Enzymes and Vitamins Flashcards
1
Q
are proteins that catalyze the body’s chemical reactions
A
Enzymes
2
Q
They can increase the rate of reaction as much as ___ by reducing the activation energy without affecting the equilibrium.
A
106
3
Q
Enzymes reducing the ___ energy without affecting the equilibrium.
A
activation
4
Q
are made up of amino acids linked together by peptide bonds. The reactant of an enzyme-catalyzed reaction is called a
A
substrate
5
Q
The specificity of the enzyme for its substrate is known as
A
molecular recognition
6
Q
are organic molecules commonly derived from vitamins.
A
coenzymes
7
Q
is a substance that the body cannot normally synthesize, but it is required in small amounts for normal body function
A
vitamins
8
Q
example of vitamins
A
niacin
vitamin B1
vitamin B2
vitamin B6
vitamin B12
vitamin H
vitamin K
9
Q
allow reactions to occur in the body that would be impossible otherwise
A
enzymes
10
Q
the enzyme recognizes its substrate based on its ___ and specific ____
A
3D shape
electrostatic interactions
11
Q
enzymatic activity is always ___
A
stereospecific
12
Q
enzyme that cleaves lactose
A
lactase
13
Q
types of enzymes
A
hydrolase
lyase
ligase
transferase
isomerase
oxidoreductase
14
Q
type of enzyme that catalyzes hydrolysis
A
hydrolase
15
Q
type of enzyme that cleaves covalent bonds
A
lyase
16
Q
enzyme that combines two molecules
A
ligase
17
Q
enzyme that transfers functional groups
A
transferase
18
Q
enzymes that catalyzes spatial rearrangement
A
isomerase
19
Q
enzyme that transfers electrons from one molecule to another
A
oxidoreductase
20
Q
Enzymes are generally very specific; they catalyze some specific chemical process; to perform their function, they often need specific substances called
A
cofactors
21
Q
If the body does not produce this material, it must be present in the diet; these cofactors are
A
vitamins
22
Q
The ____ site of an enzyme is generally hollow on the protein surface where the substrate can bind.
A
active
23
Q
is generally bound to amino acids present in the binding site by a variety of interactions such as van der Waals interaction, H-bonding and ionic bonding.
A
substrate
24
Q
what interaction can be present in enzyme-substrate complex
A
van der Waals interaction
H-bonding
ionic bonding
25
is commonly involved in enzyme-catalyzed reaction mechanisms and will form a covalent bond with the substrate as part of the reaction mechanism
what kind of amino acid
serine
26
is hydrolyzed by the enzyme acetylcholinesterase
what neurotransmitter
acetylcholine
27
are drugs that inhibit the catalytic activity of enzymes.
enzyme inhibitors
28
enzyme inhibitors can be classified as
competitive
non-competitive
29
compete with the substrate for the active site
competitive inhibitors
30
do not compete with the substrate to enter the active site. Instead, they bind at a different region of the enzyme and produce an induced fit, which changes the shape of the enzyme such as the active site no longer being available to the substrate. I
noncompetitive inhibitors
31
The binding site of the noncompetitive inhibitors is known as the
allosteric site
32
often present in the enzyme at the start of biosynthesis.
noncompetitive inhibitors
33
the inhibitor binds with the enzyme through intermolecular interactions such as H-bond, ionic bonding, and van der Waals interactions. There will be an equilibrium between the enzyme-inhibitor complex and free enzyme and unbound inhibitor
what kind of inhibitor
reversible inhibitor
34
the inhibitor may react with the enzyme generating a covalent bond. Such bonds are strong, and the enzyme remains permanently blocked making the inhibition irreversible.
