slide 8 Flashcards

1
Q

Metabolism

A

The Energy of Life

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2
Q

The living cell

A

• Is a miniature factory where thousands of
reactions occur
• Converts energy in many ways

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3
Q

Metabolism

A
  • Includes all of an organism’s chemical reactions
  • Is a network of pathways
  • Arises from interactions between molecules
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4
Q

An organism’s metabolism transforms

A

matter and

energy subject to the laws of thermodynamics

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5
Q

A metabolic pathway has many steps
These begin with a specific molecule or
molecules and end with a specific product

A

Each step is facilitated by a specific catalyst

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6
Q

A catalyst

A
is a substance that
accelerates the rate of a
chemical reaction without
affecting the products of the
reaction and without itself
being altered or consumed by
the reaction.
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7
Q

enzymes.

A

The catalysts in living
organisms are proteins called
enzymes

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8
Q

Metabolic pathways balance supply and demand.

A

• Speed up reactions when not enough product is present
• Slow down reactions when a surplus of product is present
• Products in one set of reactions are the starting molecules
in other sets of reactions.

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9
Q

Catabolic pathways

A

• Break complex molecules into simpler ones
• Release energy
e.g. hydrolysis
reactions

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10
Q

Anabolic pathways

A

• Build complicated molecules from simpler ones
• Consume energy
e.g. dehydration
reactions

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11
Q

Energy

A

– Is the capacity to cause change

– Exists in various forms, some can perform work

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12
Q

Kinetic energy

A

– Is the energy associated with motion

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13
Q

Potential energy

A

– Is stored in the location of matter
– Includes chemical energy stored in molecular
structure (chemical bonds)

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14
Q

There are many forms of energy
(light, heat, chemical, electrical,
etc.) but only two states:

A

Potential energy is stored energy

Kinetic energy is the energy
present in the motion of a body

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15
Q

1st law of thermodynamics

A
  • energy is neither
    created or destroyed, but can be transformed
    from one form to another
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16
Q

2nd law of thermodynamics -

A

physical systems
tend to proceed to a state of greater disorder
(entropy)

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17
Q

Energy enters a biological system

A

is spent, transformed, and lost as heat.

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18
Q

Gibbs free energy is the energy available for

work in a system at uniform temperature.

A

Josiah Willard Gibbs

1839-1903

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19
Q

The free-energy change of a reaction tells us

whether the reaction occurs spontaneously.

A

During a spontaneous change free energy

decreases and the stability of a system increases

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20
Q

Spontaneous change:

A
- The free energy of the system
decreases
- The system becomes more stable
- The released free energy can be
harnessed to do work
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21
Q

exergonic reactions.

A

The majority of the reactions in living cells release

free energy and are called exergonic reactions.

22
Q

endergonic reactions.

A

Many important reactions in cells, however,
require the addition of energy and are called
endergonic reactions

23
Q

equilibrium,

A

Reactions in a closed system eventually reach

equilibrium, and can do no more work.

24
Q

Equilibrium and Metabolism

A
Cells in our body
experience a constant flow
of materials in and out,
preventing metabolic
pathways from reaching
equilibrium
25
Cellular metabolism
is an open, multi-step process
26
Entropy (disorder)
is decreased in living organisms by metabolic processes, but this results in increased entropy of the larger system.
27
Entropy (disorder)
is decreased in living organisms by metabolic processes, but this results in increased entropy of the larger system.
28
• Just because a reaction is exergonic, and therefore | occurs spontaneously, does not mean it occurs rapidly.
• Even exergonic reactions require destabilization of | chemical bonds through the input of activation energy
29
Enzymes catalyze
reactions | by lowering the EA barrier
30
enzyme’s substrate.
The reactant that an enzyme acts on is | called the enzyme’s substrate.
31
enzyme-substrate complex
The enzyme binds to its substrate, forming | an enzyme-substrate complex.
32
The active site
is the region on the enzyme | where the substrate binds
33
The active site can lower an EA barrier by
* Orienting substrates correctly * Straining substrate bonds * Providing a favorable microenvironment * Covalently bonding to the substrate
34
Each enzyme has an optimal temperature | in which it can function properly
Each enzyme has an optimal pH | in which it can function properly
35
Cofactors
are nonprotein enzyme helpers
36
Cofactors may be
inorganic (such as a metal | in ionic form) or organic
37
coenzyme
An organic cofactor is called a coenzyme | Coenzymes include vitamins.
38
Competitive inhibitors
bind to the active site of | an enzyme, competing with the substrate.
39
Noncompetitive inhibitors
bind to another part of an enzyme, causing the enzyme to change shape and making the active site less effective.
40
Allosteric regulation
occurs when a regulatory molecule binds to a protein at one site and affects the protein’s function at another site.
41
Metabolism can be regulated by switching
on or off the genes that encode specific enzymes or by regulating the activity of enzymes
42
Cooperativity
is a form of allosteric regulation | that can amplify enzyme activity
43
Cooperativity
is a form of allosteric regulation | that can amplify enzyme activity
44
One substrate molecule primes
an enzyme to act | on additional substrate molecules more readily.
45
Allosteric regulators are attractive drug candidates for enzyme regulation because of their specificity
Inhibition of proteolytic enzymes called caspases may help management of inappropriate inflammatory responses
46
In feedback inhibition,
the end product of a | metabolic pathway shuts down the pathway
47
Feedback inhibition prevents a cell from wasting
chemical resources by synthesizing more product | than is needed
48
Location of Enzymes
Structures within the cell help bring | order to metabolic pathways.
49
Some enzymes act as structural | components of membranes
In eukaryotic cells, some enzymes | reside in specific organelles.
50
Changes (mutations) in genes lead to changes | in amino acid composition of an enzyme
Altered amino acids in enzymes may alter their | substrate specificity
51
Lab experiments have been successful in | altering the function
of β–galactosidase from | the bacterium E. coli.