Chapter 8 Section 4+5 Flashcards

(38 cards)

1
Q

Enzyme

A

macromolecule that acts as a catalyst that speeds up reaction w/out being consumed by the reaction

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2
Q

Activation Energy

A

the initial amount of energy needed to start a reaction

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3
Q

The Ea creates a ____ that determines what?

A

barrier, the speed of a reaction

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4
Q

Catalysis

A

the process where enzymes reduces the Ea barrier in order for reactant molecules to reach a transition state at moderate temps.

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5
Q

Substrate

A

the reactant an enzyme acts on

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6
Q

Enzyme-Substrate Complex

A

when enzyme binds w/substrate

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7
Q

Active Site

A

restricted region the enzyme binds to substrate

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8
Q

Induced Fit

A

enzyme changes shape slightly to fit in more snuggly w/ substrate to enhance ability to catalyze

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9
Q

Ways an active site can lower Ea and speed up reaction

A
  • acting as a template for substrate orientation
  • stressing the substrates & stabilizing the transition state
    -providing favorable microenvironment
  • participating directly in catalytic reaction
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10
Q

synthesis

A

active site orients substrate in correct position for reaction

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10
Q

synthesis

A

active site orients substrate in correct position for reaction

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11
Q

digestion

A

active site binds w/ substrate & puts stress on bonds that must be broken, making it easier to separate molecules

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12
Q

What are responsible for the fit of substrate & active site & enzyme?

A

H-Bonds

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13
Q

An increase in enzymes means an increase in what?

A

reaction rate

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14
Q

When does a reaction level off when there is an enzyme concentration?

A

when substrate is limiting factor & not all enzymes can find substrate

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15
Q

An increase in substrate means an increase in what?

A

reaction rate

16
Q

When does a reaction level off when there is an substrate concentration?

A

when all enzyme have active sites engaged, enzymes are saturated, max. rate of reaction

17
Q

Optium Temp.

A

greatest # of molecular collisons, humans 35-40 C

18
Q

Heat above Optium Temp.

A

the energy level disrupts bonds in enzymes and b/tw enzyme & substrate

19
Q

Cold Temp.

A

molecules move slower, decrease in collision b/tw enzyme & substrate

20
Q

Changes in pH

A

disrupts bonds & charged amino acids, disrupts 3D shapes

21
Q

Optimal pH

22
Q

Changes in Salinity

A

disrupts bonds, 3D shapes & attraction b/tw charged amino acid

23
Q

What are the types of activators

A

cofactors & coenzymes

24
Cofactors
non-protein, small inorganic compounds & ions, bound within enzyme molecule
25
Coenzymes
non-protein, organic molecules
26
Compettive Inhibator
mimics substrate competing for active site
27
How can a Competitive Inhibitor be overcome?
Increasing substrate concentration, so it out competes inhibitor for active site
28
Inhibitors
molecules that reduce enzyme activity
29
Non-Competitive Inhibitor
binds to site other than active site
30
When an allosteric inhibitor binds w/ allosteric site, what happens to the enzyme?
the enzyme changes shape
31
Conformational change
active site is no longer functional binding site
32
Irreversible Inhibition
inhibitor permanently binds w/enzyme -competitive permanently binds to active site -allosteric permanently binds to allosteric site permanently changes enzyme's shape
33
Allosteric Regulation
conformational changes by regulatory molecules inhibitors -keeps enzyme in inactive form
33
Allosteric Regulation
conformational changes by regulatory molecules inhibitors -keeps enzyme in inactive form
34
Metabolic Pathways
Chem reactions of life are organized in pathways, divide chem reactions into many small steps
35
Feedback Inhibition
Regulation & coordination of production -product is used by next step in pathway -final product is inhibitor of earlier step allosteric inhibitor of earlier enzyme -no unnecessary accumulation of products
36
Caspases
enzymes that are activated when a cell has ordered to go through apoptosis