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Chemistry 1120 > Chapter 19 > Flashcards

Chapter 19 Flashcards

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1
Q

Which enzyme does oxidation reduction reactions?

A

Oxidoreductases

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2
Q

Which enzyme transfers groups of atoms?

A

Transferases

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3
Q

Which enzyme can perform hydrolysis?

A

Hydrolases

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4
Q

Which enzyme can add atoms to double bond or remove atoms to form double bond/ ring?

A

Lyases

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5
Q

Which enzyme interconverts isomers?

A

Isomerases

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6
Q

Which enzyme uses the energy only of ATP to combine two molecules together?

A

Ligases

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7
Q

Which enzyme can translocate things across membranes?

A

Translocases

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8
Q

What affect reaction rates of enzymes?

A

Substrate concentration
Enzyme concentration
Temperature
pH

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9
Q

Do enzyme catalyzed reactions keep increasing with rising temperatures or is there a cutoff at some point?

A

Cutoff

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10
Q

A protein or other molecule that is a catalyst that accelerates the rate of bio molecule reactions but at the end of the reaction remain unchanged themselves

A

Enzyme

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11
Q

Do enzymes lower or raise the activation energy to decrease time for reaction to hit equilibrium?

A

Lower activation energy

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12
Q

What are some characteristics of enzymes?

A

Usually globular
Water soluble proteins
Very specific

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13
Q

Non-protein part of an enzyme that is essential to enzymes catalytic activity

A

Cofactors

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14
Q

What are some examples of cofactors?

A

Metal ions and coenzymes

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15
Q

What is able to form coordinate covalent bonds and functions as Lewis acids by accepting lone pair electrons present on N or O in enzymes?

A

Metal ions

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16
Q

What can anchor a substrate into an active site because of it being able to a accept lone pairs?

A

Metal ions

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17
Q

What is the difference between lock and key vs. induced fit?

A

Induced fit is a conformational change while lock and key is a ridged shape that cannot be changed

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18
Q

If an enzymes concentration doubles then the rate will ____. Of enzyme concentration triples then the rate will ___

A

Double
Triple

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19
Q

An increase in temperature usually _____ (increase/decrease) chemical reactions

A

Increase

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20
Q

Activation or inhibition?
Any process that initiates/ increases the action of an enzyme

A

Activation

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21
Q

Activation or inhibition?
Any process that slows down or stops the action of an enzyme

A

Inhibition

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22
Q

_____ inhibition is where the inhibitor can leave, while ______ inhibition is where the inhibitor is permanently bound to the enzyme

A

Reversible and irreversible

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23
Q

What type of inhibition doesn’t compete with the substrate for the active site and cannot bind to the enzyme alone?

A

Non competitive

24
Q

What type of inhibition competes with the substrate for binding to the active site reversibly/ noncovalently? Does it undergo a reaction if it binds?

A

Competitive inhibition, undergoes no reaction

25
Q

What type of inhibition forms a bond not easily broken with a group in the active site so the substrate can’t bond to it?

A

Irreversible inhibitors

26
Q

Interaction in which the binding of a regulator at one site affects the proteins ability to bind to another molecule at a different site

A

Allosteric control

27
Q

What had the ability to change the shape of an enzyme and the active site?

A

Noncovalent binding of a regulator

28
Q

Does a positive or negative regulator change the unavailable active site so the substrate can fit into the active site so a reaction can occur?

A

Positive

29
Q

Does a positive or negative regulator change the active site so the enzyme can’t bind the substrate to the active site to slow down the reaction?

A

Negative regulator

30
Q

Result of a process feeds information back to affect the beginning of the process

A

Feedback control

31
Q

A compound that becomes an active enzyme after undergoing a chemical change (not active until synthesized for use later)

A

Zymogen/ proenzyme

32
Q

Reversible addition phosphoryl groups to _____, _____, or _______ residue that is catalyzed by kinase enzymes is called what?

A

Serine, tyrosine, threonine
Phosphorylation

33
Q

Why are vitamins needed for life?

A

Because they cannot be synthesized in the body, must be gotten from the diet

34
Q

What are the water soluble vitamins?

A

B 1,2,3,6,12, and 5
Vitamin C

35
Q

Are water soluble or lipid soluble vitamins a higher risk for getting to much? Why?

A

Fat soluble since they are stored in fat deposits

36
Q

Are both water and lipid soluble vitamins coenzymes?

A

Lipid soluble are not, not all water soluble are

37
Q

What do antioxidants do?

A

Prevent oxidation by reacting with oxidizing agents

38
Q

Vitamin C, vitamin E, B-carotene, and the mineral selenium are all _____

A

Antioxidants

39
Q

What are transition element cofactors that are necessary for enzymes to properly function?

A

Minerals

40
Q

What class of enzyme does this reaction belong to? What are the subclasses?

A

Class: oxidoreductases
Subclasses: oxidases, reductases, dehydrogenases

41
Q

What class of enzyme does this reaction belong to? What are the subclasses?

A

Class: transferases
Subclass: transaminases and kinases

42
Q

What class of enzyme does this reaction belong to? What are the subclasses?

A

Class: Hydrolases
Subclass: lipases, proteases, amylases, nucleases

43
Q

What class of enzyme does this reaction belong to? What are the subclasses?

A

Class: Isomerases
No subclasses

44
Q

What class of enzyme does this reaction belong to? What are the subclasses?

A

Class: lyases
Subclass: decarboxylases, deanimases, dehydrogenases, hydratases

45
Q

What class of enzyme does this reaction belong to? What are the subclasses?

A

Class: ligases
Subclasses: synthetases and carboxylases

46
Q

Vitamin _____ causes scurvy and epithelial and mucosal deterioration

A

Vitamin C

47
Q

Vitamin ___ is essential for night vision and a deficiency can cause night blindness

A

Vitamin A

48
Q

Vitamin ___ is required for normal bone growth and a deficiency can cause _____

A

D
Rickets

49
Q

Vitamin ___ prevents the breakdown of vitamin A, is an antioxidant and a deficiency can cause anemia

A

Vitamin E

50
Q

Vitamin K is essential for ____ synthesis and clotting factors and a a deficiency can cause bleeding disorders

A

Vitamin K

51
Q

You have been hired to develop a drug to inhibit the action of a certain enzyme. Where should the drug bind to allosterically inhibit the enzyme?
A. To the substrate of the enzyme
B. To a site on the enzyme other than the active site
C. To the active site of the enzyme
D. To the mRNA that encodes the enzyme

A

B

52
Q

Where do noncompetitive inhibitors bind on the enzyme and what do they do?

A

Bind noncovalently away from active site
Change shape of site to make it harder to catalyze reaction

53
Q

Where do competitive inhibitors bind to and what do they do?

A

Noncovalently bind to active site so substrate cannot enter

54
Q

_____ forms ____ bonds to active site and destroys an enzymes catalytic ability

A

Irreversible inhibitors
Covalent bonds

55
Q

Why do allosteric enzymes have two types of binding sites?

A

One for catalysis
One for regulation

Chemistry 1120 (16 decks)

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