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
Q

The induced fit model explains

A

stability of
ES complex with
limits (no real
distortion)

26
Q

What are the matter involved for chemical catalysts

A

acid, bases, or metals

27
Q

Enzymes typically have

A

1 substrate/1 enzyme

28
Q

Enzymes have no

A

non-productive side reactions

29
Q

What are the systemic name for enzymes/ nonmenclature

A

substrate+ ase

30
Q

What are serine proteases

A

a class of peptidases with Ser in the active site

31
Q

How are serine proteases grouped together

A

into 13 clans by catalytic mechanismes and 40 families by seq homology

32
Q

What are the major clans in humans for serine proteases

A

chymotrypsin-like

33
Q

chymotrypsin-like is

A

subtilisin-like, the α/β hydrolase, and signal peptidase clan

34
Q

Serine proteases participate in

A

a wide range of functions in both prokaryotes and eukaryotes like blood clotting, immunity, inflammation, digestion

35
Q

What are some Chymotrypsin-like serine proteases

A

Chymotrypsin,trypsin, and elatase

36
Q

Chymotrypsin-like serine proteases are synthesized by

A

pancreatic acinar cells and secreted into the small intestince

37
Q

Whats the difference between Chymotrypsin, trypsin, and elastase

A

the peptide bond being cleaved

38
Q

Chymotrypsin has a big

A

hydrophobic pocket at active site

39
Q

What are the bulky hydrophobic amino acids for Chymotrypsin

A

Tyr, Trp, Phe, MEt

40
Q

Trypsin prefers

A

Lys or Arg

41
Q

Elastase prefers

A

Ala, Gly, or Val

42
Q

Where is the catalytic traid

A

in the active site

43
Q

Asp

A

102

44
Q

His

A

57

45
Q

Ser

A

195

46
Q

Serine acts as a

A

nucleophile

47
Q

Hisditine has ability to

A

accept H from the serine -OH groupSe

48
Q

Serine attacks the

A

carbonyl carbon of the scissile bond of the substrate

49
Q

the peptide bond being cleaved is called the

A

scissile bond

50
Q

Histidine coordinates the

A

attack of the peptide bond by the serine

51
Q

Aspartic acid makes.

A

H-bond by the serine

52
Q

Apartic acid makes the pair of

A

electrons on the histidine much more electronegative

53
Q

Zymogens are the

A

inactive percusors

54
Q

Zymogen is large

A

inactive structure that goes to smaller active enzyme

55
Q

Zymogen active site

A

is hidden or distored and is actived only at the right location

56
Q

What are some cofactors

A

metal ions and coenzymes

57
Q

Cosubstrates are

A

loosely bound and cycle is one and off

58
Q

prosthetic groups are tightly.

A

covalently bound.

59
Q

What vitamins coenzymes are water soluble

A

Vitamins B and C

60
Q

What vitamins are lipid-soluble

A

Vitamins A,D,E,K