Unit 1 - Enzymes Flashcards

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1
Q

What is an enzyme

A

“biological catalysts” = speed up body rxn

  • biological mols that catalyze or speed up rxn wout being consumed
  • enzymes = proteins
  • each enzyme has its own 3D shape which dictates the rxn it will catalyze.
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2
Q

What is an enzyme pt. 2

A

ends in ase
- often globular
- larger than substate
- has ACTIVE SITES

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3
Q

Activation Energy

A

in order for a rxn to proceed, particles must collide w sufficient energy. if mols collide w not enough energy, they will remain unchanged. the min amt of energy for a rxn to occur is called the AE.

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4
Q

Lower The Activation Energy

A

this means that rxn can occur at lower body temperatures if enzymes r present. this gives cells control over which rxn will occur. Not only that but since enzymes r catalysts they CAN BE REUSED.

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5
Q

Binding to an enzyme

A
  • active site interacts w specific mol to catalyze specific rxn
  • called a substrate

sucrose = glucose & fructose
starch = sugars
deoxynucleotide triphosphates = DNA

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6
Q

Models of enzymes

A

1) lock and key
2) induced fit model

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7
Q

Lock and Key model

A
  • enzyme has an active site that is unchanging (rigid)
  • substrates bind = chemical process occurs
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8
Q

Induced Fit Model (new)

A

enzyme change its shape (flexible).

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9
Q

IFM 1)

A

when a substrate enters the active site, it binds to the enzyme through many weak intermolecular bonds.

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10
Q

IFM 2)

A

the enzyme itself slightly changes shape to envelop the substrate

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11
Q

IFM 3)

A

this changes of shape can line up substrate mol and or stress chemical bonds producing the product

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12
Q

activation energy can be lowerd in 3 ways?

A

a) orientation
bring substrates in correct position
b) physical strain
make bonds weaker and easier to rearrange
c) chemical change
+ / - ions to destabilize

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13
Q

The catalytic cycle

A

since enzymes r not used up themselves in a chemical rxn they r reusable
(an enzyme binds to one or more substrate

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14
Q

Cofactors and Coenzymes

A

some enzymes need to bind to additional mols to functions

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15
Q

Cofactors

A

nonprotein inorganic substance (metal ions)

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16
Q

Coenzymes

A

nonprotein organic cofactos that r needed for some enzymes to function (shuttle btw enzymes )
ie. NAD / FAD

17
Q

Apoenzyme

A

the enzyme without its cofactors or coenzymes

18
Q

Holoenzymes

A

the active form bound to cofactors and coenzymes

19
Q

Factor affecting enzyme activity

A

-concentration
-enzyme
-substrate
-temp
-ph

20
Q

enzyme concentration

A

concentration of both the enzyme and substrate will influence the rate of a catalysis rxn.
so if there is excess substrate present then the rate of rxn is proportional to the enzyme concentration

21
Q

Increasing EC

A

will speed up the reaction as long as there is a substrate to bind too. once all substrate is bound, the rxn will no longer speed up since there will be nothing for additionl enxymes to bind which limits the rate of rxn.

22
Q

Substrate Concentration

A

increasin substrate concentration also increase the rate of rxn to a certain point. once all of the enzymes have bound, any substrate incease will have no effect on the rate of rxn, as the avaliable enzymes will be saturated and working at their max rate

23
Q

pH and Temp

A

changes in pH and temp strognly affect the activity of most enxymes. enzymes usually reach max activity with a narrow range

24
Q

pH

A
  • enzymes also have optimal pH
  • normal pH is 7 ; outside of this range will slow enzyme activity
    -dependent on location
    ie. pepsin = ph of 2
    ie. trypins = ph 8 - 12
25
Q

temperature

A

enzymes catalyzed reaction increase as temp increases
but if temp increase past a certain point, protein structure will be disrupted and enzymes will be denatured

26
Q

Optimal temp

A

each enzyme has its own best OT.
but for most it is between 40 - 50c
humans = 37c
archaebacteria = 100c

27
Q

regulation of enzyme activity

A

1) inhibition
2) allosterically
3) feedback inhibition

28
Q

enzyme inhibitors

A
  • lower the rate at which an enzyme catelyzes a rxn
  • inhibitors r mols that bind to an enzyme and decreases its activity
29
Q

competitive inhibition

A
  • v similar in shape
  • bind to the active site and physically block the correct substrate from binding
  • if the concentration of inhibitor is high enough the rxn will stop
30
Q

Non-Competitive inhibition

A
  • substance that attach to a binding site on an enzyme other than active site causing a change in the enzymes shape abd loss of affinity
  • may be allosteric
  • inhibitor directly affects the enzyme so that it cannot carry out its function
31
Q

Allosteric Regulation (2)

A

cells must control enzymes to coordinate cellular activities. they may accomplish this in 2 ways
1) restricting the production of a specific enzyme
2) inhibiting the action of an enzyme that had already been produced

32
Q

Allosteric sites

A

receptor site; some distance from the active site of certain enzymes that bind substances that may inhibit or stimulate an enzymes activity.

33
Q

Effector

A

substance that binds to the allosteric site may inhibit or stimulate and enzymes activity

34
Q

Feedback inhibitor

A

the production of a series of enzymes catalyzed rxn acts to allosterically inhibit and enzyme that acts earlier in the series. this is an effective way to stop the synthesis of that product when aq level r produced in a cell.

35
Q
A