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Biomolecules > Enzymes and Vitamins > Flashcards

Enzymes and Vitamins Flashcards

1
Q

are proteins that catalyze the body’s chemical reactions

A

Enzymes

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2
Q

They can increase the rate of reaction as much as ___ by reducing the activation energy without affecting the equilibrium.

A

106

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3
Q

Enzymes reducing the ___ energy without affecting the equilibrium.

A

activation

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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

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5
Q

The specificity of the enzyme for its substrate is known as

A

molecular recognition

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6
Q

are organic molecules commonly derived from vitamins.

A

coenzymes

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7
Q

is a substance that the body cannot normally synthesize, but it is required in small amounts for normal body function

A

vitamins

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8
Q

example of vitamins

A

niacin
vitamin B1
vitamin B2
vitamin B6
vitamin B12
vitamin H
vitamin K

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9
Q

allow reactions to occur in the body that would be impossible otherwise

A

enzymes

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10
Q

the enzyme recognizes its substrate based on its ___ and specific ____

A

3D shape
electrostatic interactions

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11
Q

enzymatic activity is always ___

A

stereospecific

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12
Q

enzyme that cleaves lactose

A

lactase

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13
Q

types of enzymes

A

hydrolase
lyase
ligase
transferase
isomerase
oxidoreductase

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14
Q

type of enzyme that catalyzes hydrolysis

A

hydrolase

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15
Q

type of enzyme that cleaves covalent bonds

A

lyase

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16
Q

enzyme that combines two molecules

A

ligase

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17
Q

enzyme that transfers functional groups

A

transferase

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18
Q

enzymes that catalyzes spatial rearrangement

A

isomerase

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19
Q

enzyme that transfers electrons from one molecule to another

A

oxidoreductase

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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

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21
Q

If the body does not produce this material, it must be present in the diet; these cofactors are

A

vitamins

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22
Q

The ____ site of an enzyme is generally hollow on the protein surface where the substrate can bind.

A

active

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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

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24
Q

what interaction can be present in enzyme-substrate complex

A

van der Waals interaction
H-bonding
ionic bonding

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25
Q

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

A

serine

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26
Q

is hydrolyzed by the enzyme acetylcholinesterase

what neurotransmitter

A

acetylcholine

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27
Q

are drugs that inhibit the catalytic activity of enzymes.

A

enzyme inhibitors

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28
Q

enzyme inhibitors can be classified as

A

competitive
non-competitive

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29
Q

compete with the substrate for the active site

A

competitive inhibitors

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30
Q

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

A

noncompetitive inhibitors

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31
Q

The binding site of the noncompetitive inhibitors is known as the

A

allosteric site

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32
Q

often present in the enzyme at the start of biosynthesis.

A

noncompetitive inhibitors

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33
Q

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

A

reversible inhibitor

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34
Q

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.

A

non-reversible inhibitors

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35
Q

enzyme may exist in different forms having a different amino acid composition, but identical catalytic reaction

A

isozymes

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36
Q

how many vitamins are needed by the body in total

A

13 vitamins

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37
Q

two types of vitamins

A

water-soluble
lipid (fat)-soluble

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38
Q

dissolve in water and are able to roam freely in body in the blood

A

water-soluble vitamins

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39
Q

type of vitamins that is not stored in the body

A

water-soluble vitamins

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40
Q

need fat in order to be dissolved

require special carrier proteins to be transported in the blood

A

fat-soluble vitamins

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41
Q

fat soluble vitamins are stored in

A

fat cells

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42
Q

example of water-soluble vitamins

A

vitamin B
vitamin C

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43
Q

how many types of vitamin B are there

A

8

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44
Q

two main functions of vitamin B

A

make energy from food
make RBC

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45
Q

vitamin B6 and B12 deficiency can lead to

A

Anemia

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46
Q

deficiency in B1 and B3 lead to

A

mental confusion

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47
Q

most important function of vitamin C

A

protect the body from infection

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48
Q

deficency in vitamin C

A

scurvy

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49
Q

symptoms and signs can include anemia, exhaustion, spontaneous bleeding, limb pain, swelling, and sometimes ulceration of the gums and loss of teeth