non-reversible inhibitors
35
enzyme may exist in different forms having a different amino acid composition, but identical catalytic reaction
isozymes
36
how many vitamins are needed by the body in total
13 vitamins
37
two types of vitamins
water-soluble
lipid (fat)-soluble
38
dissolve in water and are able to roam freely in body in the blood
water-soluble vitamins
39
type of vitamins that is not stored in the body
water-soluble vitamins
40
need fat in order to be dissolved
require special carrier proteins to be transported in the blood
fat-soluble vitamins
41
fat soluble vitamins are stored in
fat cells
42
example of water-soluble vitamins
vitamin B
vitamin C
43
how many types of vitamin B are there
8
44
two main functions of vitamin B
make energy from food
make RBC
45
vitamin B6 and B12 deficiency can lead to
Anemia
46
deficiency in B1 and B3 lead to
mental confusion
47
most important function of vitamin C
protect the body from infection
48
deficency in vitamin C
scurvy
49
symptoms and signs can include anemia, exhaustion, spontaneous bleeding, limb pain, swelling, and sometimes ulceration of the gums and loss of teeth
scurvy
50
vitamin C is necessary to produce what kind of protein
collagen
51
main protein component of tissues
collagen
52
two fat soluble vitamins
Vitamin A
vitamin D
53
primary role is maintain and protect vision
vitamin A
54
protein that detects and absorb light in the eyes
vitamin A
55
inability to see in lowlight or darkness
Xerophthalmia
56
also known as sunshine vitamin
vitamin D
57
works to promote bone growth and bone strength
vitamin D
58
vitamin D deficiency
rickets or osteomalacia
59
active form of niacin
Nicotinamide adenine dinucleotide
60
is a coenzyme that is used by enzymes as an oxidizing agent for biological oxidations
Nicotinamide adenine dinucleotide
61
Since this is the portion of coenzyme NAD+, it is to be added to the diet so that the body can synthesize NAD+.
niacine
62
vitamin B2
riboflavin
63
riboflavin is composed of what
flavin plus ribitol
64
required to synthesize coenzyme flavin adenine dinucleotide (FAD)
riboflavin
65
an oxidizing agent in enzyme-catalyzed oxidation reactions
flavin adenine dinucleotide
66
used by succinate dehydrogenase to oxidize succinate to fumarate
FAD
67
vitamin B1
Thiamine
68
required to form the coenzyme thiamine pyrophosphate (TPP)
Thiamine (B1)
69
is required by enzymes that catalyze the transfer of two carbon fragments from one species to another
Thiamine pyrophosphate
70
what enzyme requires TPP for the decarboxylation of pyruvate and transfers the remaining two-carbon fragment to a proton to afford acetaldehyde
pyruvate decarboxylase
71
vitamin H
biotin
72
synthesized by bacteria that live in the intestines
vitamin H (bitoin)
73
does not have to be incorporated into the diet and the deficiencies are generally rare
biotin
74
is the coenzyme required by enzymes that catalyze the carboxylation of a carbon adjacent to a carbonyl group
biotin
75
The coenzyme pyridoxal phosphate (PLP) is derived from
vitamin B6
76
Enzymes that catalyze the reactions of amino acids require what coenzyme
pridoxal phosphate (PLP)
77
One of the common examples is the transamination using enzyme
aminotransferases
78
Enzymes that catalyze certain rearrangement reactions require coenzyme
B12
79
in this vitamin, the cyano group is coordinated with cobalt.
vitamin B12
80
in this coenzyme this group is replaced by a 5’-deoxyadenosine group compared to its vitamin version
coenzyme B12
81
is used by enzymes that catalyze reactions in which a group (Y) bonded to one carbon changes to hydrogen-bonded an adjacent carbon
coenzyme B12
82
is the coenzyme required by enzymes that catalyze the transfer of a group having a single carbon to their substrates
tetrahydrofolate
83
The one-carbon in folic acid may be
methyl (CH3), methylene (CH2), or formyl (CH) group
84
required for the synthesis of bases in RNA and DNA and the synthesis of some aromatic amino acids
THF
85
is the vitamin used for the synthesis of the coenzyme THF
folic acid
86
is the enzyme that catalyzes the synthesis of T’s from U’s.
thymidylate synthase
87
is synthesized by intestinal bacteria and is required for proper clotting of blood
vitamin K
88
is the coenzyme that is derived from vitamin K.
vitamin KH2
89
is required by an enzyme that catalyzes the carboxylation of the γ-carbon of glutamate side chains in proteins, forming γ-carboxyglutamates.
