Chapter 19

Question 1

Which enzyme does oxidation reduction reactions?

Answer 1

Oxidoreductases

Question 2

Which enzyme transfers groups of atoms?

Answer 2

Transferases

Question 3

Which enzyme can perform hydrolysis?

Answer 3

Hydrolases

Question 4

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

Answer 4

Lyases

Question 5

Which enzyme interconverts isomers?

Answer 5

Isomerases

Question 6

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

Answer 6

Ligases

Question 7

Which enzyme can translocate things across membranes?

Answer 7

Translocases

Question 8

What affect reaction rates of enzymes?

Answer 8

Substrate concentration
Enzyme concentration
Temperature
pH

Question 9

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

Answer 9

Cutoff

Question 10

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

Answer 10

Enzyme

Question 11

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

Answer 11

Lower activation energy

Question 12

What are some characteristics of enzymes?

Answer 12

Usually globular
Water soluble proteins
Very specific

Question 13

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

Answer 13

Cofactors

Question 14

What are some examples of cofactors?

Answer 14

Metal ions and coenzymes

Question 15

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?

Answer 15

Metal ions

Question 16

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

Answer 16

Metal ions

Question 17

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

Answer 17

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

Question 18

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

Answer 18

Double
Triple

Question 19

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

Answer 19

Increase

Question 20

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

Answer 20

Activation

Question 21

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

Answer 21

Inhibition

Question 22

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

Answer 22

Reversible and irreversible

Question 23

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

Answer 23

Non competitive

Question 24

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

Answer 24

Competitive inhibition, undergoes no reaction

Question 25

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?

Answer 25

Irreversible inhibitors

Question 26

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

Answer 26

Allosteric control

Question 27

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

Answer 27

Noncovalent binding of a regulator

Question 28

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?

Answer 28

Positive

Question 29

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?

Answer 29

Negative regulator

Question 30

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

Answer 30

Feedback control

Question 31

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

Answer 31

Zymogen/ proenzyme

Question 32

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

Answer 32

Serine, tyrosine, threonine Phosphorylation

Question 33

Why are vitamins needed for life?

Answer 33

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

Question 34

What are the water soluble vitamins?

Answer 34

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

Question 35

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

Answer 35

Fat soluble since they are stored in fat deposits

Question 36

Are both water and lipid soluble vitamins coenzymes?

Answer 36

Lipid soluble are not, not all water soluble are

Question 37

What do antioxidants do?

Answer 37

Prevent oxidation by reacting with oxidizing agents

Question 38

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

Answer 38

Antioxidants

Question 39

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

Answer 39

Minerals

Question 40

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

Answer 40

Class: oxidoreductases Subclasses: oxidases, reductases, dehydrogenases

Question 41

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

Answer 41

Class: transferases Subclass: transaminases and kinases

Question 42

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

Answer 42

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

Question 43

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

Answer 43

Class: Isomerases No subclasses

Question 44

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

Answer 44

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

Question 45

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

Answer 45

Class: ligases Subclasses: synthetases and carboxylases

Question 46

Vitamin _____ causes scurvy and epithelial and mucosal deterioration

Answer 46

Vitamin C

Question 47

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

Answer 47

Vitamin A

Question 48

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

Answer 48

D Rickets

Question 49

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

Answer 49

Vitamin E

Question 50

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

Answer 50

Vitamin K

Question 51

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

Answer 51

B

Question 52

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

Answer 52

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

Question 53

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

Answer 53

Noncovalently bind to active site so substrate cannot enter

Question 54

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

Answer 54

Irreversible inhibitors Covalent bonds

Question 55

Why do allosteric enzymes have two types of binding sites?

Answer 55

One for catalysis One for regulation