enzymes Flashcards

1
Q

oxidoreductases

A

REDOX rxns that involve the transfer of electrons

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2
Q

transferases move a

A

function group from one molecule to another

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3
Q

hydrolases catalyze

A

cleavage w/ the addition of water

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4
Q

lyases catalyze cleavage without

A

the addition of water and transfer of electrons

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5
Q

isomerases catalyze the interconversion of

A

isomers

including constitutional isomers + stereoisomers

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6
Q

ligases join two large

A

biomolecules often of the same type

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7
Q

lipases catalyze the

A

hydrolysis of fats

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8
Q

dietary fats are broken down into

A

fatty acids and glycerol/other alcohols

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9
Q

kinases add a

A

phosphate group

type of transferase

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10
Q

phosphatases remove a

A

phosphate group

type of transferase

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11
Q

phosphorylases introduce a

A

phosphate group into an organic molecule (notably glucose)

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12
Q

exergonic rxn

A

RELEASE energy

gibbs free E = negative

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13
Q

endergonic rxns

A

require energy

gibbs free E = positive

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14
Q

enzymes do not alter the

A

gibbs free E or enthalpy or the final equilibrium position

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15
Q

enzymes only alter the

A

changing the rate of the reaction

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16
Q

as substrate increases, so does the

A

rxn rate until a max value is reached

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17
Q

K is the [S] at which an enzyme…

A

runs at half its Vmax

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18
Q

Vmax is the max rate at which an enzymes can….

