UNIT 2 Flashcards
(103 cards)
1
Q
- biologic proteins
- biocatalysts
- body tissues
- minute concentration
A
enzymes
2
Q
All enzymes are proteins, but not all proteins are enzymes.
A
TRUE
3
Q
number, type, and sequence of amino
acids in the polypeptide chain. In order to function properly,
proteins must have the correct sequence of amino acids
Linear structure
A
PRIMARY
4
Q
commonly formed arrangements
stabilized by hydrogen bonds between nearby amino acids
within the protein molecule
Bends, turns and folds in the structure
A
SECONDARY STRUCTURE
5
Q
overall shape of the protein molecule.
The conformation is known as the fold, or the spatial relationship of the secondary structure to one another.
Has 3D conformation
A
tertiary structure
6
Q
results from the interaction of more
than one protein molecule, or protein subunits, referred to as
multimer, that functions as a single unit.
A
quarternary structure
7
Q
substance acted upon by the
enzyme.
It binds to the active site of the enzyme
A
substrate
8
Q
A water free cavity, where the substrate
interacts with particular charged amino acid
residues
A
active site
9
Q
A cavity other than the active site; binds the
regulator molecules.
A
allosteric site
10
Q
These are enzymes with same function but
exist in different forms.
A
isoenzymes
11
Q
These are forms of enzymes that were
post-transcriptionally modified.
The function is different
A
isoforms
12
Q
These are non-CHON molecule necessary
for enzyme activity such as activators and
coenzymes.
A
cofactors
13
Q
inorganic cofactors
that can either be metallic or
nonmetallic
A
ACTIVATORS
14
Q
are organic cofactors
A
coenzyme
15
Q
calcium, magnesium,
manganese, zinc, cobalt, etc
A
metallic
16
Q
chloride, bromide,
etc
A
nonmetallic
17
Q
Vitamins, niacin, biotin, and NAD
A
coenzymes
18
Q
is what we use to quantify
the enzyme because it becomes
NADH
A
NAD
19
Q
Alteration of the cofactor is measured,
instead of the concentration of the enzyme
because enzymes are present in minute
concentrations
A
TRUE
20
Q
The different forms may differ in select
physical properties,
A
- diffrent AA composition
- electrophoresis pattern
- solubility and resistance
21
Q
Because the amino acid composition is different
from one isoenzyme to another, they have different
charges that allow for separation in
electrophoresis because of the different mobility
that each isoenzyme possesses.
A
electrophoretic pattern
22
Q
Some isoenzymes are soluble in either acid or basic
solution
A
solubility and resistance
23
Q
present in the heart, and it increases if there is
acute myocardial infarction
A
CK-MB
24
Q
most abundant because it is present in all of
the muscle
A
CK-MM
25
most anodic isoenzyme of CK due to its
charge.
CK-BB
26
This is a coenzyme bound tightly to the
enzyme
prosthetic group
27
The enzyme portion that is activated by the
prosthetic group
Site where co-enzyme binds.
apoenzyme
28
Prosthetic group + Apoenzyme
holoenzyme
29
Inactive precursor of an enzyme
Inactive to prevent itself from reacting with a
substrate and will only activate once needed.
zymogen/proemzyme
30
Enumerate the major classification of enzymes based on the
standardized enzyme nomenclature
OTHLIL
1. oxidoreductase
2. transferase
3. hydrolase
4. lyase
5. isometase
6. ligase
31
Catalyze an oxidation-reduction reaction between
two substrates.
oxidoreductase
32
Dehydrogenases (Ex: LDH, GLDH, G6PD)
oxidoreductase
33
Catalyze the transfer of a group other than
hydrogen from one substrate to another.
transferases
34
Kinases (Ex: Creatine Kinase)
●GGT, AST, ALT
transferases
35
Catalyze hydrolysis of various chemical bonds.
●Water enters the chemical bonds
hydrolases
36
Catalyze removal of groups from substrates without
hydrolysis; the product contains double bonds.
lyases
37
Catalyze the interconversion of geometric optical,
or positional isomers.
●configuration or modification happens
isomerases
38
Catalyze the joining of two substrate molecules,
coupled with breaking of the pyrophosphate bond in ATP or a similar compound
ligases
39
intermediate state where both substrate and
enzyme exists and reacted but has not
formed a product yet
transition state
40
energy you can give to the reaction
free energy
41
As you go to the ______, you reach equilibrium (where
no energy is consumed)
right
42
______ shows a reaction without an enzyme and a
______ activation energy
red line; high
43
Products are not formed unless the _______ is reached
transition
state
44
shows a reaction with an enzyme and a
lower activation energy
orange line
45
Enzyme _______ the activation energy, hence
faster reaction and reach equilibrium
lowers = faster
46
proposes that enzymes have a specific, rigid active site that precisely fits a corresponding substrate, much like a key fitting into a lock. This model suggests that the enzyme and substrate interact through complementary shapes, allowing for a highly
selective and efficient biochemical reaction.
emil fischer
lock and key
47
proposed by ______, suggests that the enzyme's active site is flexible and
undergoes conformational changes upon substrate binding, enhancing the fit between the enzyme and substrate. This dynamic adaptation allows for a more precise interaction, facilitating the catalytic process
Enzyme adjusts itself for the substrate to produce a product
DANIEL KOSHLAND
INDUCED FIT THEORY
48
refers to the ability of an enzyme to
selectively bind to a particular substrate, facilitating a specific biochemical reaction.
enzyme specificity
49
This selectivity is determined
by the enzyme's active site, which has a unique shape and chemical environment that only accommodates certain molecules.