A

scurvy

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50
Q

vitamin C is necessary to produce what kind of protein

A

collagen

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51
Q

main protein component of tissues

A

collagen

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52
Q

two fat soluble vitamins

A

Vitamin A
vitamin D

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53
Q

primary role is maintain and protect vision

A

vitamin A

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54
Q

protein that detects and absorb light in the eyes

A

vitamin A

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55
Q

inability to see in lowlight or darkness

A

Xerophthalmia

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56
Q

also known as sunshine vitamin

A

vitamin D

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57
Q

works to promote bone growth and bone strength

A

vitamin D

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58
Q

vitamin D deficiency

A

rickets or osteomalacia

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59
Q

active form of niacin

A

Nicotinamide adenine dinucleotide

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60
Q

is a coenzyme that is used by enzymes as an oxidizing agent for biological oxidations

A

Nicotinamide adenine dinucleotide

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61
Q

Since this is the portion of coenzyme NAD+, it is to be added to the diet so that the body can synthesize NAD+.

A

niacine

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62
Q

vitamin B2

A

riboflavin

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63
Q

riboflavin is composed of what

A

flavin plus ribitol

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64
Q

required to synthesize coenzyme flavin adenine dinucleotide (FAD)

A

riboflavin

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65
Q

an oxidizing agent in enzyme-catalyzed oxidation reactions

A

flavin adenine dinucleotide

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66
Q

used by succinate dehydrogenase to oxidize succinate to fumarate

A

FAD

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67
Q

vitamin B1

A

Thiamine

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68
Q

required to form the coenzyme thiamine pyrophosphate (TPP)

A

Thiamine (B1)

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69
Q

is required by enzymes that catalyze the transfer of two carbon fragments from one species to another

A

Thiamine pyrophosphate

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70
Q

what enzyme requires TPP for the decarboxylation of pyruvate and transfers the remaining two-carbon fragment to a proton to afford acetaldehyde

A

pyruvate decarboxylase

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71
Q

vitamin H

A

biotin

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72
Q

synthesized by bacteria that live in the intestines

A

vitamin H (bitoin)

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73
Q

does not have to be incorporated into the diet and the deficiencies are generally rare

A

biotin

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74
Q

is the coenzyme required by enzymes that catalyze the carboxylation of a carbon adjacent to a carbonyl group

A

biotin

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75
Q

The coenzyme pyridoxal phosphate (PLP) is derived from

A

vitamin B6

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76
Q

Enzymes that catalyze the reactions of amino acids require what coenzyme

A

pridoxal phosphate (PLP)

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77
Q

One of the common examples is the transamination using enzyme

A

aminotransferases

78
Q

Enzymes that catalyze certain rearrangement reactions require coenzyme

A

B12

79
Q

in this vitamin, the cyano group is coordinated with cobalt.

A

vitamin B12

80
Q

in this coenzyme this group is replaced by a 5’-deoxyadenosine group compared to its vitamin version

A

coenzyme B12

81
Q

is used by enzymes that catalyze reactions in which a group (Y) bonded to one carbon changes to hydrogen-bonded an adjacent carbon

A

coenzyme B12

82
Q

is the coenzyme required by enzymes that catalyze the transfer of a group having a single carbon to their substrates

A

tetrahydrofolate

83
Q

The one-carbon in folic acid may be

A

methyl (CH3), methylene (CH2), or formyl (CH) group

84
Q

required for the synthesis of bases in RNA and DNA and the synthesis of some aromatic amino acids

A

THF

85
Q

is the vitamin used for the synthesis of the coenzyme THF

A

folic acid

86
Q

is the enzyme that catalyzes the synthesis of T’s from U’s.

A

thymidylate synthase

87
Q

is synthesized by intestinal bacteria and is required for proper clotting of blood

A

vitamin K

88
Q

is the coenzyme that is derived from vitamin K.

A

vitamin KH2

89
Q

is required by an enzyme that catalyzes the carboxylation of the γ-carbon of glutamate side chains in proteins, forming γ-carboxyglutamates.

