L4 - Enzymes Flashcards

1
Q

From the Greek work “en” meaning “in” and
“zyme” meaning “yeast”

A

ENZYMES

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2
Q

Study of enzymes

A

Enzymology

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3
Q

composed only of protein (amino acid
chains)

A

Simple enzymes

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4
Q

has a nonprotein part in addition to a
protein part

A

Conjugated enzymes

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5
Q

the extent to which an enzyme’s activity is
restricted to a specific substrate, a specific group of
substrates, a specific type of chemical bond, or a specific
type of chemical reaction

A

ENZYME SPECIFICITY

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6
Q

the enzyme will catalyze only one
reaction

A

Absolute Specificity

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7
Q

the enzyme will act only on molecules
that have a specific functional group

A

Group Specificity

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8
Q

the enzyme will act on a particular
type of chemical bond

A

Linkage Specificity

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9
Q

the enzyme will act on a particular
stereoisomer

A

Stereochemical Specificity

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10
Q

Acted upon by the enzyme and specific

A

Substrate

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11
Q

“crevicelike” location in the enzyme

A

Active Site

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12
Q

small part of an enzyme’s structure that is
actually involved in catalysis

A

Active Site

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13
Q

binding site on the surface of an enzyme other
than the active site

A

Allosteric Site

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14
Q

different forms of an enzyme that catalyze the
same reaction in different cells or tissues of the body

A

Isoenzyme

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15
Q

the non protein part of a conjugated enzyme

A

Cofactor

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16
Q

the protein part of a conjugated enzyme

A

Apoenzyme

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17
Q

biochemically active conjugated enzyme
produced from an apoenzyme and a cofactor

A

Holoenzyme

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18
Q

Apoenzyme + Cofactor =

A

Holoenzyme

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19
Q

also called zymogen, the inactive form of a
proteolytic enzyme

A

Proenzyme

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20
Q

The suffix -ase identifies a substance as
an enzyme

A

Substrate + ase

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21
Q

is often noted in
addition to the type of reaction

A

Identity of the substrate

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22
Q

catalyzes an oxidation–reduction
reaction

A

Oxidoreductase

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23
Q

catalyzes the transfer of a functional
group from one molecule to another

A

Transferase

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23
Q

catalyzes the transfer of
an amino group from one molecule to
another

A

Transaminase

24
transfer of phosphate group from ATP to ADP + phosphorylated product
Kinases
25
catalyzes a hydrolysis reaction in which the addition of a water molecule to a bond causes the bond to break
Hydrolase
26
breaking of glycosidic bonds in oligosaccharides and polysaccharides
Carbohydrases
27
breaking of peptide linkages in proteins
Proteases
28
breaking of ester linkages in triglycerides
Lipases
29
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.
Lyase
30
removal of the components of water from a double bond
Dehydratase
31
addition of water to a double bond
Hydratase
32
catalyzes the isomerization (rearrangement of atoms) of a substrate in a reaction, converting it into a molecule isomeric with itself
Isomerase
33
catalyzes the bonding together of two molecules into one with the participation of ATP
Ligase
34
a general explanation of the velocity and gross mechanism of enzyme-catalyzed reactions
Michaelis-Menten Theory
35
highly specific way an enzyme recognizes a substrate and binds it to the active site
Lock and Key Theory
36
the flexibility of the active site allows it to adapt to the shape of the substrate
Induced-fit Model
37
a measure of the rate at which an enzyme converts substrate to products in a biochemical reaction.
Enzyme Activity
37
As the ___ of an enzymatically catalyzed reaction increases, so does the rate (velocity) of the reaction.
Temperature
38
Small changes in ___ (less than one unit) can result in enzyme denaturation and subsequent loss of catalytic activity
pH
38
Enzyme activity increases up to a certain substrate concentration and thereafter remains constant
Substrate concentration
39
Are those which proceed at a rate exactly proportional to the concentration of one reactant
First-order reaction
39
Are those in which the rate is proportional to the product of the concentration of two reactants
Second-order reaction
40
The reactions are zero-order with respect to the reactants
Zero-order reaction
41
If the amount of substrate present is kept constant and the enzyme concentration is increased, the reaction rate increases because more substrate molecules can be accommodated in a given amount of time.
Enzyme concentration
42
Nonprotein entities that must bind to particular enzymes before a reaction occurs
Cofactor
43
Proper substrate binding
Activator
44
Interfere with enzyme reactions
Inhibitor
45
a substance that slows or stops the normal catalytic function of an enzyme by binding to it
Enzyme Inhibitor
46
A molecule closely resembling the substrate.
Competitive inhibitor
47
A molecule that binds to a site on an enzyme that is not the active site.
Noncompetitive inhibitor
48
A molecule that forms a covalent bond to a part of the active site, permanently preventing substrates from occupying it
Irreversible inhibition
49
Substances other than substrate or coenzyme are necessary and must be present in excess
Coupled-Enzymatic Assays
50
Reactants are combined
Fixed-Time (Endpoint) Assays
51
Multiple measurements
Continuous-monitoring (Kinetic) Assays
52
Amount of enzyme that will catalyze the reaction of 1 micromole of substrate per minute under specified conditions
International Unit (IU)
53
Enzyme concentration
International Unit per Liter (IU/L)
54
Amount of enzyme that will catalyze the reaction of 1 mole of substrate per second under specified condition
Katal Unit (mole/s)