Exp 3: Enzymes Flashcards

(50 cards)

1
Q

Identify the term:
biological catalysts that accelerate the rate of biochemical reactions

A

enzymes

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2
Q

Identify the mechanism:
how enzyme accelerates the reaction rate

A

by reducing free energy activation
( a factor of up to 10^20 over an uncatalyzed reaction)

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3
Q

T/F:
an enzyme is regenerated after the reaction

A

true

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4
Q

T/F:
an enzyme changes the equilibrium of the reaction

A

false;
does not change

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5
Q

Identify the term:
suffix to identify enzyme

A

Name+ase

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6
Q

Enumerate:
chemical nature of enzymes

A
  1. majority are proteins
  2. some are RNA: ribozymes
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7
Q

T/F:
enzymes function at MILDER reaction conditions

A

true

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8
Q

T/F:
enzymes are efficient in catalyzing LOWER reaction rate than a chemical catalyst

A

false;
higher

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9
Q

T/F:
enzymes have LOW reaction specificity

A

false;
greater reaction specificity
(some catalyze the reaction of only one stereoisomer; others catalyze a family of similar reactions)

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10
Q

Identify the term:
biomolecule acted upon by the enzyme

A

substrate

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11
Q

Identify the term:
specific region of the enzyme that creates a 3D surface complementary to the substrate

A

active site

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12
Q

Enumerate:
6 classes of enzymes

A

EC 1: oxidoreductases
EC 2: transferases
EC 3: hydrolases
EC 4:lyases
EC 5: isomerases
EC 6: ligases

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13
Q

Identify the enzyme class
(based on the type of reaction catalyzed):
1. redox reactions
2. transfer of electrons
(hydride ions or H atoms)

A

oxidoreductases

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14
Q

Identify the enzyme class
(based on the type of reaction catalyzed):
transfer of a group from one substrate (donor) to another (acceptor)

A

transferases

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15
Q

Identify the enzyme class
(based on the type of reaction catalyzed):
hydrolysis (addition of H2O) of C-C, C-O, C-N and bonds like phosphoanhydride

A

hydrolases

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16
Q

Identify the enzyme class
(based on the type of reaction catalyzed):
addition (other than H2O) of groups to double bonds or removal of groups to form double bonds

A

lyases

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17
Q

Identify the enzyme class
(based on the type of reaction catalyzed):
1. convert the substrate into its isomer
2. transfer of groups within molecules to form isomers

A

isomerases

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18
Q

Identify the enzyme class
(based on the type of reaction catalyzed):
joining 2 molecules with the hydrolysis of ATP

A

ligases

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19
Q

Enumerate:
subclasses of oxidoreductases

A
  1. oxidases
  2. oxygenase
  3. hydroxylase/ monooxygenase
  4. dehydrogenase
  5. reductase
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20
Q

Identify which subclass of oxidoreductases:
introduction of one oxygen atom from a molecule of O2

A

oxidases

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21
Q

Identify which subclass of oxidoreductases:
introduction of both atoms of the O2 into the substrate

22
Q

Identify which subclass of oxidoreductases:
1 atom of O2 is introduced to the substrate and the other atom forms water

A

hydroxylase/ monooxygenase

23
Q

Identify which subclass of oxidoreductases:
redox where electrons are removed from the substrate

A

dehydrogenase

24
Q

Identify which subclass of oxidoreductases:
e- (with accompanying H+) are added to the substrate

25
Identify the enzyme class (based on the type of reaction catalyzed): cleavage of chemical bonds by the transfer of water
hydrolase
26
Enumerate: classifications of isomerase
1. epimerase 2. isomerase 3. mutase
27
Identify which type of isomerase: ribulose 5-phosphate _________
epimerase
28
Identify which type of isomerase: triose phosphate __________
isomerase
29
Identify which type of isomerase: change in position of a substituent
mutase
30
Identify other term: ligase
also known as synthetases
31
Identify: new classification of enzyme
translocases (EC 7)
32
Identify the enzyme class (based on the reaction catalyzed): assists movement of another molecule across a cell membrane
translocases
33
Enumerate: factors affecting enzyme activity
1. pH 2. temperature 3. enzyme concentration [E] 4. substrate concentration [S] 5. inhibitor 6. cofactor
34
Identify: pH at which an enzyme exhibits maximum activity (achieves Vmax/ maximum reaction rate)
optimal pH
35
Identify the degree of change in pH: alters the charge of acidic and basic amino acid residues found in active site
slight change in pH
36
Identify the degree of change in pH: denatures enzyme irreversibly; loss of catalytic activity
extreme pH (too acidic/ basic)
37
Identify: temperature at which an enzyme exhibits maximum activity
optimal temperature
38
Enumerate: what happens at ↓ temp
↓ KE = less molecular collisions = ↓ rxn rate
39
Enumerate: what happens beyond optimum T
1. disrupts 3° structure of enzyme 2. substrate may not fit the active site 3. impedes catalytic reaction
40
Identify: how E conformation is altered (may be irreversible)
by change in temperature
41
Identify the enzyme: yeast-derived enzyme
invertase
42
Identify: official name of invertase
β-fructofuranosidase (EC 3.2.1.26)
43
Determine: hydrolysis of invertase
hydrolyzes α1→β2 glycosidic bond in sucrose
44
Identify: invertase's enzyme class
hydrolase (catalyzing hydrolysis of the terminal non-reducing β-fructofuranosidase residues)
45
Fill in the blanks: Invertase splits sucrose to _________ and __________.
glucose fructose
46
Identify the method: used to monitor enzyme activity
dinitrosalicylic acid method
47
Identify: principle involved in dinitrosalicylic acid method
3,5-dinitrosalicylic acid (DNS) reacts with reducing sugars to form 3-amino-5-nitrosalicylic acid (ANS)
48
T/F: DNS reacts with sucrose (non-reducing sugar)
false; does not react
49
Identify: DNS color new color formed
DNS: yellow upon reaction: red
50
Identify: red coloration indication
↑ red coloration = ↑ [glucose & fructose] = ↑ invertase activity