vitamin KH2
90
use of vitamins
metabolism
energy production
immunity
cell formation
91
may cause deficiency symptoms such as circulatory disturbance, metabolic disorder, anemia or muscular atrophy
lack of vitamins
92
13 vitamins regarded as vital for humans
Vitamin A
Vitamin B6
Vitamin C (ascorbic acid)
Vitamin B1
Vitamin B7 (Biotin)
Vitamin D
Vitamin B2
Folic acid
Vitamin E
Vitamin B3 (Niacin)
Vitamin B12 - Vitamin K
Pantothenic acid
93
Since vitamins cannot be produced by the human body itself (with the exception of
vitamin D and niacin
94
are one commonly used method in vitamin analysis
immuno-affinity columns (IAC)
95
IAC are used for sample purification prior to what process
HPLC
96
3 method of vitamins analysis
ELISA test
Microbiological test
Immuno-affinity column
97
vitamin analysis that has the ff characteristics:
25 minutes of incubation
easy to use no toxic chemicals required
used for B12 and folic acid
ELISA test
98
vitamin analysis that has the ff characteristics:
44-48 hours incubation (except Pantothenic acid -24hours)
High precision and are AOAC-RI certified
use for B12, Folid Acid, Biotin, B1, B2, B3, B6, C, Pantothenic Acid, and Inositol
Microbiological test
99
vitamin analysis that has the ff characteristics:
2-3 hours for clean-up plus HPLC or LC/MS-Analysis
High recovery
Low coefficient of variation
available for B12, Folid Acid, and Biotin
Immuno-affinity column
100
substrate bound to the enzyme using the following interactions except
Van Der Waals Interaction
H-bonding
Ionic bonding
Covalent bonding
Covalent bonding
101
metal that binds to blood clotting proteins
calcium ion
102
is a coenzyme required to catalyze carboxylation of a carbon adjacent to a carbonyl group
biotin
103
coenzyme used in oxidizing succinate to fumarate
Flavin Adenine Dinucleotide
104
a coenzyme required to catalyze the transfer of 2-carbon fragment
Thiamine Pyrophoshpate
105
vitamin required for proper blood clotting
vitamin K
106
the other name of vitamin B2 is
riboflavin
107
the following vitamisn cannot be produced by the human body except
vitamin B6
vitamin B12
Vitamin D
vitamin B1
vitamin D
108
the inhibitor that binds to the active site of the enzyme is classified as
competitive
109
coenzyme required for synthesis of RNA and DNA
Tetrahydrofolate
110
vitamin that tis part of nicotinamide adenine dinucletoide
Niacin
111
a nucleophilic amino acid
Serine
112
vitamin used in the synthesis of THF
folic acid
113
vitamin that is required in the synthesis of FAD
vitamin B2
114
among the methods used in vitamin analysis, the method that is able to analyze the most number of vitamins is
Microbiological test
115
the type of inhibitor that binds to a location other than the active site is called
non-competitive
116
enzymes are able to increase the rate of chemical reactions by
decreasing activation energy
117
all methods in the group are used in vitamin analysis except
Thermogravimetric test
118
different forms of same enzyme is called
isozyme
119
vitamin that contains a cyano group coordinated to cobalt is
vitamin B12
120
vitamin used to form TPP is
vitamin B1
121
other name for vitamin H
biotin
122
is the general term that refers to the material acted upon by an enyzme
substrate
123
organic molecule derived from a vitamin that is needed in enzyme reactions
coenzyme
124
refers to the part of an enzyme where a non-competitive inhibitor binds
allosteric site
125
vitamin that consists of a flavin group and ribitol
vitamin B2
126
is the word that stands for letter "I" in the acronym IAC
Immuno
127
the vitamin required for proper clotting of blood
vitamin K
128
specificity of an enzyme for its substrate is known as
molecular recognition
129
increases the rate of chemical reaction that is not consumed in the process
enzyme
130
nearly all are proteins
enzyme
131
any substance that increases rate or speed of chemical reaction
catalyst
132
caused by HIV
AIDS
133
oxidation and reduction reactions catalyze
what enzyme
oxidoreductases
134
catalyze oxidation-reduction reactions involving hydrogen and reductases catalyze reactions in which a substrate is reduce
oxidoreductases
135
transfer reactions of groups, such as methyl, amino and acetyl
transferases
136
catalyze the transfer of amino group
transaminases
137
catalyze the transfer of a phosphate group
kinase
138
enzyme for hydrolysis reactions
hydrolases
139
catalyze the hydrolysis of lipids
