Metabolism Review Flashcards

(35 cards)

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?

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

20
Q

What is an example of a non-protein enzyme?

21
Q

Chemical reactants to which an enzyme binds

22
Q

Place on an enzyme where substrate binds

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

25
What determines the 3D shape of a protein?
Amino Acid Sequence
26
How can an enzyme help the substrate reach its transition state?
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
How can enzymes be regulated?
1. Modifications to temp. or pH 2. Production of molecules that inhibit/promote enzyme function 3. Availability of coenzymes or cofactors
28
Have a similar shape to substrate that competes with it for the active site; slow reactions without affecting maximal rate
Competitive Inhibitors
29
Bind to the enzyme at a different location than the active site, causing a slower reaction rate; slow reaction rates and reduce maximal rates
Noncompetitive Inhibitors
30
Modify active site of an enzyme so substrate binding is reduced/prevented
Allosteric Inhibitors
31
Modify active site of an enzyme so affinity for substrate increases
Allosteric Activators
32
Inorganic helper ions (iron or magnesium)
Cofactors
33
Organic helper molecules (vitamin C)
Coenzymes
34
Enzymes required for certain cellular processes are housed separately inside structures with their substrates
Compartmentalization
35
End product of a pathway inhibits an upstream step; important regulatory mechanism in cells
Feedback inhibition