chapter 8⚡️ Flashcards

1
Q

the first law of thermodynamics

A

energy can be transferred and transformed but it cannot be created or destroyed

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2
Q

the second law of thermodynamics

A

every energy transfer or transformation increases the entropy of the universe

ex. during energy transformation some energy is converted to thermal energy and released as heat

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3
Q

metabolic pathway

A

a specific molecule is altered in a series of defined steps resulting in a certain product

each step is catalyzed by an enzyme(macromolecule that speeds up chemical reaction)

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4
Q

metabolism

A

the totality of an organisms chemical reactions

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5
Q

catabolic pathways

A

release energy by breaking down complex molecules to simpler compounds

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6
Q

anabolic pathways

A

consume energy to build complicated molecules from simpler ones

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7
Q

catabolic pathways do what and an ex of it

A

-release energy
-break down molecules
-require enzymes to catalyze the

ex.cellular respiration like breakdown of glucose

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8
Q

anabolic pathways do what and an example

A

-consume energy
-build up larger molecules
-considered uphill
-requires enzymes to catalyze them

ex. photosynthesis

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9
Q

exergonic reaction

A

proceeds with a net release of free energy and is spontaneous

G decreases and G is negative

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10
Q

endergonic reaction

A

absorbs free energy from its surroundings and nonspontaneous

G increases and G is positive

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11
Q

kinetic energy

A

energy associated with motion

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12
Q

atp(adenosine triphosphate)

A

it is the cells energy shuttle

composed of ribose(a sugar)
adenine(a nitrogenous base) and three phosphate groups

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13
Q

what does atp do in metabolism

A

it lowers cellular work by pairing exergonic reactions to endergonic reactions

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14
Q

atp can be regenerated by what

A

the addition of phosphate to adp

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15
Q

enzyme do what

A

speed up metabolic reactions by lowering energy barriers

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16
Q

enzymes are

A

a macromolcule(protein) that speed up a reaction without being consumed by the reaction

biological catalysts that facilitate chemical reactions by lowering activation energy

17
Q

activation energy (EA)

A

the initial energy needed to break bonds of the reactants

18
Q

activation energy is supplied by what

A

heat in the form of thermal energy

thermal energy accelerates the reactant molecules so they collide more often

19
Q

when molecules absorb enough activation energy they are in an unstable condition called

A

transition state

20
Q

substrate

A

the reactant that an enzyme acts on

21
Q

enzyme-substrate complex

A

the enzyme binds to its substrate

while bound the catalytic activity of the enzyme converts substrate to product

22
Q

for an enzyme mediated chemical reaction to occur what must happen

A

the shape and charge of the substrate must be compatible with the active site

23
Q

active site

A

region of the enzyme where substrate binds( where catalysis occurs)

24
Q

active site is formed from

A

few of the enzymes amino acids and the rest of the protein molecule provides the framework that determines shape of active site

25
the specificity of an enzyme is attributed to
a complementary fit between the shape of its active site and the shape of the substrate
26
induced fit is when and it results from
the substrate enters the active site and the enzyme shape changes slightly, tightening around the substrate like a handshake it results from interactions between chemical groups on the substrate and active site
27
what does induced fit do
it brings chemical groups of the active site into positions that enhance catalysis of the reaction
28
effects of temp on enzyme activity
reaction rate increases with increasing temp at optimal temp enzyme catalyzes it’s reaction at the maximum possible rate enzymes denature at temps beyond the optimal
29
effects of substrate concentration on enzyme activity
increasing substrate concentration speeds up the rate of enzyme catalyzed reaction any increase past optimal doesn’t change reaction(every enzyme is filled)
30
effects of pH on enzyme activity
each enzyme has an optimal pH that is dependent on the environment where it’s active
31
cofactor
no protein helpers for catalytic activity
32
competitive inhibitor and how can it be overcome
mimics the substrate and competes for the active site it reduces the productivity of enzymes by blocking substrates from entering active sites it can be overcome by increasing the concentration of substrate
33
non competitive inhibitors
binds to enzyme away from the active site it alters the shape of the enzyme so that even though the substrate can still bind the active site functions less effectively
34
allosteric regulation
when a regulatory molecule binds to a protein at one site and affects the proteins function at another site this regulation can either inhibit or stimulate enzyme activity
35
allosteric enzymes are made from
polypeptide subunits each with its own active site
36
binding of activator vs inhibitor
activator- stabilizes the shape that has functional sites inhibitor- stabilizes the inactive form of the enzyme
37
feedback inhibition
the end product of a metabolic pathway shuts down the pathway prevents a cell from wasting chemical resources by synthesizing more product than needed