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Biochemistry Lab > Enzymes > Flashcards

Enzymes Flashcards

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1
Q

Biomolecules that function as catalysts

A

Enzymes

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2
Q

All enzymes are ___

with an exception to ____

A

proteins

Some RNAs can catalyse their own self-cleavage

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3
Q

Enzymes can increase the rate of a reaction by

A

10^20

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4
Q

rate of reactions

catalyzed:
uncatalyzed:

A

catalyzed: 10^20
uncatalyzed: 10^9

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5
Q

Lowers the activation energy

A

enzymes

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6
Q

a higher curve in the graph means

A

uncatalyzed because requires more activation energy

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7
Q

a lower curve in the graph means

A

catalyzed because there is a low activation energy required

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8
Q

For an enzyme to function optimally, you have to satisfy these conditions:

A

All the active sites of the enzyme is saturated with the substrate

Optimum pH

Optimum temperature

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9
Q

helps us approximate the original dynamics under the assumption that the concentration of the enzyme remains constant

A

Michaelis-Menten equation plot

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10
Q

As the enzyme gets consumed

A

the more steeper the curve is but at the same time the lesser concentration is needed

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11
Q

shows that the concentration of the substrate when the reaction velocity is equal to half of the maximum velocity of the reaction

A

Km

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12
Q

When enzyme gets consumed, the more steeper the curve is and

A

the faster the reaction

Higher binding affinity means lower Km and
lower substrate concentration is needed

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13
Q

Relationship of binding affinity and substrate concentration

A

inversely proportional

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14
Q

a measure of how well the substrate complexes with the given enzyme
binding affinity

A

Michaelis-menten equation

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15
Q

used for analyzing how enzymes kinematics change in the presence of either competitive or noncompetitive inhibitor

A

Lineweaver-Burk Plot

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16
Q

What are the classification of enzymes

A 
Oxidoreductase
Transferases
Hydrolases
Lyases
Isomerases
Ligases
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17
Q

Transfer of hydrogen and oxygen atoms or electrons from one substrate to another

A

Oxidoreductase

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18
Q

Transfer of electrons (hydride ions or H atoms and O atoms) from one substrate to another

A

Oxidoreductase

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19
Q

Examples of Oxidoreductase

A

Oxidases,
Reductases,
Dehydrogenases

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20
Q

important reaction in anaerobic glycolysis

A

Lactate dehydrogenase

Oxidoreductase

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21
Q

Catalyze transfer of a group from one substrate (donor) to another (acceptor)

A

Transferases

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22
Q

Transfer of specific group (a phosphate or methyl et.) from one substrate to another

A

Transferases

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23
Q

Examples of Transferases

A

Kinases (phosphate grp),

Transaminases (amino grp)

