Chapter 8 Flashcards

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1
Q

DeltaG and the reaction rate are…?

A

independent.

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2
Q

What is the reaction rate?

A

How quickly a reaction happens.

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3
Q

What does DeltaG tell us?

A

If the reaction will occur without a net input of energy.

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4
Q

How does temperature influence reaction rate?

A

As temp increases so does reaction rate.

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5
Q

How can cells increase or decrease the reaction rate?

A

By manipulating the activation energy.

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6
Q

What is activation energy?

A

The energy you have to invest to get the reactants to the transition state.

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7
Q

What is the transition state?

A

The intermediate state where all the components are separated and ready to collide to form a reaction producing the products.

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8
Q

on the graph displaying a chemical reaction what does it mean if the products are lower than the reactants?
Or if the reactants are lower than the products?

A
  1. ) if the products are the lowest point on the chemical reaction graph the reaction is exergonic or spontaneous.
  2. ) if the products are the higher than the point of the reactants on the chemical reaction graph, the reaction is endergonic or non-spontaneous.
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9
Q

What does lowering the activation energy do?

A

It creates a faster rate of reaction.

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10
Q

How do cells lower activation energy?

A

Via catalyst.

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11
Q

What are enzymes?

A

A class of proteins that serve as a biological catalyst used to lower the activation energy of a reaction, thus increasing the rate of the reaction.

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12
Q

T/f Each is enzyme is the same shape?

A

false, each enzyme has to be shaped perfectly so that it fits each with the reactants or substrates. in order for them to be brought to their transition states.

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13
Q

The correct shaped enzyme paired with correct substrate/reactant = ?

A

the reactants reaching their transition state

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14
Q

What is the portion of the enzyme where the substrates nestle?

A

The active site.

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15
Q

Describe how you can tell the difference between an uncatalyzed and catalyzed reaction?

A

You can give each an increase in substrate concentration.

  • Catalyzed reaction: they initial take up producing massive amounts of products but then slowly tappers off.
  • Uncatalyzed reaction: there is a slow and linear increase in the rate of product formation.
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16
Q

T/F: the same enzyme in two different organism’s will not be exactly the same? Why?

A
  • Those two organisms don’t live in the exact same environments. Proteins fold differently based on environment, therefor the “same” enzymes will have differing structures.
17
Q

Describe the steps of the model of enzyme action?

A
  1. ) Initiation: substrates bind to the active site in a specific orientation, forming an an enzyme-substrate complex
  2. Transition state facilitation: interactions between enzyme and substrate lower the activation energy.
  3. Termination: products have lower affinity for active site and are released. Enzyme is uncharged after the reaction.
18
Q

What is competitive inhibition?

A

cell produces some molecule that is similar enough in shape as the substrate to fit into the active site,
- but it is also different enough in shape that it doesn’t get modified by the active site.
EFFECTIVLY BLOCKING FURTHER SUBSTRATES FROM ENTERING THE ENZYME.

19
Q

Allosteric regulation (inhibition) ?

A

A molecule binds to some other site ( not the active site) and causes the active site to change in shape.
- This in turn allows for the active site to no longer interact with the substrate.

20
Q

Allosteric regulation (activation) ?

A

A molecule binds to some other site ( not the active site) and causes the active site to change in shape.
- This in turn allows for the active site to better intake of the substrates.

21
Q

what are the ways in which an enzyme can be activity regulated?

A
  1. What is competitive inhibition
  2. Allosteric regulation (inhibition)
  3. Allosteric regulation (activation)
22
Q

What is the difference in Allosteric vs Competitive regulation?

A

Allosteric regulation: the molecules that regulates the activity of the enzyme binds to the some other site on the enzyme, rather than the active site like it does in competitive regulation.

23
Q

T/F, an enzyme can simultaneously catalyze an exergonic and endergonic reaction?
Why or why not?

A

True, because: The energy released form the exergonic reaction can be used to drive the endergonic reaction.

24
Q

What is the idea of an enzyme catalyzing an exergonic and endergonic reaction at the same time known as?

A

Energetic coupling

25
Q

What are the two forms of energetic coupling?

A
  1. ) the exergonic reaction is ATP hydrolysis.

2. ) there exergonic reaction is a redox reaction

26
Q

What is a Metabolic Pathway?

A

Is a set of sequential enzyme-catalyzed reactions that culminate the formation of some important biochemical product.

27
Q

What is feedback inhibition?

A

the product of one step in the pathway acts as an allosteric inhibitor of an earlier step

28
Q

What is the retro-evolutionary hypothesis?

A
  • Some key molecule, nucleotide, and some readily available substrate was available in the environment and an enzyme evolved that could take that substrate and turn it into the nucleotide.
  • Now once this has happened for a while selective pressure occurs to make more substrates so the first enzyme can make more of the enzyme 2.
  • this happens repeatedly.