Enzymes

Question 1

Are enzymes important to living things

Answer 1

Yes

Question 2

what is enzymology

Answer 2

study of enzymes

Question 3

Do enzymes randomly/ selectively catalyze chemical reactions

Answer 3

selectively

Question 4

Chemical catalysis are done in which conditions

Answer 4

,Mild reaction

Question 5

Is it important for enzymes to be catalyzed?

Answer 5

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

Question 6

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

Answer 6

greater reaction specificity

Question 7

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

Answer 7

it is increased/higher

Question 8

For an uncatalyzed reaction, how long is peptide bond hydrolysis

Answer 8

450 years

Question 9

Catalyzed reaction half times are in

Answer 9

milliseconds

Question 10

nitrogen fixation is catalyzed by

Answer 10

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

Question 11

Why can you use symbiotic bacteria for nitrogen fixation

Answer 11

They carry the nitrogenase enzyme inside of them

Question 12

An example of a milder reaction using enzyme is

Answer 12

nitrogen fixation

Question 13

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

Answer 13

they produce NADH and formaldehyde (CHO)

Question 14

What happens to a person that undergoes methanol poisoining

Answer 14

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

Question 15

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

Answer 15

give them high levels of methanol to compete with ethanol

Question 16

Enzymes have greater reaction specificty with respect to

Answer 16

substrate and product

Question 17

Why does stereospecificity in products

Answer 17

so it can orient to the active site to the enzyme

Question 18

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

Answer 18

Allostery

Question 19

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

Answer 19

Covalently modification

Question 20

Ways to regulate enzyme

Answer 20

Allostery
Covalent modification
Macromolecules complexes
Feedback inhibition

Question 21

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

Answer 21

Feedback inhibition

Question 22

An active site is also known as

Answer 22

Catalytic state

Question 23

AN enzyme that has nothing bound to it is known as

Answer 23

Apoenzyme/apoprotein

Question 24

What makes an holoenzyme

Answer 24

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

Question 25

ATP + D-glucose >>>

Answer 25

ADP + D-glucose-6-phosphate

Question 26

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

Answer 26

cofactor

Question 27

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

Answer 27

Coenzyme

Question 28

When cofactors are tightly bound is known as

Answer 28

Prosthetic group

Question 29

what is the corn-based diet called

Answer 29

Pellagra

Question 30

Pellagra can be prevented by

Answer 30

Nixtamalization

Question 31

Pellagra is defined by which characteristics

Answer 31

Dementia, diarrhea, dermatitis

Question 32

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

Answer 32

Niacin through alkali treatment

Question 33

Is biochemical reaction thought about in the standard conditions

Answer 33

no, in biochemical condition

Question 34

What is the symbol for biochemical standard free energy change

Answer 34

delta G'

Question 35

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

Answer 35

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

Question 36

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

Answer 36

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

Question 37

When ΔG0' < 0, which reaction is favorable

Answer 37

forward rxn is favorable

Question 38

When ΔG0'> 0, whcih reaction is favorable

Answer 38

reverse rxn is favorable

Question 39

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

Answer 39

equilibrium equal state of S and P

Question 40

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

Answer 40

never reaches equilibrium, no matter how negative ΔG0'

Question 41

What do enzyme do when ΔG‡ is too big

Answer 41

they lower the ΔG‡ but never touch the ΔG0'

Question 42

Do enzymes always stay bound or recatalyze to a product

Answer 42

recatalyze

Question 43

Which k is the rate limiting step?

Answer 43

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

Question 44

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

Answer 44

few products

Question 45

Why does a reaction which enzyme complementray have few products

Answer 45

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

Question 46

What happens when enzyme is complementary to transition state

Answer 46

It bends it in the transitions state to form products

Question 47

What happens to the energy needed to get to transition state

Answer 47

it it lowered by ΔGm / ΔGB

Question 48

How do enzyme affect a reaction

Answer 48

they lower the activity energy making the reaction reach product faster

Question 49

Catalytic power of enzymes are derived from

Answer 49

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

Question 50

BInding energy ΔGB contributes to

Answer 50

specificity and catalysis

Question 51

Enzymes bind preferably in what state

Answer 51

transition state

Question 52

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

Answer 52

protein are cradle for active sites

Question 53

What are some of the things ΔGB must overcome?

Answer 53

1. Entropy reduction 2.Desolvation of substrates 3. Distortion of substrates 4. Catalytic functional groups on E must be aligned

Question 54

Types of entropy reduction

Answer 54

UNCATALYZED BIMOLECULAR RECTIONS Uncatalyzed unimolecular reactions Catalyzed reactions

Question 55

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

Answer 55

entropically unfavorable

Question 56

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

Answer 56

entropically unfavorable for flexible reactants

Question 57

The entropy cost of catalyzed reaction is paid during

Answer 57

binding

Question 58

Rigid reactant complex >>> rigid transition state is what conversion

Answer 58

entropically ok, becaause enzymes catalyze

Question 59

The rate enhancement is highest in which entropy reduction rxn

Answer 59

catalyzed reaction

Question 60

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

Answer 60

Desolvation of substrates

Question 61

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

Answer 61

Distortion of subtrates

Question 62

Why must catalytic functional groups on E be properly aligned ?

Answer 62

to produce an induced fit for binding

Question 63

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

Answer 63

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

Question 64

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

Answer 64

Acid-base catalysis

Question 65

What 2 groups are involved in the acid-base catalysis

Answer 65

hydroxyl and carbonyl group

Question 66

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

Answer 66

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

Question 67

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

Answer 67

Covalent catalylsis

Question 68

What is the result of the covalent catalysis

Answer 68

a new pathway that is faster than the uncatalyzed rxn.

Question 69

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

Answer 69

Metal ions

Question 70

In the metal ion catalysis, what can metals do

Answer 70

contribute to binding energy orient substrates change redox state