Enzymes Flashcards

1
Q

What are the 2 subfields of Enzymology?

A

kinetics and structural biology

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2
Q

Enzymology is the study of

A

enzymic reaction mechanisms, regulations, and rates.

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3
Q

Enzymes are the

A

biochemical catalysts that are usually proteins, but can also consist of RNA.

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4
Q

What is the purpose of Catalyst?

A

speed up the rate of the reaction

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5
Q

The protein (or RNA) folds into a structure

A

binding a substrate, forming a product. The product is released from the enzyme.

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6
Q

Catalyst are not

A

consumed or altered in the reaction

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7
Q

Catalyst don’t change in

A

Keq (equilibrium constant) or ∆G⁰ of the process (∆G⁰ = -RT ln Keq

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8
Q

Enzymes increase the rate of reactions, in what direction?

A

both directions

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9
Q

Certain fraction of A+B has enough

A

energy to achieve transition state

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10
Q

Enzymes do not change the

A

equilibrium point of reactions.

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11
Q

Transition states are higly

A

reactive and are high-energy state

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12
Q

Enzyme activity is often tightly

A

regulated

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13
Q

When it comes to the conformational change, what state is the molecule in during the transition stage

A

‘half-chair’ conformation

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14
Q

∆G ‡ ensures the reaction

A

does not always occur

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15
Q

∆G ‡ is also known as the

A

activation energy

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16
Q

What are 2 ways to speed up a reaction

A

Lower ∆G ‡
o Raise T

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17
Q

What would happen if you raise the temperature in a reaction

A

T+10ºC = 2X rate

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18
Q

the active site of an enzyme is

A

is complementary to the substrate.

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19
Q

Enzymes and substrate connect via

A

weak noncovalent bonds

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20
Q

Enzymes lower the activation energy of the transition state by

A

having a smaller delta S between the [ES] and [EX] complex.

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21
Q

Under what conditions does enzyme work in

A

under mild conditions (37ºC, 1 atm, pH 7

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22
Q

Under what conditions does chemical catalyst work

A

optimal under extreme conditions

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23
Q

What are the type of bond between substrate and enzyme

A

Geometric or electronic

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24
Q

The lock and key model explains

A

specificity but not stabilization of the intermediate shape of
the substrate

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25
The induced fit model explains
stability of ES complex with limits (no real distortion)
26
What are the matter involved for chemical catalysts
acid, bases, or metals
27
Enzymes typically have
1 substrate/1 enzyme
28
Enzymes have no
non-productive side reactions
29
What are the systemic name for enzymes/ nonmenclature
substrate+ ase
30
What are serine proteases
a class of peptidases with Ser in the active site
31
How are serine proteases grouped together
into 13 clans by catalytic mechanismes and 40 families by seq homology
32
What are the major clans in humans for serine proteases
chymotrypsin-like
33
chymotrypsin-like is
subtilisin-like, the α/β hydrolase, and signal peptidase clan
34
Serine proteases participate in
a wide range of functions in both prokaryotes and eukaryotes like blood clotting, immunity, inflammation, digestion
35
What are some Chymotrypsin-like serine proteases
Chymotrypsin,trypsin, and elatase
36
Chymotrypsin-like serine proteases are synthesized by
pancreatic acinar cells and secreted into the small intestince
37
Whats the difference between Chymotrypsin, trypsin, and elastase
the peptide bond being cleaved
38
Chymotrypsin has a big
hydrophobic pocket at active site
39
What are the bulky hydrophobic amino acids for Chymotrypsin
Tyr, Trp, Phe, MEt
40
Trypsin prefers
Lys or Arg
41
Elastase prefers
Ala, Gly, or Val
42
Where is the catalytic traid
in the active site
43
Asp
102
44
His
57
45
Ser
195
46
Serine acts as a
nucleophile
47
Hisditine has ability to
accept H from the serine -OH groupSe
48
Serine attacks the
carbonyl carbon of the scissile bond of the substrate
49
the peptide bond being cleaved is called the
scissile bond
50
Histidine coordinates the
attack of the peptide bond by the serine
51
Aspartic acid makes.
H-bond by the serine
52
Apartic acid makes the pair of
electrons on the histidine much more electronegative
53
Zymogens are the
inactive percusors
54
Zymogen is large
inactive structure that goes to smaller active enzyme
55
Zymogen active site
is hidden or distored and is actived only at the right location
56
What are some cofactors
metal ions and coenzymes
57
Cosubstrates are
loosely bound and cycle is one and off
58
prosthetic groups are tightly.
covalently bound.
59
What vitamins coenzymes are water soluble
Vitamins B and C
60
What vitamins are lipid-soluble
Vitamins A,D,E,K