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

25
hydrolysis of glycosidic bonds in carbohydrates
Carbohydrases
26
hydrolysis of phosphate–ester bonds
Phosphatases
27
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
LYASES
28
removal of H2O from a substrate
Dehydratases
29
removal of CO2 from a substrate
Decarboxylases
30
removal of NH3 from a substrate
Deaminases
31
addition of H2O to a substrate
Hydratases
32
It is an enzyme that catalyze the isomerization (rearrangement of atoms) of substrate in a reaction converting it into a molecule isomeric with itself.
ISOMERASE
33
conversion of D isomer to L isomer, or vice versa
Racemases
34
transfer of a functional group from one position to another in the same molecule
Mutases
35
is an enzyme that catalyzes the bonding together of 2 molecules into one with the participation of ATP.
LIGASE
36
formation of new bond between two substrates, with participation of ATP
Synthetases
37
formation of new bond between a substrate and CO2, with participation of ATP
Carboxylases
38
is relatively small part of an enzyme structure that is actually involved in catalysis.
Active site
39
is the intermediate reaction species that is formed when substrate binds to the active site of enzyme.
ENZYME-SUBSTRATE COMPLEX
40
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.
lock and key model
41
This model allows small changes in the shape or geometry of the active site of an enzyme to accommodate a substrate.
induced fit model
42
is a measure of the rate at which an enzyme converts substrate to products in a biochemical reaction.
Enzyme activity
43
Factors that affects Enzyme activity
- Temperature - pH
44
Enzymes exhibit different levels of selectivity or specificity for substrates.
1. Absolute specificity 2. Stereochemical specificity 3. Group specificity 4. Linkage specificity
45
the enzyme will catalyze only one particular reaction.
Absolute specificity
46
Because amino acid are chiral compounds L- Amino acid to L- amino acid
Stereochemical specificity
47
similar compound with same functional group example carboxypeptidase. It cleaves amino acids one at a time from the carboxyl end of the peptide chain.
Group specificity
48
involves a particular type of bond. Phosphatases hydrolyze phosphate-ester bond.
Linkage specificity
49
is a substance that slows or stops the normal catalytic function of an enzyme by binding to it
INHIBITORS
50
The rates of enzyme-catalyzed reactions can be decreased by a group of substance called ________
INHIBITORS
51
Three modes by which inhibition takes place are considered:
1. Reversible Competitive Inhibition 2. Reversible Noncompetitive Inhibition 3. Irreversible Inhibition
52
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.
Competitive Enzyme Inhibitor
53
is a molecule that decreases enzyme activity by binding to a site on an enzyme other than the active site.
Noncompetitive Enzyme Inhibitor
54
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
noncompetitive inhibitor
55
is a molecule that inactivates enzyme by forming a strong covalent bond to an amino acid side chain group at the enzyme’ active site.
Irreversible Enzyme Inhibitor
56
Substances that bind to an enzyme and stop or slow its normal catalytic activity
ENZYME INHIBITORS
57
A molecule closely resembling the substrate. Binds to the active site and temporarily prevents substrates from occupying it, thus blocking the reaction.
Competitive Enzyme Inhibitor
58
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.
Noncompetitive Enzyme Inhibitor
59
A molecule that forms a covalent bond to a part of the active site, permanently preventing substrates from occupying it.
Irreversible Enzyme Inhibitor