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BIOCHEMISTRY > L4 - Enzymes > Flashcards

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
Q

transfer of phosphate
group from ATP to ADP +
phosphorylated product

A

Kinases

25
Q

catalyzes a hydrolysis reaction in which
the addition of a water molecule to a bond
causes the bond to break

A

Hydrolase

26
Q

breaking of glycosidic
bonds in oligosaccharides and
polysaccharides

A

Carbohydrases

27
Q

breaking of peptide linkages
in proteins

A

Proteases

28
Q

breaking of ester linkages in
triglycerides

A

Lipases

29
Q

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

Lyase

30
Q

removal of the
components of water from a double
bond

A

Dehydratase

31
Q

addition of water to a
double bond

A

Hydratase

32
Q

catalyzes the isomerization
(rearrangement of atoms) of a substrate in a
reaction, converting it into a molecule isomeric
with itself

A

Isomerase

33
Q

catalyzes the bonding together of two
molecules into one with the participation of ATP

A

Ligase

34
Q

a general explanation of the velocity
and gross mechanism of enzyme-catalyzed
reactions

A

Michaelis-Menten Theory

35
Q

highly specific way an enzyme
recognizes a substrate and binds it to the active
site

A

Lock and Key Theory

36
Q

the flexibility of the active site allows it
to adapt to the shape of the substrate

A

Induced-fit Model

37
Q

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

A

Enzyme Activity

37
Q

As the ___ of an enzymatically
catalyzed reaction increases, so does the rate
(velocity) of the reaction.

A

Temperature

38
Q

Small changes in ___ (less than one unit)
can result in enzyme denaturation and
subsequent loss of catalytic activity

A

pH

38
Q

Enzyme activity increases up to a
certain substrate concentration and thereafter
remains constant

A

Substrate concentration

39
Q

Are those which proceed at a
rate exactly proportional to the
concentration of one reactant

A

First-order reaction

39
Q

Are those in which the rate is
proportional to the product of the
concentration of two reactants

A

Second-order reaction

40
Q

The reactions are zero-order
with respect to the reactants

A

Zero-order reaction

41
Q

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.

A

Enzyme concentration

42
Q

Nonprotein entities that must bind to
particular enzymes before a reaction occurs

A

Cofactor

43
Q

Proper substrate binding

A

Activator

44
Q

Interfere with enzyme reactions

A

Inhibitor

45
Q

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

A

Enzyme Inhibitor

46
Q

A molecule closely resembling the
substrate.

A

Competitive inhibitor

47
Q

A molecule that binds to a site on an
enzyme that is not the active site.

A

Noncompetitive inhibitor

48
Q

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

A

Irreversible inhibition

49
Q

Substances other than substrate or
coenzyme are necessary and must be present in
excess

A

Coupled-Enzymatic Assays

50
Q

Reactants are combined

A

Fixed-Time (Endpoint) Assays

51
Q

Multiple measurements

A

Continuous-monitoring (Kinetic) Assays

52
Q

Amount of enzyme that will catalyze the
reaction of 1 micromole of substrate per minute
under specified conditions

A

International Unit (IU)

53
Q

Enzyme concentration

A

International Unit per Liter (IU/L)

54
Q

Amount of enzyme that will catalyze the
reaction of 1 mole of substrate per second
under specified condition

A

Katal Unit (mole/s)

BIOCHEMISTRY (1 decks)

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