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T2 - BioChem midterm 2 > Unit 6 > Flashcards

Unit 6 Flashcards

1
Q

reactants/substrates are ___ the arrow

A

before

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2
Q

products are ___ the arrow

A

after

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3
Q

A+B –> C+D

A+B are the ____/____

A

reactants/substrates

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4
Q

A+B –> C+D

C+D are the ____

A

products

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5
Q

A+B –> [AB] –> C+D

[AB] is the ___

A

intermediate

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6
Q

the intermediate is not _____

A

isolatable

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7
Q

–> means that the reaction is ____

A

irreversible

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8
Q

means the reaction is ____

A

reversible

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9
Q

rate of a rxn is determined by 5 things

A 
[reactants]
temperature
pH
activation E and the energy barrier
[products]
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10
Q

forward and reverse reactions occur ____, although the ____ reaction rates are different

A

simultaneously

initial

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11
Q

both forward and reverse reactions are happening at the ____ same time, but at ___ rates

A

same

different

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12
Q

____ _____: the concentration of the products cannot increase further

A

equilibrium state

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13
Q

at equilibrium states, the forward and reverse reactions are still happening, but with no ___ __

A

net change

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14
Q

2 formulas to calculate equilibrium constant Keq

A

[products]/[reactants]

k1(rate of forward reaction)/k-1(rate of backward reaction

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15
Q

___ ___: when two reactants collide A+B. energy is released

A

activation energy

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16
Q

activation energy must be ___ than energy barrier for the reaction to proceed

A

greater

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17
Q

activation energy can be demarcated by 2 things

A

Ea or (delta)G*

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18
Q

___ ___: the amount of energy required for the formation of products

A

energy barrier

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19
Q

+(delta)G

A

low energy state–>high energy state

costs energy

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20
Q

-(delta)G

A

high energy state–>low energy state

releases energy

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21
Q

____ ___/____: how fast the products are formed

A

reaction rate

velocity (v)

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22
Q

reaction rate/velocity: measured ____ in reaction

A

early

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23
Q

(delta)G ultimately determines the ___ ____ of the reactants and products, but not the ___ ___

A

final concentration

reaction rate

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24
Q

____: change in free energy from standard state, 1.0M concentrations of substrates and products to equilibrium

A

(delta)G0

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25
Q

standard state:
___ degrees C
____K
__atm

A

25
298
1

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26
Q

____ defines (delta)G0 at STP and pH 7.0

A

(delta)G0’

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27
Q

if free energy of products is lower than substrates, the signs of (delta)G0 and (delta)G0’ will be ____

A

negative

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28
Q

if free energy of products is higher than substrates, the signs of (delta)G0 and (delta)G0’ will be ____

A

positive

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29
Q

in ___ reactions, energy is lost

A

endergonic

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30
Q

in ___, energy is gained

A

exergonic

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31
Q

(-) delta G: reaction will occur ____ although the rate is ____

A

spontaneously

unknown

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32
Q

enzymes are ____:

  • ___ the rate of the reaction
  • are not ____
  • bind to _____, lowering ___
  • do not change ___
A 
catalysts
increase
consumed
substrates
Ea
Keq
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33
Q

enzymes are ____

  • some are ___ (____)
  • many have ___ groups attached to apoprotein forming a ____
  • if the prosthetic group is metal, it is a ___
A 
proteins
RNAs (ribozymes)
prosthetic
holoenzymes
metalloenzyes
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34
Q

enzymes are __ and ___-____

  • enzymes have optimal ___ and ____
  • ___ or ___ that denature proteins denature enzyme activity
A 
pH
temperature-dependant
enzymes
temperatures
chemicals
factors
35
Q

enzymes are ___

- some are ___, some are ___

A

specific
absolute
group

36
Q

some enzymes have ____ specificity, the ability to distinguish between L and D forms of amino acids or sugars

A

optical

37
Q

____ ___: binds the reactants and facilitates the reaction

A

catalytic site

38
Q

specificity is dictate by the 3D structure of the ___ ___ of the enzyme and the substrate
— requires a minimum of ____ point attachment

A

catalytic site

3

39
Q

___ ___: the substrate induces a conformational change in the catalytic site (lock and key)

A

induced fit

40
Q

enzymes are saturable; a reaction mixture has a fixed amount of enzyme, so the reaction rate increases with [substrate] to a point, until all enzymes are _____

