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term 2 - BioChem unit 2 BT > Unit 6. Enzymes and coenzymes > Flashcards

Unit 6. Enzymes and coenzymes Flashcards

1
Q

The rate of the rxn is dependant on (5) things

A 
Reaction concentration 
temp 
pH - [H+] 
activation E (NRG barrier)
Product concentration
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2
Q

def:______: the cencentration of products cannot increase further

A

equilibrium state

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3
Q

What is Keq?

A

Equilibrium constant : [product]/[reactant]

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4
Q

Equilibrium constant can be calc. from _____ concentration or ratio of _____

A

equilibrium concentration
or
ratio of rate constants

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5
Q

______ must be greater than the NRG barrier for the rxn to proceed

A

activation NRG (Ea or delta G)

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6
Q

What is delta G?

A

activation NRG (Ea)

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7
Q

def: ____: when 2 reactants collide, NRG is released . It must be greater than the NRG barrier for the reaction to proceed

A

Activation NRG

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8
Q

_____: the amt of NRG required for the formation of products

A

Energy barrier

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9
Q

_____: how fast the products are formed

A

Reaction rate (or velocity) (v)

  • must be measured very early in reaction (before reverse reaction )
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10
Q

When must the reaction rate be measured ?

A

before the reverse reaction occurs

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11
Q

_____: the difference btw the initial free NRG of the reactants and the products

A

Gibbs Free ENERGY

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12
Q

What determines the final concentration of the reactants and products ?

A

Delta G

  • but not the reaction rate
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13
Q

If free NRG of product is lower than substrate the sign of Delta G will be ______ (+/-)

A

negative

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14
Q

If he free NRG of product is greater than substrate the sign of Delta G will be _____(+/-)

A

positive

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15
Q

______ effets the reaction rate

A

Activation NRG

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16
Q

_____ is when the product ends with less nrg than the initial reactant

A

exergonic

-Delta G

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17
Q

____ is when the product ends with more NRG than the initial reactant

A

endergonic

+Delta G

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18
Q

Standard state for : Moles, temp, pH and pressure

A

Moles: 1.0M
Temp: 25C or 298K
Pressure: 1atm
pH: 7.0

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19
Q

Is endergonic or exergonic spontaneous ?

A

exergonic

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20
Q

Catalyst ___ the rate of reaction

A

increase

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21
Q

Catalyst are ____ consumed

A

not

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22
Q

______ bind to substrate, lowering Ea

A

Catalyst

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23
Q

Can catalyst change Keq

A

No

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24
Q

Enzyme proteins can be _NA

A

RNA

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25
The prosthetic group on an enzyme protein forms a _____
holoenzyme
26
If an enzyme protein prosthetic group is a metal it is a _______
metalloenzyme
27
_____ is an enzyme without a cofactor
apoprotein
28
An enzyme with optical specificity has the ability to __________
distinguish btw L- and D- forms of AA or sugars
29
Optical specificity is ________ specific
absolute
30
Specificity is dictated by the 3-D structure of the catalytic site of the enzyme and sunstrate it requires _______
3 point attachment
31
_____: substrate induces a conformational change in the catalytic site
induced fit model | 3 pt attachment
32
Difference btw absolute and group specificity
absolute enzyme will only bind to one type of substrate (ex: fructokinase) Grouped enzyme will bind to any type of substrate within a group (ex: hexokinase)
33
def: _______site : binds the reactants and facilitates the reaction
catalytic site
34
At least how many attachments must there be btw a substrate and enzyme
3 points of attachment
35
def___: the substrate fits exactly into the enzyme active site
lock and key
36
what are two models of substrate enzyme interactions
induced fit & lock and key
37
____ : increase the rate of reaction
activator (stimulator) enzymes
38
____: decreases the rate of reaction
inhibitor enzyme
39
____ is an intermediate and products of metabolism
metabolites
40
_______ compete with the natural metabolite for the active site of the enzyme
competitive inhibitors
41
Competitive inhibitors can be overcome by the addition of more _____
substrate - Reversible
42
Irreversible enzymes fxn?
eliminate enzyme fxn
43
Name 5 properties of an enzyme
1. catalyst 2. proteins 3. pH & tem dependent 4. specific 5. saturable
44
____ are secondary substrates that are required for the catalytic actions of certain enzymes
coenzymes (cosubstrates)
45
Vit. __ are coenzymes
Vit B
46
____ are secondary substrates
coenzymes
47
Coenzymes are required for the catalytic action of all enzymes T/F
false . only some
48
coenzymes can be ____ derivatives
vitamin
49
some ____ are covalently bound as prosthetic groups of enzymes
coenzymes
50
Name (3) inorganic coenzymes
Ca+, Na+, Cl-
51
Name (4) organic coenzymes
NAD?NADH H+ FAD/FADH CoASH
52
_____: substances other than substrates which regulate an enzyme's activity by binding to the allosteric site
allosteric effectors or ligands
53
Allosteric effectors bind to _____ the regulate an enzymes activiry
allosteric site
54
The binding of an activator or inhibitor ____ especially the catalytic site, altering the reaction rate _____
Changes the enzyme conformation exponentially
55
The main point of kinetics is to assess the ___ of an enzymatic reaction
velocity
56
_______: measures the velocity of a reaction, with increasing substrate concentrations, keeping pH an d temp at optimum
michaelis-menten equation
57
What factor is increased during a michaelis-menten equation
concentration of substrates
58
Lower the Km value, the ___ the affinity of the substrate to the enzyme (michaelis-menten equation )
greater
59
Km = how strong of ___ an enzyme has for its substrate | michaelis-menten equation
affinity
60
The greater the Km, the _____ the affinity of an enzyme for its substrate (michaelis-menten equation)
lower
61
_____ enzymes do redox reactions
oxidoreductase
62
_____ enzymes transfer R-groups
transferase
63
____ enzymes break substrates by addition of H2O
hydrolase | digestive enzymes
64
All digestive enzymes are _____
hydrolase
65
_____ enzymes break substrates w/o H2O
lyase
66
____ enzymes convert isomers
isomerase | they rearrange molecules
67
______ enzymes ligate with new covalent bonds
Ligase | synTHEtase/ synthase
68
Ligate means to ___
join
69
synTHEtase:______
uses ATP/GTP as NRG source | uses THE nrg
70
Synthase:_______
uses other sources of NRG | besides ATP/GTP
71
____: 2 or more enzymes that catalyze the same biochemical reaction
isozymes
72
_____: a proenzyme or an enzyme precursor
zymogen (ex: enzymes in bile are inactive when they are in the prancrease, and activate after they leave the pancrease ... so they dont eat the pancreas)
73
Isozymes are distinct, so they have _____AA sequences
different | and different physical properties

term 2 - BioChem unit 2 BT (3 decks)

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