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CHM 360 > Exam 2 > Flashcards

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
Q

Vo

A

Instantaneous Velocity

Vo=(Vmax)[S] / Km[S]

26
Q

Vmax=

A

[ES]

27
Q

Km on graph is found at?

A

Vmax over 2

28
Q

Equation for Lineweaver Burke Plot

A

1/Vo = (Km/Vmax) (1/[S]) + (1/Vmax)

29
Q

Definition of Vmax

A

Highest possible turnover rate of enzyme at full saturation

30
Q

Vmax equation?

A

K2[E]t

31
Q

Kcat?

A

Vmax

32
Q

[E]t?

A

Total active sites

33
Q

Normal Range of Km

A

10e-1 - 10e-7 M`

34
Q

Km equation in vivo

A

Km = [S] @1/2 Vmax

35
Q

@ Km, sensitive to what concentration?

A

substrate

36
Q

Catalytic Efficiency Equation

A

CE = Kcat(K2) / Km

37
Q

Pathway Convergence

A

One RXN’s product can influence another

38
Q

Allosteric Enzymes are sensitive to changes in what near what?

A

Changes in [S] near the Km

39
Q

Heterotrophic Effector Effect on enzyme curve

A

Shifts binding curve left or right

40
Q

Homotrophic Effector

A

Alters shape of binding curve

41
Q

T form does or does NOT prefer to form [ES] complex?

A

does NOT

42
Q

Increase in [S] causes an increase or decrease in T and R forms

A

Increase in R state

Deacrease in T state

43
Q

Competitive, non-competitive and uncompetive ARE reversible T/F?

A

TRUE

44
Q

4 Uses of Carbs?

A

Energy storage, structure, cell surface recognition and binding, signal transduction

45
Q

hemiacital

A

From aldehyde

46
Q

Hemiketal

A

From ketone

47
Q

Types of tests to determine if sugar reduces?

A

Tallins test (Ag0
Fehling’s Test (Cu)
Benedict’s Solution (Cu)

48
Q

How to tell whether boat or chair is most stable?

A

Confirmation with most OH groups axial

49
Q

Alpha =

A

fish

50
Q

beta =

A

boat

CHM 360 (3 decks)

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