Chapter 2 Flashcards

(66 cards)

1
Q

Proteins constitute about __% of the total dry weight of typical plant cells.

A

30

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2
Q

proteins and amino acids represent about __ to __% of the dry weight of the living cell excluding inert materials.

A

60 to 70

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3
Q

the major function of proteins in metabolism is to serve as ___, biological catalysts that
greatly increase the rates of biochemical reactions

A

enzymes

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4
Q

The most important features of enzymes are their ____,
which permits them to distinguish among very similar molecules, and their ___, which is far greater than that of ordinary catalysts.

A

specificity;
catalytic efficiency

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5
Q

“agents of life”
▪ “biological catalysts

A

enzymes

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6
Q

first step in enzyme catalysis is the formation of a tightly bound, noncovalent complex
between the enzyme and the substrate(s)— the ___

A

enzyme–substrate complex

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7
Q

enzymes do not change the position of the ___ but rather increase the ___

A

chemical equilibrium;
reaction rate

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8
Q

Two remarkable aspects of enzymes as catalysts:

A

-extremely effective (10^9
to 10^20 times increased reaction rate)
-extremely specific

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9
Q

enzymes function at ambient ___and ____ and usually in a
___pH range near ___

A

temperature and atmospheric pressure;
narrow ;neutrality

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10
Q

___– protein-degrading enzyme of the stomach (has a pH optimum
around ___)

A

pepsin; 2.0

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11
Q

____– from hyperthermophilic (“extreme heat-loving”)
archaebacterium Pyrococcus furiosus; oxidizes H2 at a temperature
optimum greater than 95 degree C; the presence of this enzyme in Pyrococcus
enables them to grow optimally at 100 degree C.

A

hydrogenase

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12
Q

hydrogenase is from the hyperthermophilic (“extreme heat-loving”)
archaebacterium ______; oxidizes __ at a temperature
optimum greater than ___degree C; the presence of this enzyme in Pyrococcus
enables them to grow optimally at __ degree C.

A

Pyrococcus furiosus;
H2;
95;
100

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13
Q

enzymes are usually named after their substrates by the addition of the suffix __

A

“-ase

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14
Q

each enzyme has been named in a systematic fashion, on the basis of the
reaction it catalyzes, by the ___

A

International Union of Biochemistry

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15
Q

reactants of enzyme catalyzed reactions are called as ____

A

substrate

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16
Q

non-protein component of enzymes

A

cofactors

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17
Q

the protein or polypeptide portion of the enzyme is called ____

A

apoenzyme

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18
Q

protein portion, inactive=
nonprotein portion, activator=
whole enzyme, active=

A

apoenzyme
cofactor
holoenzymes

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19
Q

some cofactors can either be __ or ___ in nature

A

organic or metallic

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20
Q

organic cofactors are called as ___which are transiently associated with the
apoenzyme and are themselves changed in the reaction

A

coenzymes

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21
Q

example of coenzymes (electron carriers): 2

A

nicotinamide adenine
dinucleotide (NAD+);
flavin adenine dinucleotide (FAD)

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22
Q

nicotinamide adenine
dinucleotide (NAD+) and flavin adenine dinucleotide (FAD) which are
reduced to NADH and FADH2 in a reaction called ___

A

dehydrogenation

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23
Q

metal ion cofactors are sometimes referred to as ___

A

metal activators

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24
Q

example of metal ion cofactors (4)