lipases
140
catalyze the hydrolysis of proteins
proteases
141
reactions in which groups are removed without hydrolysis or addition of groups to a double bond
lyases
142
catalyze the removal of carboxyl groups
carboxylases
143
reactions in which a compound is converted to its isomer
isomerases
144
may catalyze the conversion of aldose to a ketose
isomerases
145
catalyze reactions in which a functional group is transferred from one atom in a substrate to another
mutases
146
reactions in which new bonds are formed between carbon and another atom; energy is required
ligases
147
catalyzes reaction in which two smalelr molecules are linked to form a larger one
synthetases
148
formed when E-S collides (reversible)
enzyme-substrate complex
149
has pocket where the substrate can enter
enzyme surface
150
active site of an enzyme possess a unique conformation (position, bonding groups that is complementary to the structure of the substrate)
what theory
lock and key theory
151
enzymes undergoing a change in conformation when they meet the substrate
what model
induced fit model
152
enzymes have this characteristic wherein they catalyze specific compounds
substrate specificty
153
monitored by the rate of substrate disappearing or product forming
activity of enzyme
154
can disrupt protein structure
temperature
155
* Denaturation of enzymes occur at
45-55
156
can be used as enzyme inhibitors but is irreversibles
poisons
157
inhibits glyceraldehyde 3-phosphate dehydrogenase, substitute for phosphate
what poison
arsenate
158
inhibits triose phosphate dehydrogenase
binds to cysteine SH group
what poison
iodoacetate
159
inhibits acetylcholintesterase
binds to serine OH group
DIFP
160
a nerve poison
diisopropylfluoro-phosphate
161
formation of vision pigments; differentiation of epithelial cells
what kind of vitamin
vitamin A
162
vitamin A is also known as
retinol
163
night blindness; continued deficency lead to total blindness
what kind of vitamin deficiency
vitamin A (retinol)
164
increases the body's ability to absorb calcium and phosphorus
what kind of vitamin
Vitamin D (cholecalciferol)
165
deficiency leads to osteomalacia; known as rickets in children
what kind of vitamin
vitamin D
166
softening of bones in adults
osteomalacia
167
softening of bones in children
rickets
168
fat-soluble antioxidant
vitamin E
169
damage to cell membrane
what kind of vitamin deficiency
vitamin E (tocopherol)
170
vitamin E is also known as
tocopherol
171
formation of prothrombin, a key enzyme in blood clotting process
what kind of vitamin
vitamin K (phylloquinone)
172
vitamin K is also known as
phylloquinone
173
increases the time required for the blood to clot
what kind of vitamin deficiency
vitamin K (phylloquinone)
174
fat-soluble vitamins are
vitamins ADEK
175
has active form of thiamine pyrophoasphate functioning in decarboylation reactions
vitamin B1 (thiamine)
176
vitamin B1 is also known as
thiamine
177
deficiency in this vitamin leads to beri-beri
vitamin B1 (thiamine)
178
a disease caused by vitamin B1 deficiency, also known as thiamine deficiency. It occurs most often in people with a diet that consists mostly of white rice or highly refined carbohydrates.
beriberi
179
NAD, NADH used in oxidation-reduction reactions involving the hydride ion
vitamin B3 (niacin)
180
deficiency can lead to pellagra
vitamin B3
181
a systemic disease caused by a severe deficiency of niacin (vitamin B3). It affects the whole body and can eventually lead to death.
pellagra
182
pyridoxal phosphate
variety of reactions including transfer of amino groups
what vitamin
vitamin B6 (pyridoxine)
183
methylcobalamin or deoxyadenoxycobalamin
intramolecular rearrangement reactions
vitamin B12
184
deficiency can lead to pernicious anemia
vitamin B12
185
one of the causes of vitamin B12 deficiency, is an autoimmune condition that prevents your body from absorbing vitamin B12
Pernicious anemia
186
is a decrease in red blood cells that occurs when the intestines cannot properly absorb vitamin B12
pernicious anemia
187
tetrahydrofolate
carrier of one-carbon units such as the formyl group
folic acid
188
deficiency can lead to anemia
folic acid
189
is a condition that develops when your blood produces a lower-than-normal amount of healthy red blood cells
anemia
190
carrier of acyl groups
coenzyme A
pantothenic acid
191
antioxidant; formation of collagen
vitamin C (ascorbic acd)
