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Biochemistry > Enzymes > Flashcards

Enzymes Flashcards

1
Q

Are enzymes important to living things

A

Yes

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2
Q

what is enzymology

A

study of enzymes

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3
Q

Do enzymes randomly/ selectively catalyze chemical reactions

A

selectively

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4
Q

Chemical catalysis are done in which conditions

A

,Mild reaction

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5
Q

Is it important for enzymes to be catalyzed?

A

Yes, because the regualtion is based on whether it is inhibiting or catalyzing a reaction

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6
Q

What is the specificity of enzyme in respect to substrates and products

A

greater reaction specificity

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7
Q

What is the impact of enzymes on reaction rates compared to uncatalyzed and chemically catalyzed reactions

A

it is increased/higher

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8
Q

For an uncatalyzed reaction, how long is peptide bond hydrolysis

A

450 years

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9
Q

Catalyzed reaction half times are in

A

milliseconds

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10
Q

nitrogen fixation is catalyzed by

A
  1. Lightning
  2. Haber process (nitrogen fixation) using symbiotic bacteria in root nodule sof legumes
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11
Q

Why can you use symbiotic bacteria for nitrogen fixation

A

They carry the nitrogenase enzyme inside of them

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12
Q

An example of a milder reaction using enzyme is

A

nitrogen fixation

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13
Q

What happens to methanol (CH3OH) and NAD+ in the presence of Alcohol dehydrogenase

A

they produce NADH and formaldehyde (CHO)

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14
Q

What happens to a person that undergoes methanol poisoining

A

vomiting, going blind. alcohol dehydrogenase forms formaldehyde which can attack the eyes

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15
Q

A person has ethanol(CH3CH2OH) poisoning, what can you do to help that person?

A

give them high levels of methanol to compete with ethanol

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16
Q

Enzymes have greater reaction specificty with respect to

A

substrate and product

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17
Q

Why does stereospecificity in products

A

so it can orient to the active site to the enzyme

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18
Q

The regulation of the activity of an enzyme by binding of an inhibitor or activator at a site is called

A

Allostery

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19
Q

Phosphorylation, acetylation, removal of inhibitory peptides are all ways to

A

Covalently modification

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20
Q

Ways to regulate enzyme

A

Allostery
Covalent modification
Macromolecules complexes
Feedback inhibition

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21
Q

What is the regulation of a metabolic pathway by the inhibition of an enzyme that catalyzes a reaction early in pathway of the product

A

Feedback inhibition

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22
Q

An active site is also known as

A

Catalytic state

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23
Q

AN enzyme that has nothing bound to it is known as

A

Apoenzyme/apoprotein

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24
Q

What makes an holoenzyme

A

binding of a cofactor or coenzyme makes it from apoenzyme to holoenzyme

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25
Q

ATP + D-glucose&raquo_space;>

A

ADP + D-glucose-6-phosphate

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26
Q

what are some molecules that are required by some enzyme to catalyze reaction

A

cofactor

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27
Q

What are generally organic cofactors often derived from vitamins required as carriers of specific atoms

A

Coenzyme

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28
Q

When cofactors are tightly bound is known as

A

Prosthetic group

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29
Q

what is the corn-based diet called

A

Pellagra

30
Q

Pellagra can be prevented by

A

Nixtamalization

31
Q

Pellagra is defined by which characteristics

A

Dementia, diarrhea, dermatitis

32
Q

What is a co-enzyme dietary precursor in mammals for corn based diet

A

Niacin through alkali treatment

33
Q

Is biochemical reaction thought about in the standard conditions

A

no, in biochemical condition

34
Q

What is the symbol for biochemical standard free energy change

A

delta G’

35
Q

Does enzyme change both delta G (ΔG0’) in thermodynamics and delta G( ΔG‡) in kinetics

A

no, they can only change delta G in kinetics of how FAST it will happen.

