Enzymes Flashcards

(50 cards)

1
Q

enzymes are ….. proteins

A

globular

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2
Q

ribozymes

A

catalytic RNA molecules with no protein component

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3
Q

apoenzymes

A

protein component

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4
Q

holoenzymes

A

whole enzyme

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5
Q

active site

A

where the substrate binds

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6
Q

enzyme functions

A

lower activation energy

increase rate of spontaneous reactions

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7
Q

addition of an enzymes lower the

A

activation energy

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8
Q

delta G =

A

Delta H - T delta S

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9
Q

enzymes form non-covalent bonds with substrate molecules called the

A

binding energy

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10
Q

binding energy allows the enzymes to

A

take the reaction through a different path of reaction intermediates

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11
Q

how do enzymes reduce the activation energy?

A

entropy reduction

desolvation

induced fit

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12
Q

desolvation

A

weak bonds between substrate and enzymes replaced with H bonds

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13
Q

Vo

A

initial velocity

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14
Q

low substrate concentration gives you an

A

increase in Vo

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15
Q

when [S] becomes so large that Vo changes are vanishingly small you get

A

maximum reaction velocity

Vmax

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16
Q

E + (K1) gives ES which gives

A

E + P (k2)

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17
Q

K1 is a ……….. reaction

A

reversible

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18
Q

K2 occurs ………. than K1

A

slower

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19
Q

Study of initial rates of reaction are termed

A

steady state kinetics

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20
Q

Rate limiting step of enzymatic reactions is the breakdown of

A

ES complex to give free enzymes and product

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21
Q

Half of Vmax is

A

michealis constant

22
Q
the
substrate concentration at
which the initial reaction
rate is half of the maximum
reaction rate
23
Q

the ratio of rate constant for breakdown of ES to E + S compared to the rate constant for formation of ES from E + S

24
Q

Larger Km indicates a

A

less stable ES complex

25
Smaller Km indicates a
more stable ES complex
26
Km indicates the ....... for a substrate
affinity
27
Glucose + ATP =
glucose-6-phosphate + ADP
28
Glucokinase and hexokinase catalyse
glucose to glucose 6 phosphate
29
Glucokinase Km and Vmax are both
high
30
Hexokinase Km and Vmax are both
low
31
what increases after a meal
glucokinase
32
when blood glucose is low - it is released from the liver via
gluconeogenesis
33
when blood sugar levels are low
Glucokinase also low
34
isoenzymes
different enzymes that catalyse the same reaction
35
hexokinase is in
muscle
36
Glucokinase is in the
liver
37
electrophoresis is useful to
separate plasma protein
38
elevation of CK2 indicates
myocardial infarction
39
Catalysing reaction with two or more substrates usually involved
transfer of groups from one substrate to the other
40
In an ordered sequential reaction mechanism the enzyme exists in a .............. structure
ternary
41
Lactate dehydrogenase catalyses
pyruvate to lactate co enzyme needed: NADH
42
example of random sequential mechanism
phosphocreatine from creatine
43
Allosteric enzymes are made up of
many subunits, which contain many active sites
44
3 things that can change the way an enzyme functions
temperature pH inhibitors
45
feedback inhibition
build up at the end product of a pathway can slow the entire pathway
46
allosteric effectors bind to a site that is not the ........... which changes the enzymes structure
active site
47
allosteric enzymes concerted model
each subunit exists in two different conformations one binds substrate and the other doesn't
48
allosteric enzymes sequential model
no flipping between conformation sites substrate binding causes a change in ONE subunit
49
Different ways inhibitors can effect enzymes
Competitive inhibitor Non-competitive inhibitor Irreversible inhibitor Feedback inhibition
50
Proproteins can be cleaved to give active enzyme by
proteases