A

catalyze a rxn

all enzyme active sites are saturated w/ substrate

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19
Q

cooperative enzymes display what kind of curve

A

sigmoidal curve b/c of activity change with substrate binding

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20
Q

enzymes stabilize the

A

transition state

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21
Q

enzymes provide a favorable microenvironment and/or…

A

bonding w/ the substrate molecules

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22
Q

site of catalysis is called

A

the active site

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23
Q

lock and key theory

A

enzyme and substrate are complementary and fit together like a key into a lock

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24
Q

induced fit theory is where the enzyme and substrate…

A

undergo conformational changes to interact fully

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25
metal cation that is required by some enzymes
cofactor
26
what molecule is required by some enzymes
organic molecules
27
how does temp and pH affect enzymes
denaturation and loss of activity due to loss of 2/3/4 structure of proteins
28
salinity can impact the actions of
enzymes
29
feedback inhibition is when an enzyme is inhibited by
high levels of a product from later in the same pathway
30
reversible inhibition is the ability to replace the inhibitor with a....
compound of greater affinity or to remove i.t. using mild lab treatment
31
competitve inhibition
when inhibitior is similar to the substrate binds at the active site blocks substrate from binding
32
competitive inhibition can be overcome by
adding more substrate
33
vmax and km in competitive inhibtion
vmax unchanged km increases
34
uncompetitive inhibition is when the inhibitors binds...
only w/ the ES complex
35
vmax and km in uncompetitive inhibtion
vmax and km decrease
36
noncompetitive inhibition is when the inhibitors binds with...
equal affinity to the enzyme and ES complex
37
vmax and km for noncompetitive inhibition
vmax decreases and km unchanged
38
mixed inhibition is when the inhibitor binds with unequal...
affinity to the enzyme and ES complex
39
vmax and km in mixed inhibition
vmax decreases km increases/decreases depending on if the inhibitor has a higher affinity for the enzyme or ES complex
40
irreversible inhibition alters the enzyme in such a way that the
active site is unavailable for a prolonged duration / permanently
41
suicide inhibitor is a substrate analogue that binds...
IRREVERSIBLY to the active site via a covalent bond
42
allosteric effector binds at the allosteric site and induces a...
change in the conformation of the enzyme the substrate can no longer bind to the active site
43
allosteric effector displays
cooperativity does not obey MM-kinetics
44
positive allosteric effectors exert a
positive effect increase activity
45
negative allosteric effector exert a
negative effect decrease activity
46
homotropic effector is an allosteric regulator that is also the...
substrate e.g. O2 is a homotropic allosteric regulator of hemoglobin
47
heterotropic effector is an allosteric regulator molecule that is
different from the substrate
48
what is phosphorylation
covalent modification with phosphate
49
catabolism
phosphorylated = active
50
anabolism
phosphorylated = inactive
51
glycolsylation is the covalent modification with
carbohydrates
52
zymogens is the
precursor to an enzyme
53
zymogens are secreted in an inactive form and are...
activated by cleavage
54
which proteins made up the cytoskeleton/anchoring proteins/EC matrix
structural proteins
55
common structural proteins
collagen elastin keratin actin tubulin
56
motor proteins have 1+ heads capable of
force generation through a conformation change
57
motor proteins have catalyic activity, acting as
ATPases to power movement
58
common applications w/ motor proteins
muscle contraction vesicle mvmt within cells cell motility e.g. myosin, kinesin, dynein
59
binding proteins bind a
specific substrate either to sequester it in body or hold concentration at steady state
60
what does cell adhesion molecules allows cells to do
allows cells to bind to other cells/surfaces
61
cadherins are
calcium-dependent glycoproteins holding similar cells together
62
intergrins have two membrane-spanning chains and allow cells to...
adhere to proteins in EC matrix
63
selectins allows cells to adhere to
carbs on surfaces of other cells commonly used in immune system
64
antibodies are aka
immunoglobulins (Ig) used by immune system to target a specific antigen
65
ion channels can be used for
regulating ion flow in/out of cell
66
ungated channels are
ALWAYS OPEN
67
voltage-gated channels are
OPEN within a range of membrane potentials
68
ligand-gated channels open in the
presence of specific binding substance (usually a hormone or neurotransmitter)
69
enzyme-linked receptors participate in cell signalling through
EC ligand binding and initiation of 2nd messenger cascades
70
GCPR has a membrane-bound protein called the
G-protein (has three subunits)
71
1st messenger ligand initiates the
2nd messenger and the cascade response
72
epinephrine is a ligand
2st messenger
73
at the end of the GCPR process,
phosphodiesterase deactivated cAMP GTP hydrolyzed back to GDP
74
electrophoresis uses a
gel matrix to observe migration of proteins in response to an electric field
75
native PAGE maintains the protein's shape but results are
difficult to compare b/c mass/charge ratio differs by protein
76
SDS-PAGE denatures proteins and masks the
native charge so size comparison is more accurate func protein cannot be recaptured from gel
77
isoelectric focusing separates proteins by the
pI protein migrates towards electrode until i.t. reaches region where pH = pI of protein
78
chromatography separates protein mixtures on the basis of
their affinity for a stationary phase or mobile phase
79
column chromatography uses beads of a
polar compound (stationary phase) with a non-polar solvent (mobile phase)
80
ion-exchange chromotography uses a
charged column and a variably salin eluent
81
size exclusion chromotography relies on
poroous beads larger molecules elute first - not trapped in small pores
82
affinity chromotography uses a bound receptor or ligand and an eluding with a….
free ligand or receptor for the protein of interest
83
how is protein structure primarily determined
XRAY crystallography after protein isolated then NMR can be used
84
edmand degradation determines
AA sequence
85
bradford protein assay is most
common uses color change from brown-green to blue
86
what does topoisomerase do
unwind the DNA double helix
87
helicase function
breaks H-bonds b/w the nitrogenous bases in order to separate DNA strands
88
single strand binding protein (SSB) binds to
single-stranded DNA and prevents annealing of ssDNA into double-stranded DNA
89
what does DNA primase do
catalyzes synthesis of RNA primer
90
RNA primers allows for
DNA replication to start short RNA nucleotide sequences that are complementary to the ssDNA
91
DNA polymerase adds
nucleotides to the growing strand
92
how to read DNA template
3' to 5'
93
how is the new strand of DNA synthesized
5' to 3'
94
DNA polymerase removes the
RNA primer at the end of the strand
95
okazaki fragments are short, newly synthesized DNA fragments formed
on the lagging template strand during DNA replication
96
DNA ligase join the
DNA strands together by catalyzing formation of phosphodiester bonds
97
proofreading DNA/RNA
DNA has proofreading, RNA does NOT
98
DNA replication is more (what) than RNA replication
accurate
99
stability of DNA/RNA
RNA is less stable b/c it contains sugar ribose instead of DNA's deoxyribose
100
because RNA is less stable, it...
degrades rapidly in cytoplasm
101
strands of DNA wrap around a
histone protein forming nucleosomes
102
nucleosomes coil together and form
chromatin
103
chromatin loops and coils together to form
supercoils
104
supercoils bunch together to form
chromosomes
105
charge of DNA
negative due to phosphate backbone
106
3 parts of a nucleotide
5 carbon sugar nitrogen-rich base phosphate group
107
nucleoside lacks
phosphate group
108
nucleotide pairs
adenine - thymine guanine - cytosine
109
adenine-thymind has how many H-bonds
2 H-bonds
110
guanine-cytosine has how many H bonds
3 H bonds stronger than A-T
111
what holds DNA backbone together
phosphodiester bonds between sugar and phosphate groups
112
hydrogen bonds hold what together in DNA
nucleotide bases together inside the double helix
113
how many rings in pyrimidine
1 ring
114
how many rings in purines
2 rings pyrimidine ring fused to an imidazole ring
115
pyrimidines
cytosine thymine uracil (RNA only)
116
purines
adenine guanine
117
purines and pyrimidines have a 1:1 ratio as per
Chargaff's rule
118
purine and pyrimidine have what kind of width
UNIFORM
119
purine + purine is too
wide
120
pyrimidine + pyrimidine is too
narrow
121
diameter of DNA double helix =
20 angstroms
122
RNA is a polymer of
nucleotides
123
how does RNA differ from DNA
1) RNA is single stranded 2) sugar is ribose + more reactive 3) nitrogenous base is uracil (U) not thymine (T)
124