36
Q

If we have a big activation energy, how does that affect k, and the reaction

A

The bigger delta G is, smaller k and slower the reaction

37
Q

When ΔG0’ < 0, which reaction is favorable

A

forward rxn is favorable

38
Q

When ΔG0’> 0, whcih reaction is favorable

A

reverse rxn is favorable

39
Q

when ΔG0’ =0, what state is the reaction in

A

equilibrium equal state of S and P

40
Q

if (ΔG‡) is big enough, what happens to reaction

A

never reaches equilibrium, no matter how negative ΔG0’

41
Q

What do enzyme do when ΔG‡ is too big

A

they lower the ΔG‡ but never touch the ΔG0’

42
Q

Do enzymes always stay bound or recatalyze to a product

A

recatalyze

43
Q

Which k is the rate limiting step?

A

the one with the highest energy barrier (smallest rate constant k)

44
Q

In a reaction when the enzyme is complementary to the substrate, how many products

A

few products

45
Q

Why does a reaction which enzyme complementray have few products

A

because they are locked in and tehy do not go to transition state

46
Q

What happens when enzyme is complementary to transition state

A

It bends it in the transitions state to form products

47
Q

What happens to the energy needed to get to transition state

A

it it lowered by ΔGm / ΔGB

48
Q

How do enzyme affect a reaction

A

they lower the activity energy making the reaction reach product faster

49
Q

Catalytic power of enzymes are derived from

A
  1. binding energy ΔGB resulting from many weak interactions/bonds with substrate
  2. Binding is optimized in the transition state
50
Q

BInding energy ΔGB contributes to

A

specificity and catalysis

51
Q

Enzymes bind preferably in what state

A

transition state

52
Q

Why is the function of a protein/enzyme so closely tied to its structure

A

protein are cradle for active sites

53
Q

What are some of the things ΔGB must overcome?

A
  1. Entropy reduction
    2.Desolvation of substrates
  2. Distortion of substrates
  3. Catalytic functional groups on E must be aligned
54
Q

Types of entropy reduction

A

UNCATALYZED BIMOLECULAR RECTIONS
Uncatalyzed unimolecular reactions
Catalyzed reactions

55
Q

The conversion of two free reactants&raquo_space;> single restricted transition state is

A

entropically unfavorable

56
Q

The conversion of a flexible reactant»»>rigid transition state is

A

entropically unfavorable for flexible reactants

57
Q

The entropy cost of catalyzed reaction is paid during

A

binding

58
Q

Rigid reactant complex&raquo_space;> rigid transition state is what conversion

A

entropically ok, becaause enzymes catalyze

59
Q

The rate enhancement is highest in which entropy reduction rxn

A

catalyzed reaction

60
Q

The interactions between Subtrate (S) and water replaced by interaction between S and E is called

A

Desolvation of substrates

61
Q

Weak interactions with E only occur in transition state compensating for energy required to distort bonds. this is known as

A

Distortion of subtrates

62
Q

Why must catalytic functional groups on E be properly aligned ?

A

to produce an induced fit for binding

63
Q

What are some other methods a single enzyme can catalyze a reaction apart from transition state

A
  1. General acid-base catalysis
  2. Covalent catalysis
  3. Metal Ion catalysis
64
Q

in which catalysis is the charged intermediates not stable and can decay to reactants

A

Acid-base catalysis

65
Q

What 2 groups are involved in the acid-base catalysis

A

hydroxyl and carbonyl group

66
Q

What will enzymes do in a catalyzed base reaction where the intermediate is unstable?

A

serve as desolvation of water molecules, serve as a hold of water molecules, pushing rxn forward

67
Q

this reaction occurs generally happens in the presence of acid-base making a substrate covalent complex

A

Covalent catalylsis

68
Q

What is the result of the covalent catalysis

A

a new pathway that is faster than the uncatalyzed rxn.

69
Q

when the metals orient substrates, contributing to binding energy, redox state, this is called

A

Metal ions

70
Q

In the metal ion catalysis, what can metals do

A

contribute to binding energy
orient substrates
change redox state

Biochemistry (16 decks)

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