topic 8 Flashcards

1
Q

anabolic processes are where energy is

A

stored

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
2
Q

catabolic processes are where energy is

A

released

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
3
Q

catabolic pathways ____

A

breakdown complex molecules into simpler compounds

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
4
Q

anabolic pathways ____

A

synthesize complicated molecules from simpler ones

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
5
Q

photosynthesis is an example of (catabolic or anabolic)?

A

anabolic pathway

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
6
Q

cellular respiration is an example of?

A

catabolic pathway

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
7
Q

the first law of thermodynamics states that ____

A

energy cannot be created or destroyed (but can be transferred/transformed)

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
8
Q

the second law of thermodynamics states that ____

A

spontaneous changes that do not require outside energy (no energy consumption) increase the entropy (disorder)
of the universe

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
9
Q

what is free energy? (ΔG)

A

a living system’s energy that can do work under cellular conditions

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
10
Q

what are exergonic reactions?

A
  • when ΔG < 0
  • free energy is released
  • spontaneous reactions
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
11
Q

what are endergonic reactions?

A
  • ΔG > 0
  • absorb free energy from their surroundings
  • non-spontaneous reactions
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
12
Q

what is ATP?

A
  • adenosine triphosphate
  • nucleotide that stores energy in phosphate bonds
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
13
Q

what is the function of ATP?

A

provides energy for cellular functions

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
14
Q

ATP powers cellular work by energy coupling; what is energy coupling?

A

the use of an exergonic process to drive an
endergonic one

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
15
Q

what are the 3 main types of endergonic cellular work?

A
  • mechanical
  • transport
  • chemical
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
16
Q

how is ATP an example of mediated energy coupling?

A

ATP hydrolysis provides the energy required for the endergonic reaction to occur

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
17
Q

what is phosphorylation?

A

the transfer of a phosphate to other molecules

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
18
Q

how does ATP undergo mechanical, transport, and chemical work?

A

mechanical - ATP phosphorylates motor proteins

transport - ATP phosphorylates transport proteins

chemical - ATP phosphorylates key reactants

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
19
Q

what is the activation energy Ea?

A

the initial amount of energy need to start a chemical reaction

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
20
Q

what does the activation energy do?

A

it is needed to de-stabilize the structure of the reactants so they can react more easily

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
21
Q

what is denaturation?

A

the loss of a protein’s native conformation due to unravelling => loss of function

22
Q

what are some environmental factors that may affect enzyme activity?

A
  • pH
  • temperature
  • cofactors
23
Q

what are cofactors?

A

non-protein enzyme helpers required for enzyme activity

24
Q

what is an example of an inorganic cofactor?

A

metal ions (ex: Zn, Cu)

25
what are coenzymes? give an example
organic cofactors such as vitamins
26
what are irreversible inhibitors?
bind to an enzyme by covalent bonding => inhibition is irreversible
27
examples of irreversible inhibitors of the nervous sytsem?
sarin, DDT, parathion
28
what are penicillin derivatives?
inhibit the enzyme transpeptidase that synthesizes the bacterial cell wall peptidoglycan
29
what are reversible inhibitors?
bind to enzymes by weak bonds (non-covalent interactions: H-bonds, hydrophobic interactions, ionic bonds) => inhibition is reversible
30
what are the 2 types of reversible inhibitors?
- competitive inhibitors - non-competitive inhibitors
31
what are competitive inhibitors?
-compete with the substrate - bind to the active site of an enzyme (weak binding) to inhibit substrate binding
32
what are non-competitive inhibitors?
- bind to another part of an enzyme not to the active site - change the shape of the enzyme - inhibit the function of the enzyme
33
in ONLY competitive inhibition, how can inhibition be overcome?
by adding excess substrate
34
what are 2 basic methods of enzyme regulation?
1. regulation of gene expression 2. feedback inhibition (by allosteric regulation)
35
what is feedback inhibition?
- prevents a cell from wasting chemical resources by synthesizing more product than is needed - (end products always inhibits the pathway)
36
give 2 examples of feedback inhibition
1. inhibition of catabolic pathways by ATP 2. inhibition of anabolic pathways by their end product (tryptophan)
37
what is allosteric regulation?
- a form of reversible modulation common in enzymes (and proteins) made from polypeptide subunits – can be positive (activation) or negative (inhibition)
38
allosteric activators stabilize the ____
active form of the enzyme
39
allosteric inhibitors stabilize the ____
inactive form of the enzyme
40
what is homotropic allosteric regulation?
binding of substrate to active site of one subunit locks all subunits into active conformation
41
what is heterotropic allosteric regulation?
binding of regulatory molecules to sites other than the active sites
42
what is cooperativity?
special form of positive allosteric regulation (activation) that can amplify enzyme activity
43
given an example of cooperativity
- O2 binding to hemoglobin - the binding of substrate (oxygen) at one subunit increases the binding affinity of the other subunits (oxygen= allosteric activator)
44
allosteric inhibitors can be ____
competitive or non-competitive
45
heterotropic allosteric modulator
non-competitive inhibitors + activators
46
give an example of a heterotropic allosteric activator
AMP is a heterotropic allosteric activator of PFK => (phosphofructokinase= glycolysis enzyme)
47
give an example of a heterotropic allosteric inhibitor
CO2 is a heterotropic allosteric inhibitor (noncompetitive inhibitor) of hemoglobin => reduces hemoglobin's affinity for oxygen => oxygen is released in the tissues
48
homotropic allosteric modulator
(competitive inhibitors + activators)
49
give an example of a homotropic allosteric modulator
O2 and CO are homotropic allosteric modulators of hemoglobin
50
O2 is a _____ of hemoglobin
homotropic allosteric activator
51
CO is a _____ of hemoglobin
competitive inhibitor
52
what is the main difference between homotropic and heterotropic allosteric modulators?
heterotropic --> a regulatory molecule that is NOT the enzyme's substrate homotropic --> both a substrate for its target enzyme and a regulatory molecule of the enzyme's activity