lecture 15 - regulation of metabolic pathways Flashcards

1
Q

do chem rxns and pathways take place even if they delta G < 0

A

no

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2
Q

if reactions are thermodynamically favorable can they be wasteful to the cell or organism

A

yes

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3
Q

what are main pathways regulated by

A

feedback inhibition

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4
Q

feedback inhibition

A

inhibition of enzyme by a product of that reaction or metabolic pathway

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5
Q

when does feedback inhibition occur

A

when product is plentiful

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6
Q

what is feedback regulation a form of

A

negative feedback or refulation

-something is binding to enzyme and turning it off

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7
Q

what type of enzyme does feedbakc inhibition use

A

allosteric enzyme

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8
Q

how many binding sites does allosteric enzyme have

A

2 binding sites

-active site for sustrate
-allosteric site for end product (inhibitor)

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9
Q

what happens if too much inhibitor accumulates

A

pathway becomes blocked and nothing can bind to the allosteric enzyme

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10
Q

what happens if end product binds to allosteric site

A

substrate can’t bind at active ste

-active site shape is altered

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11
Q

what happens when product is plentiful

A

it inhibits the enzyme an thus metabolic pathway

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12
Q

example of feedback inhibition

A

isoleucine synthesis using threonine as first substrate of the pathway

-feedback inhibition of isoleucine synthesis by isoleucine

if there is plenty of isoleucine don’t make more

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13
Q

are all enzymes in a pathway allosteric

A

no, only slect ones

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14
Q

what type of forms can allosteric enzyme be

A

active and inactive

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15
Q

what are some allosteric enzymes regulated by

A

-allosteric inhibitor
-allosteric activators

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16
Q

where do allosteric activators and inhibitorsbind

A

at allosteric site of enzyme

17
Q

what can binding of an activatir stabilize

A

the active form of an enzyme

18
Q

what can binidng the inhibitor stabilize

A

the inactive form of enzyme

19
Q

what do most allosterically regulated enzymes consist of

A

multiple polypeptide subunits

20
Q

what does activator binding induce

A

active site to adopt the right shape to bind subtrate

21
Q

what happens to Km when activatir binds

A

Km is lower - higher affinity for substrate enzyme turned “on” or catalysts speed up

22
Q

what does inhibitor binding induce

A

induces active site to adopt the incorrect shape to bind substrate

23
Q

what happens to Km when inhibitor binds

A

Km is higher - lower affinity for substrate enzyme turned “off” or catalysis slows

24
Q

third step of glycolysis

A

-key regulatory step in cellular respiration

25
main enzyme in third step of glycolysis and describe process of the step
enzyme = PFK -Enzyme binds to F-G-D in active site and ATP moleq -enzyme catalyzes phosphate from ATP to make F-I,6-P to make 2 phosphates -PFK is under allosteric regulation by several molecules
26
what does allosteric regualtion of PFK regaulte
the rate of glycolysis and thus the rest of cellular respiration too
27
PFK is under allosteric regaultion by what
-allosteric inhibitors (citrate + ATP) -allosteric activator (AMP)
28
what nolecules is an indicator of low ATP levels when it is high
AMP
29
need energy, so cells convert _____
ADP + ADP -> ATP + AMP
30
in glycolysis in a resting muscle there is more ____ and less _______
ATP, pyruvate
31
glycolysis in active muscle
less ATP and more AMP which binds to PFK, so ATP can't bind to allosteric site and has to bind to active site and be used as a substrate
32
check notes for fate of lactate generated by fermentation
ok
33
gluconeogenesis
synthesis of glucose from small organic molecules
34
in mammals where does gluconeogensis occur
mostly in the liver
35
is gluconeogenesis glycolysis run in reverse
no!