A

vitamin KH2

90
Q

use of vitamins

A

metabolism
energy production
immunity
cell formation

91
Q

may cause deficiency symptoms such as circulatory disturbance, metabolic disorder, anemia or muscular atrophy

A

lack of vitamins

92
Q

13 vitamins regarded as vital for humans

A

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
Q

Since vitamins cannot be produced by the human body itself (with the exception of

A

vitamin D and niacin

94
Q

are one commonly used method in vitamin analysis

A

immuno-affinity columns (IAC)

95
Q

IAC are used for sample purification prior to what process

A

HPLC

96
Q

3 method of vitamins analysis

A

ELISA test
Microbiological test
Immuno-affinity column

97
Q

vitamin analysis that has the ff characteristics:

25 minutes of incubation

easy to use no toxic chemicals required

used for B12 and folic acid

A

ELISA test

98
Q

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

A

Microbiological test

99
Q

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

A

Immuno-affinity column

100
Q

substrate bound to the enzyme using the following interactions except

Van Der Waals Interaction
H-bonding
Ionic bonding
Covalent bonding

A

Covalent bonding

101
Q

metal that binds to blood clotting proteins

A

calcium ion

102
Q

is a coenzyme required to catalyze carboxylation of a carbon adjacent to a carbonyl group

A

biotin

103
Q

coenzyme used in oxidizing succinate to fumarate

A

Flavin Adenine Dinucleotide

104
Q

a coenzyme required to catalyze the transfer of 2-carbon fragment

A

Thiamine Pyrophoshpate

105
Q

vitamin required for proper blood clotting

A

vitamin K

106
Q

the other name of vitamin B2 is

A

riboflavin

107
Q

the following vitamisn cannot be produced by the human body except

vitamin B6
vitamin B12
Vitamin D
vitamin B1

A

vitamin D

108
Q

the inhibitor that binds to the active site of the enzyme is classified as

A

competitive

109
Q

coenzyme required for synthesis of RNA and DNA

A

Tetrahydrofolate

110
Q

vitamin that tis part of nicotinamide adenine dinucletoide

A

Niacin

111
Q

a nucleophilic amino acid

A

Serine

112
Q

vitamin used in the synthesis of THF

A

folic acid

113
Q

vitamin that is required in the synthesis of FAD

A

vitamin B2

114
Q

among the methods used in vitamin analysis, the method that is able to analyze the most number of vitamins is

A

Microbiological test

115
Q

the type of inhibitor that binds to a location other than the active site is called

A

non-competitive

116
Q

enzymes are able to increase the rate of chemical reactions by

A

decreasing activation energy

117
Q

all methods in the group are used in vitamin analysis except

A

Thermogravimetric test

118
Q

different forms of same enzyme is called

A

isozyme

119
Q

vitamin that contains a cyano group coordinated to cobalt is

A

vitamin B12

120
Q

vitamin used to form TPP is

A

vitamin B1

121
Q

other name for vitamin H

A

biotin

122
Q

is the general term that refers to the material acted upon by an enyzme

A

substrate

123
Q

organic molecule derived from a vitamin that is needed in enzyme reactions

A

coenzyme

124
Q

refers to the part of an enzyme where a non-competitive inhibitor binds

A

allosteric site

125
Q

vitamin that consists of a flavin group and ribitol

A

vitamin B2

126
Q

is the word that stands for letter “I” in the acronym IAC

A

Immuno

127
Q

the vitamin required for proper clotting of blood

A

vitamin K

128
Q

specificity of an enzyme for its substrate is known as

A

molecular recognition

129
Q

increases the rate of chemical reaction that is not consumed in the process

A

enzyme

130
Q

 nearly all are proteins

A

enzyme

131
Q

any substance that increases rate or speed of chemical reaction

A

catalyst

132
Q

caused by HIV

A

AIDS

133
Q

oxidation and reduction reactions catalyze

what enzyme

A

oxidoreductases

134
Q

catalyze oxidation-reduction reactions involving hydrogen and reductases catalyze reactions in which a substrate is reduce

A

oxidoreductases

135
Q

transfer reactions of groups, such as methyl, amino and acetyl

A

transferases

136
Q

catalyze the transfer of amino group

A

transaminases

137
Q

catalyze the transfer of a phosphate group

A

kinase

138
Q

enzyme for hydrolysis reactions

A

hydrolases

139
Q

catalyze the hydrolysis of lipids

A

lipases

140
Q

catalyze the hydrolysis of proteins

A

proteases

141
Q

reactions in which groups are removed without hydrolysis or addition of groups to a double bond

A

lyases

142
Q

catalyze the removal of carboxyl groups

A

carboxylases

143
Q

reactions in which a compound is converted to its isomer

A

isomerases

144
Q

may catalyze the conversion of aldose to a ketose

A

isomerases

145
Q

catalyze reactions in which a functional group is transferred from one atom in a substrate to another

