Enzymes Flashcards

(58 cards)

1
Q

Majority of the chemical reactions in our body are catalyzed by proteins known as?

A

enzymes

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2
Q

____, which are large molecules that increase the rates of chemical reactions without themselves undergoing any change.

A

enzymes

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3
Q

Majority of the enzymes in our body are what type of proteins?

fibrous or globular

A

globular

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4
Q

____ are enzymes made of ribonucleic acids. They catalyze the self-cleavage of certain portions of their own molecules

A

Ribozymes

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5
Q

Like all catalysts, enzymes do not change the chemical what? They, rather, increase the what?

singilan time!!!

A

chemical equilibrium; reaction rate

enzymes do not change equi just rxn rates

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6
Q

Enzymes cause reactions to occur faster by lowering or adjusting the?

A

activation energy

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7
Q

Enzymes increase ____ by anywhere from 109 to 10</sup>20</sup> times

A

reaction rates

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8
Q

A characteristic of an enzyme wherein it is being choosy, to the point of being able to distinguish between the stereoisomers of the same molecule

A

specific

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9
Q

what enzyme catalyzes the hydrolysis of peptide bonds of proteins on the C-side of K & R?

A

Trypsin

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10
Q

what enzymes specifically catalyze the hydrolysis of only the last amino acid on a protein chain – the one on the C-terminal end?

A

Carboxypeptidases

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11
Q

What do you call the enzymes that catalyze the hydrolysis of any triglyceride, but still do not affect carbohydrates or proteins?

A

Lipases

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12
Q

What do you call the protein-splitting enzymes that are in the blood, ready to promote clotting?

A

Proteases

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13
Q

Identify the group of enzyme

catalyze oxidations and reductions

redox reactions or transfer of electrons

A

Oxidoreductases

EC1

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14
Q

Identify the group of enzyme

catalyze the transfer of a group of atoms, such as from one molecule to another

transfer of a group from one substrate to another

A

Transferases

EC2

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15
Q

Identify the group of enzyme

catalyze hydrolysis reactions

addition of water to break bonds

A

Hydrolases

EC3

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16
Q

Identify the group of enzyme

catalyze the addition of two groups to a double bond or the removal of two groups from adjacent atoms to create a double bond

addition of groups to double bonds or removal to form double bonds

A

Lyases

EC4

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17
Q

Identify the group of enzyme

catalyze isomerization reactions

convertion of substrate into its isomer

A

Isomerases

EC5

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18
Q

Identify the group of enzyme

catalyze the joining of two molecules

Joining 2 molecules with the hydrolysis of ATP

A

Ligases

EC6 or synthetases

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19
Q

Identify the group of enzyme

helping the protein move across the cell membrane

this is new btw

A

Translocase

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20
Q

what do you call the measure of how fast an enzyme is able to catalyze the reaction?

A

Enzyme activity

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21
Q

In an enzymatic reaction, what do you call the molecule being acted upon?

A

Substrate

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22
Q

What do you call nonprotein parts of enzymes necessary for catalytic function?

A

cofactors

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23
Q

what do you call organic molecules that act as cofactors?

A

Coenzymes

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24
Q

What do you call the 3-D cavity of the enzyms with specific chemical properties to accommodate the substrate?

