Enzyme Kinetics and Inhibition 10/4 Flashcards

1
Q

characteristics of enzymes

A
  1. cataylze chemical reactions without being consumed 2. very selective 3. products of natural selection
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2
Q

delta G less than 0

A

spontaneous reaction

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3
Q

delta G greater than 0

A

non-spontaneous reaction

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4
Q

enzyme catalysis reaction

A

E+S →[ES]→E+P

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5
Q

active site

A

has a shape that accomodates and complements the subtrate, including polarity and charge complentarily to the substrate transition state

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6
Q

to be an effective catalyst, should the enzyme bind tighter to the substrate or to the transition state?

A

the transition state! **this makes TS analogs good inhibitors of enzyme (for drugs)

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7
Q

kcat

A

the rate at which the ES complex converts to free enzyme and product. units: s-1

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8
Q

Km

A

the dissociation constant for the enzyme substrate complex. units=M

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9
Q

Vmax

A

the maximal value for an enzyme reaction

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10
Q

rate saturation equation

A

[E]0=[E]+{ES]

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11
Q

when [S] is low, the enzyme is mostly ________. how does v increase?

A

[E]

v increases proportionally to [S]

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12
Q

when [S] is high, the enzyme is mostly _____. how does v increase?

A

[ES]

v increases slowly in proportion to [S]

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13
Q

steady state enzyme kinetics equation

A

v=(Vmax[S])/Km+[S]

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14
Q

the upper limit of the forward reaction is

A

Kcat

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15
Q

carbonic anhydrase

A

catalyzes interconversion of carbon dioxide and bicarbonate

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16
Q

reversible inhibitor I

A

binds and dissociates from an enzyme; doesn’t react, just prevents substrates from reacting

17
Q

irreversible inhibitor

A

binds to and permanently inactivates an enzyme

18
Q

how does aspirin affect COX (cyclooxygenase)?

A

aspirin inactivates cox enzymes (cox synthesize prostaglandins, causing inflammation) - aspirin PERMANENTLY acetylates the active site serine residue. this slows blood clotting

19
Q

aspirin toxicity

A
  1. salicylate (the remainder of the aspirin molecule ones it inactivates COX) binds to other proteins causing tinnitus (ear ringing) - can result in SATURATION of liver enzymes
  2. anion gap metabolic acidosis - interrupts aerobic respiration, leading to anaerobic production of lactate
20
Q

for reversible enzyme inhibitors, the amount of inhibition depends on:

A

the concentration of the inhibitor [I]

21
Q

competitive inhibitors prevent substrates from binding to…

A

the free enzyme. normally binds to the enzyme’s ACTIVE SITE

22
Q

noncompetitive inhibitor

A

has no effect on substarte binding - prevents reaction of the bound substrate

23
Q

dihydrofolate reductase (DHFR)

A

enzyme that is used to make DNA

24
Q

what does methotrexate inhibit?

A

DHFR - used in leukemia (acute lymphoblastic leukemia) treatments. is COMPETITIVE inhibitor

25
Q

there are 5 ways that enzymes can be regulated. they are:

A
  1. substrate/cofactor availability
  2. product inhibition
  3. allosteric activation and inhibition
  4. positive and negative cooperativity
  5. post-translational modification
26
Q

negative feedback

A

the product inhibtis the process from happening again

27
Q

glucose-6-P is catalyzed by:

A

glucokinase and hexokinase

28
Q

the Km for glucose is higher in ______ than _______. why is this important?

A

Km is higher in glucokinase (10mM) than hexokinase (0.1 mM). This means that hexokinase has a high affinity for the substrate

29
Q

allosteric regulation of an enzyme occurs where? what type of inhibitors do this?

A

at a site on the enzyme OTHER that the active site. noncompetitive inhibitors are allosteric inhibitors.

30
Q

thrombin

A

a blood clotting factor. has 2 confirmations:

  1. slow: an anticoagulent (cleaves protein C, a clotting inhibitor)
  2. fast form: cleaves fibrinogen; coagulent

conversion between the slow and fast forms is ALLOSTERICALLY REGULATED by the binding of Na+

31
Q

amount of slow/fast thrombin in the blood?

A

serum thrombin is 60%fast/40%slow

32
Q

what type of curve does positive cooperativity give?

A

sigmoid curve - means that v is less responsive at low [S]

33
Q

glycogen phosphorylase

A

enzyme that converts glycogen to glucose-1-P. exists in 2 forms.

  1. b (native form), T (tense) state - has a high Km, or poor substrate affinity (would want to DISSOCIATE)
  2. a form favors R (relaxed) state, has low Km, meaning it has high substrate affinity

(a phosphorylase converts the a form back to the b form)

34
Q

AMP is a(n) ____________ activator

A

allosteric

35
Q

what is a zymogen?

A

an inactive precursor that is turned on by proteolytic cleavage, many pancreatic/digestive enzymes are this