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Biochemistry Finals > Enzymes > Flashcards

Enzymes Flashcards

1
Q

They govern all chemical reactions in living organisms. They are specialized proteins that with fascinating precision and selectivity, catalyze metabolic reactions that store and release energy, make pigments in our hair and eyes, digest the food we eat, synthesize cellular building materials and protect us by repairing cellular damage and clotting our blood.

A

Enzymes

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2
Q

Without this, most chemical reactions in biochemical systems would occur too slowly to produce adequate amounts of the substances needed for cells to function properly. In some cases, needed reactions would not occur at all without their presence.

A

enzymes

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3
Q

It is an organic compound that acts as a
catalyst for biochemical reaction.

A

Enzyme

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4
Q

The word enzyme come from the greek word ____ - which means ___ and ____– which means ____.

A

en ; in
Zyme ; yeast

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5
Q

Enzymes undergo _______ also, which means slightly alteration in pH, temperature or other proteins denaturants affect the enzyme
activity.

A

denaturation

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6
Q

it is an enzyme composed only
protein (amino acid chains)

A

Simple Enzymes

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7
Q

It is an enzyme that has nonprotein part in addition to a protein part.

A

Conjugated Enzymes

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8
Q

It is the biochemically active conjugated enzyme produced from an
apoenzyme and a cofactor.

A

HOLOENZYME

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9
Q

It is a non protein part of conjugated
enzyme.

A

Cofactor

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10
Q

It is a protein part of a conjugated
enzyme.

A

Apoenzyme

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11
Q

HOLOENZYME is the biochemically active conjugated enzyme produced from an ______ and a ______.

A

apoenzyme ; cofactor

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12
Q

It is the reactant in an enzyme-catalyzed reaction ; is the substance upon which the enzyme acts.

A

Substrate

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13
Q

Suffix ___ that identifies a substance as an enzyme.

A

–ase

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14
Q

Suffix _____ are also digestive enzymes

A

in

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15
Q

The type of reaction catalyzed by an enzyme is often noted with ___________.

A

prefix

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16
Q

It is an enzyme that catalyzes an oxidation – reduction reaction.

A

OXIDOREDUCTASE

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17
Q

It is an enzyme that catalyzes the transfer of a functional group from one molecule to another.

A

TRANSFERASE

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18
Q

Two major subtypes of transferases:

A

transaminases and kinases

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19
Q

Transfer of an amino group between Substrates

A

transaminases

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20
Q

Transfer of a phosphate group between substrates

A

kinases

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21
Q

It is an enzyme that catalyzes a hydrolysis reaction in which the addition of water molecule to a bond causes the bond to break.

A

HYDROLASE

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22
Q

hydrolysis of ester linkages in lipids.

A

Lipases

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23
Q

hydrolysis of amide linkages in proteins

A

Proteases

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24
Q

hydrolysis of sugar–phosphate ester bonds in nucleic acids

A

Nucleases

25
Q

hydrolysis of glycosidic bonds in carbohydrates

A

Carbohydrases

26
Q

hydrolysis of phosphate–ester bonds

A

Phosphatases

27
Q

It is an enzyme that catalyzes the addition of a group to a double bond or the removal of a group to form a double bond in a manner that does not involve hydrolysis or oxidation

A

LYASES

28
Q

removal of H2O from a substrate

A

Dehydratases

29
Q

removal of CO2 from a substrate

A

Decarboxylases

30
Q

removal of NH3 from a substrate

A

Deaminases

31
Q

addition of H2O to a substrate

A

Hydratases

32
Q

It is an enzyme that catalyze the
isomerization (rearrangement of atoms) of substrate in a reaction converting it into a molecule isomeric with itself.

A

ISOMERASE

33
Q

conversion of D isomer to L isomer, or vice versa

A

Racemases

34
Q

transfer of a functional group from one position to another in the same molecule

A

Mutases

35
Q

is an enzyme that catalyzes the bonding together of 2 molecules into one with the participation of ATP.

A

LIGASE

36
Q

formation of new bond between two substrates, with participation of ATP

A

Synthetases

37
Q

formation of new bond between a substrate and CO2, with participation of ATP

A

Carboxylases

38
Q

is relatively small part of an enzyme
structure that is actually involved in catalysis.

A

Active site

39
Q

is the intermediate reaction species that is formed when substrate binds to the active site of enzyme.

A

ENZYME-SUBSTRATE COMPLEX

40
Q

In this model, the active site in the enzyme has a fixed rigid geometrical conformation. Only substrate with a complementary geometry can be accommodated at such site.

A

lock and key model

41
Q

This model allows small changes in the shape or geometry of the active site of an enzyme to accommodate a substrate.

A

induced fit model

42
Q

is a measure of the rate at which an enzyme converts substrate to products in a biochemical reaction.

A

Enzyme activity

43
Q

Factors that affects Enzyme activity

A
  • Temperature
  • pH
44
Q

Enzymes exhibit different levels of selectivity or specificity for substrates.

A
  1. Absolute specificity
  2. Stereochemical specificity
  3. Group specificity
  4. Linkage specificity
45
Q

the enzyme will catalyze
only one particular reaction.

A

Absolute specificity

46
Q

Because amino acid are chiral compounds L- Amino acid to L- amino acid

A

Stereochemical specificity

47
Q

similar compound with same
functional group example carboxypeptidase. It cleaves amino acids one at a time from the carboxyl
end of the peptide chain.

A

Group specificity

48
Q

involves a particular type of bond. Phosphatases hydrolyze phosphate-ester bond.

A

Linkage specificity

49
Q

is a substance that slows or stops the
normal catalytic function of an enzyme by binding to it

A

INHIBITORS

50
Q

The rates of enzyme-catalyzed reactions can be decreased by a group of substance called ________

A

INHIBITORS

51
Q

Three modes by which inhibition takes place are considered:

A
  1. Reversible Competitive Inhibition
  2. Reversible Noncompetitive Inhibition
  3. Irreversible Inhibition
52
Q

is a molecule that sufficiently resembles an enzyme substrate in shape and charge distribution that it can compete with the substrate for occupancy of the enzyme active site.

A

Competitive Enzyme Inhibitor

53
Q

is a molecule that decreases enzyme activity by binding to a site on an enzyme other than the active site.

A

Noncompetitive Enzyme Inhibitor

54
Q

This inhibitor binds to a site other than the active site; the normal substrate still binds to the active site but the enzyme cannot catalyze the reaction due to the presence of the inhibitor

A

noncompetitive inhibitor

55
Q

is a molecule that inactivates
enzyme by forming a strong
covalent bond to an amino acid side chain group at the enzyme’ active site.

A

Irreversible Enzyme Inhibitor

56
Q

Substances that bind to an enzyme and stop or slow its normal catalytic activity

A

ENZYME INHIBITORS

57
Q

A molecule closely resembling the substrate. Binds to the active site and temporarily prevents substrates from occupying it, thus blocking the reaction.

A

Competitive Enzyme Inhibitor

58
Q

A molecule that binds to a site on an enzyme that is not the active site. The normal substrate still occupies the active site but the enzyme cannot catalyze the reaction due to the presence of the inhibitor.

A

Noncompetitive Enzyme Inhibitor

59
Q

A molecule that forms a covalent bond to a part of the active site, permanently preventing substrates from occupying it.

A

Irreversible Enzyme Inhibitor

Biochemistry Finals (4 decks)

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