A

mutases

146
Q

reactions in which new bonds are formed between carbon and another atom; energy is required

A

ligases

147
Q

catalyzes reaction in which two smalelr molecules are linked to form a larger one

A

synthetases

148
Q

formed when E-S collides (reversible)

A

enzyme-substrate complex

149
Q

has pocket where the substrate can enter

A

enzyme surface

150
Q

active site of an enzyme possess a unique conformation (position, bonding groups that is complementary to the structure of the substrate)

what theory

A

lock and key theory

151
Q

enzymes undergoing a change in conformation when they meet the substrate

what model

A

induced fit model

152
Q

enzymes have this characteristic wherein they catalyze specific compounds

A

substrate specificty

153
Q

monitored by the rate of substrate disappearing or product forming

A

activity of enzyme

154
Q

can disrupt protein structure

A

temperature

155
Q
  • Denaturation of enzymes occur at
A

45-55

156
Q

can be used as enzyme inhibitors but is irreversibles

A

poisons

157
Q

inhibits glyceraldehyde 3-phosphate dehydrogenase, substitute for phosphate

what poison

A

arsenate

158
Q

inhibits triose phosphate dehydrogenase

binds to cysteine SH group

what poison

A

iodoacetate

159
Q

inhibits acetylcholintesterase

binds to serine OH group

A

DIFP

160
Q

a nerve poison

A

diisopropylfluoro-phosphate

161
Q

formation of vision pigments; differentiation of epithelial cells

what kind of vitamin

A

vitamin A

162
Q

vitamin A is also known as

A

retinol

163
Q

night blindness; continued deficency lead to total blindness

what kind of vitamin deficiency

A

vitamin A (retinol)

164
Q

increases the body’s ability to absorb calcium and phosphorus

what kind of vitamin

A

Vitamin D (cholecalciferol)

165
Q

deficiency leads to osteomalacia; known as rickets in children

what kind of vitamin

A

vitamin D

166
Q

softening of bones in adults

A

osteomalacia

167
Q

softening of bones in children

A

rickets

168
Q

fat-soluble antioxidant

A

vitamin E

169
Q

damage to cell membrane

what kind of vitamin deficiency

A

vitamin E (tocopherol)

170
Q

vitamin E is also known as

A

tocopherol

171
Q

formation of prothrombin, a key enzyme in blood clotting process

what kind of vitamin

A

vitamin K (phylloquinone)

172
Q

vitamin K is also known as

A

phylloquinone

173
Q

increases the time required for the blood to clot

what kind of vitamin deficiency

A

vitamin K (phylloquinone)

174
Q

fat-soluble vitamins are

A

vitamins ADEK

175
Q

has active form of thiamine pyrophoasphate functioning in decarboylation reactions

A

vitamin B1 (thiamine)

176
Q

vitamin B1 is also known as

A

thiamine

177
Q

deficiency in this vitamin leads to beri-beri

A

vitamin B1 (thiamine)

178
Q

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.

A

beriberi

179
Q

NAD, NADH used in oxidation-reduction reactions involving the hydride ion

A

vitamin B3 (niacin)

180
Q

deficiency can lead to pellagra

A

vitamin B3

181
Q

a systemic disease caused by a severe deficiency of niacin (vitamin B3). It affects the whole body and can eventually lead to death.

A

pellagra

182
Q

pyridoxal phosphate

variety of reactions including transfer of amino groups

what vitamin

A

vitamin B6 (pyridoxine)

183
Q

methylcobalamin or deoxyadenoxycobalamin

intramolecular rearrangement reactions

A

vitamin B12

184
Q

deficiency can lead to pernicious anemia

A

vitamin B12

185
Q

one of the causes of vitamin B12 deficiency, is an autoimmune condition that prevents your body from absorbing vitamin B12

A

Pernicious anemia

186
Q

is a decrease in red blood cells that occurs when the intestines cannot properly absorb vitamin B12

A

pernicious anemia

187
Q

tetrahydrofolate

carrier of one-carbon units such as the formyl group

A

folic acid

188
Q

deficiency can lead to anemia

A

folic acid

189
Q

is a condition that develops when your blood produces a lower-than-normal amount of healthy red blood cells

A

anemia

190
Q

carrier of acyl groups

coenzyme A

A

pantothenic acid

191
Q

antioxidant; formation of collagen

A

vitamin C (ascorbic acd)

Biomolecules (19 decks)

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