25
What do you call the process that increases the action of an enzyme?
Activation
26
What do you call the process by which a compound binds to an enzyme and lowers its activity?
Inhibition
27
If we keep the concentration of the substrate constant and increase the concentration of enzyme, what will happen to the rxn rate? | increases or decreases
increases | increases linearly
28
# True or False If the enzyme concentrations double, will the rxn rate double as well?
Yes ## Footnote bcoz molar concentration of enzyme is almost always much lower than that of substrate
29
If we increase the substrate concentration and keep enzyme concentration constant, what will happen to the rxn rate? | increases or decreases
increases ## Footnote but reaches a point where rxn rate stays the same even if substrate conc is increased
30
The rxn rate does not increase when substrate conc is further increased at constant enzyme conc. Why? ## Footnote Saturation curve = substrate conc up, enzyme conc constant
(at saturation) substrate molecules are bound to all active sites of an enzyme ## Footnote Increasing the substrate concentration can no longer increase the rate because the excess substrate **cannot find any active sites** to which to bind
31
When temperature is increased in a catalyzed reaction, what will happen to rxn rate?
increases
32
What will happen to the rxn rate when you go beyond the optimal temperature and pH? | increases or decreases
decreases
33
After a small temperature increase above the optimum, the decreased rate could be increased again by doing what?
lowering the temperature
34
Arrhenius suggested that catalysts speed up reactions by combining with the substrate to form some kind of intermediate compound called?
enzyme-substrate complex
35
What do you call the limitation of an enzyme to catalyze specific reactions with specific substrates?
substrate specificity
36
# Identify the enzyme-substrate complex enzyme is a rigid 3-D body wherein active site has a restricted opening into which only one kind of substrate can fit
Lock-and-Key model
37
# Identify the enzyme-substrate complex size and shape of the active site change when substrate enters ## Footnote comparison of changes occurring in the shape of the cavity upon substrate binding to the changes in the shape of a glove when a hand is inserted
Induced-fit model
38
What do you call a molecule that reduces the activity of an enzyme?
inhibitor
39
What do you call the activity-reductor of enzymes wherein they bind to enzymes and then never let go? | renders the enzyme less productive
irreversible inhibitor
40
What do you call the activity-reductors of enzymes that unbind to restore its activity to its initial level?
reversible inhibitors
41
# Identify the type of reversible inhibitor while bound to the active site of the enzyme, substrate cannot bind
competitive inhibitor
42
# Identify the type of reversible inhibitor binds not to the active site of the enzyme. its binding changes the shape of the enzyme, rendering it less efficient
noncompetitive inhibitor
43
# True or False When a competitive inhibitor is present, maximum rxn rate may take place if and only if substrate conc is increased
True ## Footnote inhibitor will be displaced from the active site in accord with Le Chatelier's principle
44
# True or False In the presence of a noncompetitive inhibitor, maximum rxn rate may take place if and only if substrate conc is increased
False ## Footnote noncompetitive inhibitors cannot be displaced by substrates kasi hindi naman sa active sites naka-bind. Therefore, maximum rxn rate will be **lower** than it would be in the absence of an inhibitor
45
What do you call the enzyme regulation process in which formation of a product inhibits an earlier reaction in the sequence?
Feedback control
46
What do you call the inactive forms of enzymes wherein a polypeptide chain must be removed to make them active?
Proenzymes or Zymogens ## Footnote trypsin & chymotrypsin (from -gen precursors); trypsin (from trypsinogen) catalyzes chymotrypsinogen to chymotripsin
47
What do you call the regulation that takes place by means of an event that occurs at a site other than the active site?
Allosterism | any enzyme regulated by this is called allosteric enzyme
48
If a molecule or a substance binds other than the active site, it may enhibit enzyme action wherein the process is called? when enzyme action is stimulated in this process, it is called?
negative modulation; positive modulation
49
the substance that binds to an allosteric enzyme is called a what?
regulator
50
what do you call the site wherein the substance of an allosteric enzyme binds to?
regulatory site
51
What do you call the enzymes that perform the same function but have different combinations of subunits (& diff quaternary structures)?
Isozymes or Isoenzymes
52
What do you call the enzyme derived from yeast?
Invertase
53
This enzyme splits sucrose to gluctose and fructose and classified as a hydrolase
Invertase ## Footnote cleaves glycosidic bonds at a1 b2
54
What is used to monitor enzyme activity in the experiment? | may be colored red or yellow
3, 5-dinitrosalicylic acid (DNS)
55
when dinitrosalicylic acids reacts with sugars to form 3-amino-5-nitrosalicylic acid, what color will be shown?
Red ## Footnote DNS does not react with sucrose
56
Red coloration in dinitrosalicylic acid means that enzyme is active, indicating that the concentration of gluc & fruc is? | high or low
high | higher [gluc] & [fruc] = higher invertase activity
57
What is the official name of Invertase?
B-fructofuranosidase
58
EC classification of Invertase (full)
EC 3.2.1.26