2 Enzymes Flashcards

1
Q

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

A

30

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2
Q

If we exclude inert materials, such as the cell wall and starch, which can account for up to _% of the dry weight of some cells, proteins and amino acids represent about _to _% of the dry weight of the living cell

A

90

60- 70

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3
Q
  • 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

Enzymes have been called the “_”

A

agents of life

since they control
almost all life processes

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5
Q

Enzymes AKA

A

biological catalysts

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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)— _

A

the enzyme–substrate complex

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7
Q

enzymes will convert about a _ molecules of substrate to product in 1 s

A

thousand

some will convert as many as a million

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8
Q

enzymes do not change the position of the chemical equilibrium but rather _ the reaction rate

A

increase

large protein molecules that increases the rates of chemical reaction without
themselves undergoing change by 10^9
to 10^20 times

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9
Q

Enzyme as catalyst are extremely specific, that is, each of them
speeding up only _ particular reaction or class of reactions

A

one

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10
Q

protein-degrading enzyme of the stomach and its optimum pH

A

pepsin

a pH optimum around 2.0

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11
Q
  • – from hyperthermophilic (“extreme heat-loving”) archaebacterium Pyrococcus furiosus*;
  • oxidizes H2 at a temperature optimum greater than 95^0C;
  • the presence of this enzyme in Pyrococcus enables them to grow optimally at 100^0C
A

hydrogenase

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12
Q

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

A

International Union of Biochemistry

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13
Q

reactants of enzyme catalyzed reactions are called as _ and each
enzyme is quite specific in character

A

substrate

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14
Q

enzymes are made of proteins with occasional non-protein part

many enzymes need only proteins in their structure for their activity while others require one or more non-protein components called _

A

cofactors

  • nonprotein component of enzymes ;without it, enzymes will lack their catalytic activity
  • some cofactors can either be organic or metallic in nature
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15
Q

protein or polypeptide portion of the enzyme is called _

A

apoenzyme

some apoenzyme cannot catalyze a reaction without its cofactor nor can the cofactor function without an apoenzyme

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16
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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17
Q

example of these coenzymes are the electron carriers

A
  • nicotinamide adenine dinucleotide (NAD+) reduced to NADH
  • flavin adenine dinucleotide (FAD) reduced to FADH2

both are reduced in a dehydrogenation reaction

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18
Q

metal ion cofactors such as _ are sometimes referred to as metal
activators

A

Fe, Mo, Cu, and Zn

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19
Q

their non-protein co-factors that are more or less permanently associated with the enzyme protein are called _

A

prosthetic groups

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20
Q

Enzyme catalysis

A

E + S -> E-S -> E + P

enzyme+substrate ->enzyme-substrate complex -> enzyme + product

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21
Q

the compound on which the enzyme works and whose reaction is being speed up is
called the _

A

substrate

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22
Q

the substrate usually binds to the enzyme surface while it undergoes the reaction on a
specific portion called the _

A

active site

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23
Q

_ can also be found on active sites

A

coenzymes

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24
Q

enzymes are able to catalyze or speed up particular reactions because they _ the
amount of activation energy required to initiate the reaction

A

lower

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25
catalysis occurs at the active site which is composed of the_ and the _
binding site catalytic group
26
active site of an enzyme contains specific _ that form temporary bonds with the substrate
amino acid residues
27
active site of the enzyme occupies _ % of the total volume of the enzyme
~10 – 20
28
_ is the most important part of the enzyme that catalyzes the chemical reaction
active site
29
the active site of the enzyme contains only _ amino acids
three to four
30
* 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
31
the binding site attracts and positions the _ while the catalytic group (the reactive side chains of amino acids or cofactors) carry out the _ reactions involved
substrate bond-breaking and bond-forming
32
- location in active site where the catalysis of the chemical reaction occurs in the enzyme
catalytic site
33
, the _ in the catalytic site of the enzyme are responsible for catalyzing the chemical reaction
amino acids
34
catalytic site _ the activation energy of the chemical reaction
reduces
35
catalytic site is one of the two main components of the _ of an enzyme
active site
36
the main function of an enzyme is to _ under physiological conditions
catalyze a chemical reaction
37
refers to a location on a macromolecule or cellular structure at which **chemical interaction with a specific active substance** takes place
Binding Site
38
temporarily binds with the substrate
Binding Site
39
binds and orients the substrate
Binding Site
40
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
41
in enzyme which catalyzes the reaction of the substrate
Catalytic Site
42
reduces the chemical activation energy
Catalytic Site
43
six major groups of enzymes based on type of reaction they catalyze
1. oxidoreductases 2. transferases 3. hydrolases 4. lyases 5. isomerases 6. ligases/ synthetases
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 reactions
Isomerases
49
catalyze the joining of two molecules
Ligases/ Synthetases –
50
When the type of reaction is omitted, it is _. like?
hydrolysis urease, lactase
51
* explains the specificity of enzyme action by comparing the active site of an enzyme to a lock and the substrate to a key, * assumes that the **enzyme is a rigid, three-dimensional body**
Lock-and-Key Model
52
* 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
53
reaction rates depend on the number of successful _ between substrate and enzyme molecules, which in turn depends upon their concentrations
collisions
54
if we keep the **concentration of the substrate constant**, an **increase in enzyme concentration** would linearly _ the rate of enzyme activity
increase
55
if we keep the concentration of the **enzyme constant** and **increase the concentration of the substrate**, there is a different scenario since rate _ continuously
does not increase
56
a point where the rate stays the same even with increase substrate concentration called as the _
saturation point
57
at saturation point, substrate molecules are bound to _ available active sites of an enzyme
all
58
* increasing substrate concentration _ the frequency with which the enzyme and substrate collide * as a result, enzyme-substrate complexes form _ and the rate of reaction _
increases more quickly increases
59
however, there is a limit as eventually there all the enzyme active sites are already occupied with substrate - the enzyme active sites become _
saturated ## Footnote * any further increase in substrate concentration has no further effect on the reaction rate * *Note that if there is excess substrate (the first part of the graph) the line can be approximated to a straight lin
60
temperature affects enzyme activity because of _ of the three-dimensional structure of the enzyme
denaturation or the alteration ## Footnote * hence, the substrate may not be able to successfully fit the active sites * each enzyme has its own optimum temperature to work with
61
pH influences the _ of substrates, _ state, and presence of charged and uncharged free amino or carboxyl groups in the enzyme
* ionization * denaturation
62
* a **neutral** carboxyl group requires a _ pH optimum * while an **uncharged amino group** needs a _ pH optimum
low high
63
_ any process that makes an active enzyme less active or inactive which is accomplished by compounds known as _
inhibition inhibitors
64
Two types of Inhibitors
1. Competitive Inhibitors 2. Non-competitive Inhibitors
65
bind to the active site of an enzyme surface, thereby, preventing the real substrate to bind
Competitive Inhibitors
66
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
67
Both competitive and noncompetitive inhibitors are _ , but some compounds alter the structure of the enzyme permanently and thus, make it irreversibly inactive
reversible