Metabolism Review Flashcards

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1
Q

All chemical reactions of a cell/organism

A

Metabolism

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2
Q

Series of biochemical reactions that convert >1 substrate into a final product

A

Metabolic Pathway

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3
Q

Pathway requiring energy to synthesize larger molecules

A

Anabolic

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4
Q

Pathway requiring energy to synthesize larger molecules

A

Anabolic

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5
Q

Pathway that releases energy and breaks down large molecules into small ones

A

Catabolic

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6
Q

Ability to do work

A

Energy

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7
Q

Total amount of energy in the universe is constant; energy cannot be created/destroyed

A

First Law of Thermodynamics

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8
Q

Within each chem. reaction, some energy is lost in a form that is unusable. This results in increased entropy

A

Second Law of Thermodynamics

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9
Q

Amount of energy available to do work (usable energy)

A

Gibb’s Free Energy

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10
Q

Energy is released in a chem. reaction (delta G < 0); products of these reactions have less free energy than substrates

A

Exergonic Reaction

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11
Q

Chem. reaction requires input of energy (delta G > 0); products have more free energy than substrates

A

Endergonic Reaction

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12
Q

What is the main source for activation energy in a cell?

A

Heat energy

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13
Q

Is ATP hydrolysis reversible?

A

Yes

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14
Q

What energy does the sodium potassium pump use?

A

Energy from exergonic ATP hydrolysis

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15
Q

How many sodium ions exit the cell in the NaK+ pump?

A

3

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16
Q

How many potassium ions enter the cell in the NaK+ pump?

A

2

17
Q

Catalyst

A

Increases the rate of a reaction without being consumed

18
Q

Why do cellular reactions need catalysts?

A

Activation energies are too high for heat energy from the surroundings to overcome

19
Q

Protein catalysts that bind with reactant molecules to promote chemical processes; very specific and can only catalyse a single reaction

A

Enzyme

20
Q

What is an example of a non-protein enzyme?

A

Ribosomes

21
Q

Chemical reactants to which an enzyme binds

A

Substrate

22
Q

Place on an enzyme where substrate binds

A

Active Site

23
Q

What determines enzyme-substrate specificity?

A

3D shape of enzyme and reactants

24
Q

Mild shift in shape of enzyme/substrate that optimizes reactions; expansion of “lock and key” model

A

Induced Fit

25
Q

What determines the 3D shape of a protein?

A

Amino Acid Sequence

26
Q

How can an enzyme help the substrate reach its transition state?

A
  1. Position two substrates so they align perfectly
  2. Provide an optimal environment within active site
  3. Contort/stress substrate so it’s more likely to react
  4. Temporarily react with substrate
27
Q

How can enzymes be regulated?

A
  1. Modifications to temp. or pH
  2. Production of molecules that inhibit/promote enzyme function
  3. Availability of coenzymes or cofactors
28
Q

Have a similar shape to substrate that competes with it for the active site; slow reactions without affecting maximal rate

A

Competitive Inhibitors

29
Q

Bind to the enzyme at a different location than the active site, causing a slower reaction rate; slow reaction rates and reduce maximal rates

A

Noncompetitive Inhibitors

30
Q

Modify active site of an enzyme so substrate binding is reduced/prevented

A

Allosteric Inhibitors

31
Q

Modify active site of an enzyme so affinity for substrate increases

A

Allosteric Activators

32
Q

Inorganic helper ions (iron or magnesium)

A

Cofactors

33
Q

Organic helper molecules (vitamin C)

A

Coenzymes

34
Q

Enzymes required for certain cellular processes are housed separately inside structures with their substrates

A

Compartmentalization

35
Q

End product of a pathway inhibits an upstream step; important regulatory mechanism in cells

A

Feedback inhibition