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lmao > Enzymes > Flashcards

Enzymes Flashcards

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?

A

Active site

25
Q

What do you call the process that increases the action of an enzyme?

A

Activation

26
Q

What do you call the process by which a compound binds to an enzyme and lowers its activity?

A

Inhibition

27
Q

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

A

increases

increases linearly

28
Q

True or False

If the enzyme concentrations double, will the rxn rate double as well?

A

Yes

bcoz molar concentration of enzyme is almost always much lower than that of substrate

29
Q

If we increase the substrate concentration and keep enzyme concentration constant, what will happen to the rxn rate?

increases or decreases

A

increases

but reaches a point where rxn rate stays the same even if substrate conc is increased

30
Q

The rxn rate does not increase when substrate conc is further increased at constant enzyme conc. Why?

Saturation curve = substrate conc up, enzyme conc constant

A

(at saturation) substrate molecules are bound to all active sites of an enzyme

Increasing the substrate concentration can no longer increase the rate because the excess substrate cannot find any active sites to which to bind

31
Q

When temperature is increased in a catalyzed reaction, what will happen to rxn rate?

A

increases

32
Q

What will happen to the rxn rate when you go beyond the optimal temperature and pH?

increases or decreases

A

decreases

33
Q

After a small temperature increase above the optimum, the decreased rate could be increased again by doing what?

A

lowering the temperature

34
Q

Arrhenius suggested that catalysts speed up reactions by combining with the substrate to form some kind of intermediate compound called?

A

enzyme-substrate complex

35
Q

What do you call the limitation of an enzyme to catalyze specific reactions with specific substrates?

A

substrate specificity

36
Q

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

A

Lock-and-Key model

37
Q

Identify the enzyme-substrate complex

size and shape of the active site change when substrate enters

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

A

Induced-fit model

38
Q

What do you call a molecule that reduces the activity of an enzyme?

A

inhibitor

39
Q

What do you call the activity-reductor of enzymes wherein they bind to enzymes and then never let go?

renders the enzyme less productive

A

irreversible inhibitor

40
Q

What do you call the activity-reductors of enzymes that unbind to restore its activity to its initial level?

A

reversible inhibitors

41
Q

Identify the type of reversible inhibitor

while bound to the active site of the enzyme, substrate cannot bind

A

competitive inhibitor

42
Q

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

A

noncompetitive inhibitor

43
Q

True or False

When a competitive inhibitor is present, maximum rxn rate may take place if and only if substrate conc is increased

A

True

inhibitor will be displaced from the active site in accord with Le Chatelier’s principle

44
Q

True or False

In the presence of a noncompetitive inhibitor, maximum rxn rate may take place if and only if substrate conc is increased

A

False

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
Q

What do you call the enzyme regulation process in which formation of a product inhibits an earlier reaction in the sequence?

A

Feedback control

46
Q

What do you call the inactive forms of enzymes wherein a polypeptide chain must be removed to make them active?

A

Proenzymes or Zymogens

trypsin & chymotrypsin (from -gen precursors); trypsin (from trypsinogen) catalyzes chymotrypsinogen to chymotripsin

47
Q

What do you call the regulation that takes place by means of an event that occurs at a site other than the active site?

A

Allosterism

any enzyme regulated by this is called allosteric enzyme

48
Q

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?

A

negative modulation; positive modulation

49
Q

the substance that binds to an allosteric enzyme is called a what?

A

regulator

50
Q

what do you call the site wherein the substance of an allosteric enzyme binds to?

A

regulatory site

51
Q

What do you call the enzymes that perform the same function but have different combinations of subunits (& diff quaternary structures)?

A

Isozymes or Isoenzymes

52
Q

What do you call the enzyme derived from yeast?

A

Invertase

53
Q

This enzyme splits sucrose to gluctose and fructose and classified as a hydrolase

A

Invertase

cleaves glycosidic bonds at a1 b2

54
Q

What is used to monitor enzyme activity in the experiment?

may be colored red or yellow

A

3, 5-dinitrosalicylic acid (DNS)

55
Q

when dinitrosalicylic acids reacts with sugars to form 3-amino-5-nitrosalicylic acid, what color will be shown?

A

Red

DNS does not react with sucrose

56
Q

Red coloration in dinitrosalicylic acid means that enzyme is active, indicating that the concentration of gluc & fruc is?

high or low

A

high

higher [gluc] & [fruc] = higher invertase activity

57
Q

What is the official name of Invertase?

A

B-fructofuranosidase

58
Q

EC classification of Invertase (full)

A

EC 3.2.1.26

lmao (14 decks)

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