Test 3: Ch. 8 Metabolism Flashcards

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1
Q

BE ABLE TO DRAW OUT THE ATP HYDROLYSIS

A

WHAT HAPPENS?!?!?

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2
Q

Things about exergonic reactions, also what is an example of Exergonic Reactions?

A

1) Example: ATP hydrolysis
2) Energy used to drive endergonic reactions
3) -change in G = free energy (energy available to do work)
4) spontaneous reaction (not necessary explosive)

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3
Q

What generally happens in exergonic reactions?

A

energy is releasing

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4
Q

What does Endergonic Reaction require?

A

Energy

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5
Q

Tell me two things about Endergonic Reaction?

A

1) + change in G

2) non-spontaneous

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6
Q

Enzymes: Catalyst. Tell me two things.

A

1) decrease activation energy needed for reaction (speeds up)
2) recycled

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7
Q

Name some enzymes:

A

1) normally substrate name and “ase”
2) ATPase
3) lactase
4) cellulase
5) peroxidase
6) catecholase
7) kinase

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8
Q

What happens in the active site?

A

1) binds and modifies substrate
2) complementary to substrate (fits like a puzzle)
3) substrate specificity

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9
Q

Look at the diagrams

A

Please, gurrrrlllll

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10
Q

Tell me about activation Energy.

A

1) initial investment of energy headed to start a reaction
2) exergonic- release more energy than what is absorbed initially
3) endergonic - absorb more energy than is released

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11
Q

How does an exergonic graph look like?

A

it eventually rises and then the energy of the products are lower than the energy of the reactions (look at the notes, man)

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12
Q

What does an endergonic graph look like?

A

The energy of the products end up be higher than the energy of the reactions (look at the notes, man)

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13
Q

What does an Exergonic and enzyme look like?

A

a) enzyme lower EA needed to start a reaction
b) however, start and stop at same point
(look at the notes, man)

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14
Q

What also lower the EA of endergonic reactions?

A

Enzymes

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15
Q
  • change in G is different in energy between what two things?`
A

reactants and products

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16
Q

What are CoFactors?

A

1) non-organic molecules that binds to an enzyme
2) it activates the enzyme
3) can control enzyme activity by only providing co-factors when you need it
4) co-factor attaches by ionic bonds

17
Q

Tell me about them Kinases.

A

1) phosphorylate other protein
2) can inhibit or activate the protein
3) Phosphorous is covalently attached to another protein

18
Q

What enzyme changes the shape of molecule?

A

kinase

19
Q

Enzyme activity increases in increase of heat up to a point, why?

A

energy causes energy, enzyme captures substrate, things, then lets go

20
Q

What happens when the temperature of an enzyme is too hot?

A

protein unravels (denatures) and it may have no active site on enzyme

21
Q

Can temporarily denature if not too hot.. why?

A

cooling can allow renaturation

22
Q

What is the optimal temperature for most human enzymes?

A

35 - 37 degrees Celsius

23
Q

What happens if the pH is too acidic in enzyme solution?

A

they repel each other (too many +)

24
Q

What happens if the pH is too acidic in enzyme solution?

A

too many OH-

25
Q

What is the optimal pH?

A

a) 7.4 for most enzymes

b) pepsin (stomach enzyme) works best at pH 2

26
Q

What are the two sites in allosteric enzymes?

A

a) active site binds substrate
b) allosteric site binds to
1) inhibitor (stops enzyme)
2) activator (start enzyme)

27
Q

what is the main purpose of the allosteric enzymes?

A

to regulate enzyme activity

28
Q

what is usually used in a multi reaction pathway?

A

allosteric enzymes

29
Q

what is usually the 1st in the pathway?

A

allosteric enzyme

30
Q

what happens after the 1st pathway thing?

A

the allosteric inhibitor binds and change shape of active site

31
Q

what is generally the last product in pathway?

A

allosteric inhibitor

32
Q

when is D is not present, the enzyme is on or off?

A

on

33
Q

why allosteric?

A

a) makes the system more energy efficient

b) but making too much of “D”

34
Q

there is high energy in phosphate bonds: if you break it what will happen?

A

you will release energy