happening to sugar-derived metabolites during glycolysis and the citric acid cycle?

A

stepwise oxidation of molecules

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4
Q

What molecules are being reduced as sugar-derived metabolites are modified?

A

NAD+ gets turned into NADH and FADH2

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5
Q

In what form is carbon released when it is fully oxidized

A

CO2

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6
Q

What process is yielding ATP during glycolysis and the citric acid cycle?

A

substrate level phosphorylation

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7
Q

What is oxidized in during oxidative phosphorylation?

A

NADH, FADH2 gets turned into NAD+

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8
Q

What is being reduced during oxidative phosphorylation?

A

metabolites, it’s a anabolic reaction

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9
Q

What is produced as a product of the transport of electrons from NADH and FADH2 to O2?

A

proton gradient

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10
Q

What is the proton gradient coupled to?

A

ATP synthase for ATP synthesis

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11
Q

What are four generalizations of catabolic pathways?

A

oxidative process of fuel molecules
generate ATP
generate reduced electron carriers
converse on intermediates (pyruvate, Acetyl-CoA)

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12
Q

What are two generalizations of anabolic pathways?

A

reductive biosynthesis (and using NADPH)
use ATP

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13
Q

What does a very negative delta G step mean in a reaction?

A

irreversible, determines the direction of the entire pathway

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14
Q

What are control points?

A

steps that have a very negative delta G, irreversible

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15
Q

What is allosteric activation?

A

effectors that bind to a site away from the active site, stabilize the R state and increase affinity

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16
Q

What is allosteric inhibition?

A

inhibitors that bind to a site away from the active site, stabilize the T state, decrease affinity

17
Q

What is product inhibiton?

A

immediate product of enzyme competes with substrate from binding to active site

18
Q

What is covalent modification?

A

adding a covalent bond to change enzyme activity, such as phosphorylation

19
Q

What is regulation of enzyme availability?

A

Transcription controlled
Sequestration- inhibitory protein binds to enzyme, making it unavailable

20
Q

What is a substrate cycle?

A

sets of opposing cycles of catabolic/anabolic pathways

21
Q

Glycolysis and gluconeogenesis are opposing pathways. What reactions do they share?

A

the ones that are near equilibrium (delta G near 0)

22
Q

What type of bonds hold up ATP/ADP/AMP?

A

phosphoanhydride bonds

23
Q

What are the three reasons why transferring a phosphoryl group from ATP has a highly negative delta G?

A

resonance stabilization is greater in products
electrostatic repulsion is reduced after hydrolysis
hydrolysis products are better solvated

24
Q

What are the three ways that ATP can be used as energy currency?

A

transfer phosphate groups to metabolites to power endergonic reactions
transfer phosphoryl groups to proteins to make conformational changes
regenerate nucleotide triphosphate

25
What are the two main ways of regenerating ATP from ADP?
Substrate level phosphorylation Oxidative Phosphorylation
26
What is substrate-level phosphorylation?
transfer of phosphoryl group from a phosphorylated substrate to ADP or another NDP (USE THE TABLE)
27
What does oxidative phosphorylation and where does it occur?
in the mitochondria, use the potential energy from a proton gradient to power the endergonic transfer of Pi to ADP
28
How is the proton gradient formed in oxidative phosphorylation?
oxidation of NADH and FADH2
29
What is NAD+ derived from?
vitamin B3 (niacin)
30
What is the difference between NADH and FADH2?
NADH carries two electrons FADH2 carries two electrons, but can carry 1 in a stepwise manner