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
standard state: ___ degrees C ____K __atm
25 298 1
26
____ defines (delta)G0 at STP and pH 7.0
(delta)G0'
27
if free energy of products is lower than substrates, the signs of (delta)G0 and (delta)G0' will be ____
negative
28
if free energy of products is higher than substrates, the signs of (delta)G0 and (delta)G0' will be ____
positive
29
in ___ reactions, energy is lost
endergonic
30
in ___, energy is gained
exergonic
31
(-) delta G: reaction will occur ____ although the rate is ____
spontaneously | unknown
32
enzymes are ____: - ___ the rate of the reaction - are not ____ - bind to _____, lowering ___ - do not change ___
``` catalysts increase consumed substrates Ea Keq ```
33
enzymes are ____ - some are ___ (____) - many have ___ groups attached to apoprotein forming a ____ - if the prosthetic group is metal, it is a ___
``` proteins RNAs (ribozymes) prosthetic holoenzymes metalloenzyes ```
34
enzymes are __ and ___-____ - enzymes have optimal ___ and ____ - ___ or ___ that denature proteins denature enzyme activity
``` pH temperature-dependant enzymes temperatures chemicals factors ```
35
enzymes are ___ | - some are ___, some are ___
specific absolute group
36
some enzymes have ____ specificity, the ability to distinguish between L and D forms of amino acids or sugars
optical
37
____ ___: binds the reactants and facilitates the reaction
catalytic site
38
specificity is dictate by the 3D structure of the ___ ___ of the enzyme and the substrate --- requires a minimum of ____ point attachment
catalytic site | 3
39
___ ___: the substrate induces a conformational change in the catalytic site (lock and key)
induced fit
40
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 _____
busy
41
enzymes are ___ or ___
inhibited | stimulated
42
_____: increase the rate of reaction
activators/stimulated
43
_____: decrease the rate of reaction
inhibitors
44
____ ___: act by competing with the natural metabolite for the active site of the enzyme therefore the are ___ ____
enzyme inhibitors | competitive inhibitors
45
___ ___: their effect can be overcome by addition of more natural substrate
reversible inhibitors
46
___ ___: eliminates enzymes function, Vmax is reduced
irreversible inhibitors
47
coenzymes are ___ ___ required for the catalytic actions of certain enzymes
secondary substrates
48
coenzymes can be ___ or ___
organic | inorganic
49
many coenzymes are ___ ___ (especially ___)
vitamin derivatives | B
50
some coenzymes are ___ ___ of enzymes
prosthetic groups
51
____: anything that help an enzyme do its function
coenzymes
52
___ ____ or ___: substances other than substrates which regulate and enzymes activity by binding to the ___ ___ of the enzyme
allosteric effectors or ligands | allosteric site
53
___ ___: can be catalytic site or another site of enzyme
allosteric site
54
binding of activator or inhibitor to the allosteric site changes the enzyme ____, especially the catalytic site, altering the reaction rate ____
conformation | exponentially
55
____: positive allosteric kinetics
acceleration
56
___: negative allosteric kinetics
deceleration
57
kinetic plot demonstrates a non linear ___ curve
S
58
kinetics assesses how ___ of an enzymatic reaction is affected by a host of factors (5 to name a few)
``` [substrate] coenzymes activators inhibitors pH temperature phase of the moon ```
59
experiments are done to obtain info on 3 things
specificity of an enzyme | mechanism of activation/inhibition
60
____ ____ ___: measures velocity of a reaction, with increasing substrate concentrations, keeping pH and temperature optimum
michaelis-menten equation
61
V max is...
max velocity of an experimental situation
62
Km =
the [substrate] that produces a velocity of 1/2 max | how strong affinity an enzyme has for its substrate
63
the ____ the Km, the ___ the affinity
lower --> higher | higher --> lower
64
lineweaver-burk (double reciprical) plot...
removes the uncertainty of the Vmax plateau of Michaelis-menten
65
michaelis-menten an lineweaver-burk are only good for ___-__ kinetics, bc of the additional substrate binding may alter the rate of the reaction
non-allosteric
66
trivial names of enzymes (2)
papain | chymotrypsin
67
hybrid name of enzymes
substrate + 'ase'
68
descriptive names of enzymes
substrate + description + ase
69
6 classifications of enzymes
``` oxidoreductase transferase hydrolase lyase isomerase ligase ```
70
____: redox reactions
oxidoreductase
71
___: transfer groups (other than H) between substrates
transferase
72
___: break substrates by addition of water
hydrolase
73
___: break sbstrates without water (leave double bonds)
lyase
74
____: convert isomers
isomerase
75
___: ligate with new covalent bonds
ligase
76
____: ligases that use ATP/GTP as energy sources
synthetase
77
____: ligases that use other energy (not GTP/ATP)
synthase
78
4 digit enzyme code: | - 1st number
class number
79
4 digit enzyme code: | - 2nd number
the first functional group of the substrate to be altered
80
4 digit enzyme code: | - 3rd number
the second functional group of the substrate to be altered
81
4 digit enzyme code: | - 4th number
denotes the particular enzyme
82
increase/decrease enzyme biosynthesis | - at the DNA/RNA level gene ___/____
induction | repression
83
REGULATION OF ENZYMES - SLIDE 27
aldkjf
84
____: two or more enzymes that catlyze the same biochemical reactions
isozymes