A

busy

41
Q

enzymes are ___ or ___

A

inhibited

stimulated

42
Q

_____: increase the rate of reaction

A

activators/stimulated

43
Q

_____: decrease the rate of reaction

A

inhibitors

44
Q

____ ___: act by competing with the natural metabolite for the active site of the enzyme therefore the are ___ ____

A

enzyme inhibitors

competitive inhibitors

45
Q

___ ___: their effect can be overcome by addition of more natural substrate

A

reversible inhibitors

46
Q

___ ___: eliminates enzymes function, Vmax is reduced

A

irreversible inhibitors

47
Q

coenzymes are ___ ___ required for the catalytic actions of certain enzymes

A

secondary substrates

48
Q

coenzymes can be ___ or ___

A

organic

inorganic

49
Q

many coenzymes are ___ ___ (especially ___)

A

vitamin derivatives

B

50
Q

some coenzymes are ___ ___ of enzymes

A

prosthetic groups

51
Q

____: anything that help an enzyme do its function

A

coenzymes

52
Q

___ ____ or ___: substances other than substrates which regulate and enzymes activity by binding to the ___ ___ of the enzyme

A

allosteric effectors or ligands

allosteric site

53
Q

___ ___: can be catalytic site or another site of enzyme

A

allosteric site

54
Q

binding of activator or inhibitor to the allosteric site changes the enzyme ____, especially the catalytic site, altering the reaction rate ____

A

conformation

exponentially

55
Q

____: positive allosteric kinetics

A

acceleration

56
Q

___: negative allosteric kinetics

A

deceleration

57
Q

kinetic plot demonstrates a non linear ___ curve

A

S

58
Q

kinetics assesses how ___ of an enzymatic reaction is affected by a host of factors (5 to name a few)

A 
[substrate]
coenzymes
activators
inhibitors
pH
temperature
phase of the moon
59
Q

experiments are done to obtain info on 3 things

A

specificity of an enzyme

mechanism of activation/inhibition

60
Q

____ ____ ___: measures velocity of a reaction, with increasing substrate concentrations, keeping pH and temperature optimum

A

michaelis-menten equation

61
Q

V max is…

A

max velocity of an experimental situation

62
Q

Km =

A

the [substrate] that produces a velocity of 1/2 max

how strong affinity an enzyme has for its substrate

63
Q

the ____ the Km, the ___ the affinity

A

lower –> higher

higher –> lower

64
Q

lineweaver-burk (double reciprical) plot…

A

removes the uncertainty of the Vmax plateau of Michaelis-menten

65
Q

michaelis-menten an lineweaver-burk are only good for ___-__ kinetics, bc of the additional substrate binding may alter the rate of the reaction

A

non-allosteric

66
Q

trivial names of enzymes (2)

A

papain

chymotrypsin

67
Q

hybrid name of enzymes

A

substrate + ‘ase’

68
Q

descriptive names of enzymes

A

substrate + description + ase

69
Q

6 classifications of enzymes

A 
oxidoreductase
transferase
hydrolase
lyase
isomerase
ligase
70
Q

____: redox reactions

A

oxidoreductase

71
Q

___: transfer groups (other than H) between substrates

A

transferase

72
Q

___: break substrates by addition of water

A

hydrolase

73
Q

___: break sbstrates without water (leave double bonds)

A

lyase

74
Q

____: convert isomers

A

isomerase

75
Q

___: ligate with new covalent bonds

A

ligase

76
Q

____: ligases that use ATP/GTP as energy sources

A

synthetase

77
Q

____: ligases that use other energy (not GTP/ATP)

A

synthase

78
Q

4 digit enzyme code:

- 1st number

A

class number

79
Q

4 digit enzyme code:

- 2nd number

A

the first functional group of the substrate to be altered

80
Q

4 digit enzyme code:

- 3rd number

A

the second functional group of the substrate to be altered

81
Q

4 digit enzyme code:

- 4th number

A

denotes the particular enzyme

82
Q

increase/decrease enzyme biosynthesis

- at the DNA/RNA level gene ___/____

A

induction

repression

83
Q

REGULATION OF ENZYMES - SLIDE 27

A

aldkjf

84
Q

____: two or more enzymes that catlyze the same biochemical reactions

A

isozymes

T2 - BioChem midterm 2 (4 decks)

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