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24
Q

Enzyme that undergoes transferases of phosphate group

A

Kinases

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25
Enzyme that undergoes transferases of amino group
transaminases
26
Catalyzes hydrolysis (which is the addition of H2O) of C-C, C-O, C-N and bonds like phosphoanhydride
Hydrolases
27
Examples of Hydrolases
Estrases, Digestive enzymes (trypsin, chymotrypsin) Acetylcholinesterase ``` Proteases (peptide bonds), Phosphatases (Phosphoester bond), Glycosylases (glycosidic bond), Nucleases (phosphosugar bond), Esterases (ester bonds) ```
28
A cholinergic enzyme Found at post-synaptic neuromuscular junctions and muscles and nerves
Acetylcholinesterase
29
Catalyze addition (other than H2O) of groups to double bonds of removal of groups to form double bonds
Lyases
30
Nonhydrolytic removal of a group or addition of a group to a substrate
Lyases
31
Examples of Lyases
Decarboxylases (removal of CO2) Dehydratases (removal of H2O) Aldolases (cleavage of aldol)
32
Convert the substrate into an isomer
Isomerase
33
Transfer of groups within molecules to form isomers
Isomerase
34
change of the molecular form of the substrate
Isomerase
35
Examples of Isomerase
``` Racemases (D-L isomers) Epimerases (sugar epimers) Cis-trans-Isomerases Tantomerases (keto-enol groups) Mutases (functional/positional isomers) ```
36
Joining 2 molecules with the hydrolysis of ATP
Ligases
37
joining of two molecules by the formation of new bonds
Ligases
38
Examples of Ligases
Carboxylase Synthetase tRNA synthetase Citric acid synthetase
39
Assists movement of another molecule across a cell membrane
Translocases
40
Movement of ion or molecules across a membrane or their separation within a membrane
Translocases
41
Involved in fatty acid metabolism
Carnitine acylarnitine translocase (CACT)
42
Example of Translocases
Carnitine translocase Adenine nucleotide transclocase (ANT) Carnitine acylarnitine translocase (CACT)
43
Helps convert long chain fatty acids into energy
Carnitine acylarnitine translocase (CACT)
44
Used by the cells to produce fats and energy Without this, it will lead to low blood sugar (wont breakdown the fats) and ketone bodies within the first 48 hours for infants (?) and development of (?), seizures, sudden infant death.
Carnitine acylarnitine translocase (CACT)
45
EC NUMBER 1.2.3.4 1= 2= 3= 4=
``` 1= main class 2= specific functional groups 3= # cofactors ? 4= specific to substrates ```
46
reducing Sugars Assay Using
Dinitrosalicylic (DNS) Colorimetric Method
47
Chemical nature of enzymes
Majority are proteins some are RNA ~ ribozymes
48
Functions at milder reaction conditions
enzymes
49
Efficient in catalyzing high reaction rate than a chemical catalyst
enzymes
50
Some catalyze the reaction of only one stereoisomer; others catalyze a family of similar reactions
Greater reaction specificity
51
biological catalysts accelerate rate of biochemical reactions
enzymes
52
It accelerates the rate of a reaction by
reducing free energy activation. A factor of up to 1020 over an uncatalyzed reaction
53
TRUE OR FALSE Enzymes are not regenerated after the reaction
FALSE It is regenerated after the reaction.
54
TRUE OR FALSE Enzymes does not change the equilibrium of the reaction.
TRUE
55
biomolecule acted upon by the enzyme
Substrate
56
specific region of the enzyme that creates a 3D surface complementary to the substrate
Active site
57
pH at which an enzyme exhibits maximum activity (achieves Vmax)
Optimal pH
58
maximum reaction rate
Vmax
59
what will happen when there is a Slight change in pH
alters the charge of acidic and basic amino acid residues found in active site.
60
What will happen in Extreme pH (too acidic/basic)
denatures enzyme irreversibly; loss of catalytic activity.
61
temperature at which an enzyme exhibits maximum activity
Optimal temperature
62
at higher temperature, molecules are at their excited state =
more kinetic energy = faster reaction rate = more products
63
beyond optimum Temperature what is disrupted
disrupts tertiary structure of enzyme = substrate may not fit the active site = impedes catalytic reaction
64
TRUE OR FALSE alteration in enzyme conformation by change in temperature is reversible
FALSE alteration in enzyme conformation by change in temperature may be reversible or irreversible (point of no return)
65
yeast-derived enzyme
invertase
66
IUPAC name of invertase and EC number
β-fructofuranosidase (EC 3.2.1.26)
67
β-fructofuranosidase is considered a what type of enzyme
Hydrolase catalyzing hydrolysis of the terminal non-reducing β-fructofuranoside residues
68
Invertase hydrolases
α1 - β2 glycosidic bond in sucrose
69
Invertase splits what
sucrose to glucose and fructose
70
Mechanism of Invertase
α1-β2 linkage cleaved off by invertase to produce glucose and fructose
71
used to monitor enzyme activity
dinitrosalicylic acid method
72
MEchanism of DN
3,5-dinitrosalicylic acid (DNS) reacts with reducing sugars to form 3-amino-5-nitrosalicylic acid (ANS) Gluconic acid
73
TRUE OR FALSE DNS does not react with sucrose
True Sucrose is a non-reducing sugar
74
Red coloration means
higher concentration of glucose and fructose = higher invertase activity
75
Sucrose + DNS = what color
No color change
76
Sucrose + Sucrase + DNS = what color
Red brown coloration

Biochemistry Lab (2 decks)

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