A

Fe, Mo, Cu, Zn

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25
non-protein co-factors that are more or less permanently associated with the enzyme protein are called ___
prosthetic groups
26
the compound on which the enzyme works and whose reaction is being speed up is called the ___
substrate
27
the substrate usually binds to the enzyme surface while it undergoes the reaction on a specific portion called the ___
active site
28
can also be found on active sites
coenzymes
29
enzymes are able to catalyze or speed up particular reactions because they lower the amount of ___ required to initiate the reaction
activation energy
30
catalysis occurs at the ___ which is composed of the ___ and the ___
active site; binding site and catalytic group
31
is the site of the enzyme where the substrate molecules bind and undergo the chemical reaction
active site
32
contains specific amino acid residues that form temporary bonds with the substrate
active site
33
active site of the enzyme occupies ~___% of the total volume of the enzyme
10 – 20
34
is the most important part of the enzyme that catalyzes the chemical reaction
active site
35
active site of the enzyme contains only ___ amino acids
three to four
36
- location of substrates binding with the enzyme; one of the two components of the active site of the enzyme; bind and orient substrate molecules
binding site
37
the ____ attracts and positions the substrate while the ___ carry out the bond-breaking and bond-forming reactions involved
binding site; catalytic group
38
- location where the catalysis of the chemical reaction occurs in the enzyme
catalytic site
39
__in the catalytic site of the enzyme are responsible for catalyzing the chemical reaction
amino acids
40
reduces the activation energy of the chemical reaction
catalytic site
41
refers to a location on a macromolecule or cellular structure at which chemical interaction with a specific active substance takes place
binding site
42
refers to a portion of an enzyme molecule at which the actual reaction proceeds and is considered to consist of one or more residues or atoms in a spatial arrangement
catalytic site
43
6 major groups/classification of enzymes
Oxidoreductases; Transferases Lyases Hydrolases Ligases/Synthetases Isomerases
44
– catalyze oxidation and reduction
Oxidoreductases
45
– catalyze the transfer of a group of atoms from one molecule to another
Transferases
46
– catalyze hydrolysis reactions
Hydrolases
47
– catalyze the addition of a group to a double bond or removal of two groups from adjacent atoms to create a double bond.
Lyases
48
– catalyze isomerization reaction
Isomerases
49
– catalyze the joining of two molecules
Ligases/ Synthetases
50
e type of reaction catalyzed is often noted with a ___.
prefix
51
two model proposed that showed how specific enzymes are
Lock-and-Key Model and the Induced-Fit Model
52
explains the specificity of enzyme action by comparing the active site of an enzyme to a lock and the substrate to a key, however, this model assumes that the enzyme is a rigid, three-dimensional body
Lock-and-Key Model
53
compares the active site to a glove and the substrate to a hand, that is, like a glove to a hand that accommodates the shape of the substrate
Induced-Fit Model
54
Factors Affecting Enzyme Activity (3)
Enzyme and Substrate Concentrations; Temperature; pH
55
there is a point where the rate stays the same even with increase substrate concentration called as the ___
saturation point
56
at ___, substrate molecules are bound to all available active sites of an enzyme
saturation point
57
what will happen? increasing substrate concentration... (3)
increases frequency of enzyme and substrate collision; enzyme-substrate complexes form more quickly; rate of reaction increases
58
there is a limit as eventually there all the enzyme active sites are already occupied with substrate - the enzyme active sites become ___
saturated
59
____affects enzyme activity because of denaturation or the alteration of the three-dimensional structure of the enzyme
temperature
60
____influences the ionization of substrates, denaturation state, and presence of charged and uncharged free amino or carboxyl groups in the enzyme
pH
61
a _____ requires a low pH optimum while an ___ needs a high pH optimum
neutral carboxyl group; uncharged amino group
62
____is any process that makes an active enzyme less active or inactive which is accomplished by compounds known as ___
Inhibition ; inhibitors
63
Two types of Inhibitors:
competitive; non-competitive
64
– bind to the active site of an enzyme surface, thereby, preventing the real substrate to bind
Competitive Inhibitors
65
– binds to some portion of the enzyme surface which may sufficiently alters the tertiary structure of the enzyme so that its catalytic effectiveness is slowed down
Non-competitive Inhibitors
66
Both competitive and noncompetitive inhibitors are ____, but some compounds alter the structure of the enzyme ___and thus, make it ___
reversible; permanently ; irreversibly inactive