TRUE
50
Enzyme only combines to one specific
substrate and only catalyze the
corresponding reaction
absolute specificity
51
Enzyme combines to substrate belonging to
a certain group (Ex: ester group)
group specificity
52
Enzyme combines to substrate belonging to
a certain group (Ex: ester group)
group specificity
53
Requires a specific number of bonds (ex:
double bonds)
bond specificity
54
specific to one isomer of the enzyme
stereoisomeric specificity
55
factors affecting enzyme activity
1. substrate concentrations
2. enzyme concentration
3. pH
4. temperature
5. cofactors
6. inhibitors
56
Increase in substrate concentration =
increased rate of reaction
SUBSTRATE CONCENTRATION
INCREASE= INCREASE
57
reaction of the burger
machine (enzyme) is dependent on
the number of customers
(substrate)
TRUE
58
Increase in substrate = increase in
enzyme activity = increase in
products
TRUE
59
Determines the number of available active
sites, directly affecting the reaction rate.
● if there is no enzyme, substrates can’t bind
enzyme concentration
60
Affects enzyme shape and function;
deviations from the optimal pH can reduce
activity.
pH
61
Optimal pH:
7.0-8.0
62
Increases enzyme activity by promoting
molecular collisions, but extreme
temperatures can denature the enzyme.
temp
63
An increase of 10 degrees celsius
will double the reaction
TRUE
64
repeated freezing and thawing will
denature the enzyme
TRUE
65
Aid in enzyme catalysis by helping to
stabilize the enzyme substrate complex or
participate in the reaction.
cofactors
66
Decrease enzyme activity by blocking the
active site or altering the enzyme structure.
INHIBITOR
DECREASED
67
During a reaction, the substrate readily binds to free enzyme at a low substrate concentration. The reaction rate steadily increases when more substrate is added as substrate
increasingly associates with enzyme.
substrate conc
reaction rate increases = when more substrate is added
68
dependent on the substrate
first order
69
dependent on the enzyme
zero order kinetics
70
hypothesized the
role of substrate concentration in formation of the
enzyme–substrate (ES) complex.
michaelis- menten
71
As the amount of substrate ______, more active sites of
the enzymes are bonded.
increases = more
72
At some point, all of the enzymes are saturated with
its substrate, leading to a ______ because the amount of enzymes does not change even though there is an increase in substrate concentration.
parabolic curve
73
theoretical value in which it is the maximum rate
of reaction and is a characteristic feature of a specific
enzyme at a specific concentration of substrate
vmax
74
value in which the reaction reached half of
the maximum velocity
vmax/2
75
amount of substrate needed to
achieve Vmax/2
km or michaelis constant
76
With this, Km is ______ proportional to substrate
affinity
INVERSELY
77
If the substrate affinity is _____, it would only need
small amount of substrate to reach Vmax/2, therefore low Km
high affinity; small; low km
78
If the substrate affinity is _____, it would need
high amount of substrate to reach Vmax/2, therefore high Km.
low; high amount; high km
79
This graph shows that as substrate concentration increases,
the reaction rate also increases. This process follows
first order- SUBSTRATE
80
If substrate concentration is high enough to saturate all
enzymes, it now follow _____-order kinetics because it depends on enzyme concentration.
zero - ENZYME
81
substrate concentration at which the reaction velocity is half of the maximum level
km
82
manipulated the equation of
Michaelis-Menten curve into linear to accurately and
conveniently determine Vmax and Km
double reciprocal, it's a reverse of Michaelis constant
lineweaver-burk
83
compound that shares some structural features found in the substrate will typically physically bind to the same form of the enzyme that the substrate binds, often in the active site of an enzyme, and compete with the substrate for a place in the active site.
competitive inhibitor
84
sensitive to the presence of other
compounds that are called
Most
commonly, these inhibitors associate with enzymes at a place other than the active site showing allosteric inhibition.
binds to the allosteric site and change the enzyme
non competitive
85
A third pattern of inhibition, may be
observed in which the inhibitor binds only to the ES
complex; increasing substrate concentration results in more ES complexes to which the inhibitor binds and, thereby, increases the inhibition.
○ kumakapit na agad
○Only binds to E-S complexes
UNCOMPETITIVE
86
more substrate para di makapasok si competitive
inhibitor
dahil may remedy we achieve vmax
increased substrate para masolusyunan si
competitive inhibitor
competitive
87
Since it binds to the allosteric site, even if you
increase the concentration of the substrate, it won’t
bind to the enzyme, which results in not reaching the
Vmax, but same Km
non competitive
88
when the enzyme complex substrate is inhibited wala magiging product bumaba yung vmax
so km also decreases it will move to the left
Since in uncompetitive inhibition, the inhibitors
attaches to the ES complex, kahit anong dagdag natin ng substrate, magbibind lang yung iaadd na substrate
uncompetitive
89
same vmax, increased km
competitive
90
vmax not achived, same km
non competitive
91
vmax not achieved, decreased km
uncompetitive
92
○ amount of enzyme that will catalyze the reaction of one u/mol per minute
IU
93
oxireductases
lactate dehydrogenase
glucose-6-phosphate dehydrogenase
glutamate dehydrogenase
94
hydrolase
1. alkaline phosphatase
2. acid phosphatase
3. a-amylase
4. cholinesterase
5. chymotrypsin
6. elastase-1
7. 5’ nucleotidase
8. triacylglycerol lipase
9. trypsin
95
lyases
aldolase
96
isomerases
triosephosphate isomerase
97
ligase
glutatione synthetase
98
PDT FORMATION
increase
99
substrate conc
decrease
100
coenzyme conc
decrease
101
altered coenzyme
increase
102
single measurement at a specific time
fixed time/ endpoint
103
continuous monitoring assay
kinetic
