Exam 2 Flashcards

1
Q

Oxidoreductases

A

Catalyzes Oxidation or Reduction RXN’s

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2
Q

Transfersases

A

Transfers functional groups between molecules

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3
Q

Hydrolases

A

Breaks bonds via addition of water

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4
Q

Lyases

A

Adds atoms/functional groups to double bonds or removes them to form double bonds

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5
Q

Isomerase

A

Moves functional groups within molecule

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6
Q

Ligases

A

Binds two molecules using ATP

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7
Q

apoenzyme

A

Enzyme without cofactor

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8
Q

Holoenzyme

A

Fully functional enzyme with cofactor

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9
Q

Two Types of Cofactors

A

Small Organic Molecules
-made up by vitamins (coenzymes)
Metals

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10
Q

Coenzymes

A

organic cofactors

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11
Q

Gibbs Free Energy

A

free energy difference between products and reactants (p-r)

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12
Q
  • Gibbs Free Energy
A

Spontaneous RXN

Exergonic

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13
Q

+ Gibbs Free Energy

A

Energy required for RXN to take place

Endergonic

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14
Q

0 Gibbs Free Energy

A

RXN in equilibrium

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15
Q

2 Things Gibbs Free Energy does NOT do

A
  • Give INFO about RXN rate

- Affected by intermediates of RXN

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16
Q

allosteric enxyme

A

enzyme with control mech.

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17
Q

Pathway Convergence

A

One RXN effecting another

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18
Q

Seqential Model

A

Substrate bonding effects rate of next substrate bonding

-Ex: Binding substrate at site 1, reduces affinity for substrate binding at site 2

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19
Q

Competitive Inhibition

A

-Molecule binds to an active site of enzyme and prevents substrate from bonding

MUST BIND TO ENZYME BEFORE SUBSTRATE BINDS
-Can be ‘washed’ out if lots of [S] added

Km = increases
Vmax = unchanged
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20
Q

Uncompettitive Inhibition

A

-Molecule binds to enzyme substrate complex and prevents from going to product

MUST BIND TO ES COMPLEX

Km = decreases
Vmax = decreases
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21
Q

Noncompetivie Inhibition

A

-Molecule binds to enzyme outside of enzyme substrate complex and prevents RXN

BINDS TO E OR ES COMPLEX

Km = no change
Vmax = decreases
22
Q

Psuedo First Order

A

A + B –> P

Acts as 1st order of A because so much excess of B

23
Q

When [S] &laquo_space;Km then?

A

V is proportional to [S]

24
Q

Km Equation

A

Km= (K-1 + K2)/(K1)

25
Vo
Instantaneous Velocity | Vo=(Vmax)[S] / Km[S]
26
Vmax=
[ES]
27
Km on graph is found at?
Vmax over 2
28
Equation for Lineweaver Burke Plot
1/Vo = (Km/Vmax) (1/[S]) + (1/Vmax)
29
Definition of Vmax
Highest possible turnover rate of enzyme at full saturation
30
Vmax equation?
K2[E]t
31
Kcat?
Vmax
32
[E]t?
Total active sites
33
Normal Range of Km
10e-1 - 10e-7 M`
34
Km equation in vivo
Km = [S] @1/2 Vmax
35
@ Km, sensitive to what concentration?
substrate
36
Catalytic Efficiency Equation
CE = Kcat(K2) / Km
37
Pathway Convergence
One RXN's product can influence another
38
Allosteric Enzymes are sensitive to changes in what near what?
Changes in [S] near the Km
39
Heterotrophic Effector Effect on enzyme curve
Shifts binding curve left or right
40
Homotrophic Effector
Alters shape of binding curve
41
T form does or does NOT prefer to form [ES] complex?
does NOT
42
Increase in [S] causes an increase or decrease in T and R forms
Increase in R state | Deacrease in T state
43
Competitive, non-competitive and uncompetive ARE reversible T/F?
TRUE
44
4 Uses of Carbs?
Energy storage, structure, cell surface recognition and binding, signal transduction
45
hemiacital
From aldehyde
46
Hemiketal
From ketone
47
Types of tests to determine if sugar reduces?
Tallins test (Ag0 Fehling's Test (Cu) Benedict's Solution (Cu)
48
How to tell whether boat or chair is most stable?
Confirmation with most OH groups axial
49
Alpha =
fish
50
beta =
boat