Enzymes And Vitamins

Question 1

This is the process of chemical and physical change which goes on continually in the living organism

Answer 1

Metabolism

Question 2

The acceleration of a chemical reaction by some substance which itself undergoes no permanent chemical change.

Answer 2

Catalysis

Question 3

The catalysts of biochemical reactions are

Answer 3

Enzymes

Question 4

are composed of long chains of amino acids that have folded into a very specific three-dimensional shape which contains an active site.

Answer 4

Enzymes

Question 5

a region on the surface of an enzyme to which substrates will bind and catalyzes a chemical reaction.

Answer 5

Active site

Question 6

a molecule that an enzyme reacts

Answer 6

Substrate

Question 7

Enzymes have molecular weights ranging from

Answer 7

10,000 to 2,000,000

Question 8

are macromolecules that catalyze chemical reactions in the body.

Answer 8

Enzymes

Question 9

Enzymes catalyze reactions by weakening?

Answer 9

chemical bonds

Question 10

Has a unique 3d shape

Answer 10

Enzymes

Question 11

Each enzyme has a unique 3-D shape, including a surface groove called on

Answer 11

Active site

Question 12

are enzymes made of ribonucleic acids.

Answer 12

Ribozymes

Question 13

catalyzes only the hydrolysis of urea and not that of other amides, even closely related ones

Answer 13

Urease

Question 14

an enzyme that cleaves the peptide bonds of protein molecules—but not every peptide bond, only those on the carboxyl side of lysine and arginine residues.

Answer 14

Trypsin

Question 15

specifically catalyzes the hydrolysis of only the last amino acid on a protein chain-the one at the C-terminal end.

Answer 15

carboxypeptidase

Question 16

They catalyze the hydrolysis of any triglyceride, but they still do not affect carbohydrates or proteins

Answer 16

Lipases

Question 17

hydrolyzes the amino acid L-arginine (the naturally occurring form) to a compound called L-ornithine and urea but has no effect on its mirror image, D-arginine.

Answer 17

arginase

Question 18

earliest studies were performed in 1835 by the Swedish chemist who termed their chemical action catalytic?

Answer 18

Jon Jakob Berzelius

Question 19

earliest studies were performed in 1835 by the Swedish chemist Jon Jakob Berzelius who termed their?

Answer 19

chemical action catalytic

Question 20

What year the first enzyme was obtained in pure form?

Answer 20

1926

Question 21

In 1926, the first enzyme was obtained in pure form, a feat accomplished by?

Answer 21

James B. Sumner

Question 22

He was able to isolate and crystallize the enzyme urease from the jack bean.

Answer 22

James B. Sumner

Question 23

James B. Sumner work was to earn him the?

Answer 23

1947 Nobel Prize

Question 24

• They discovered a complex procedure for isolating pepsin.
• Shared the 1947
  Nobel Prize with Sumner.

Answer 24

John H. Northrop and Wendell M.
Stanley

Question 25

speeds up the removal of hydrogen from lactate

Answer 25

lactate dehydrogenase

Question 26

catalyzes the hydrolysis of phosphate ester bonds under acidic conditions.

Answer 26

Acid phosphatase

Question 27

the names of most enzymes end in

Answer 27

-ase

Question 28

Some enzymes, however, have older names, which were assigned before their actions were clearly understood. Among these are? ( all enzymes of the digestive tract. )

Answer 28

pepsin, trypsin, and chymotrypsin

Question 29

catalyze oxidations and reductions

Answer 29

EC 1 - oxidoreductases

Question 30

catalyze the transfer of a group of atoms, such as from one molecule to another

Answer 30

EC 2 - transferases

Question 31

catalyze hydrolysis reactions

Answer 31

EC 3 - hydrolases

Question 32

catalyze the addition of two groups to a double bond or the removal of two groups from adjacent atoms to create a double bond

Answer 32

EC 4 - lyases

Question 33

catalyze isomerization reactions

Answer 33

EC 5 - isomerases

Question 34

catalyze the joining of two molecules

Answer 34

EC 6 - ligases

Question 35

an enzyme that oxidizes a substrate by transferring one or more hydrides (H-) to an acceptor, usually NAD+/NADP+ or a flavin coenzyme FAD or FMN.

Answer 35

Dehydrogenase

Question 36

tricarboxylic acid cycle, (TCA cycle),
also called?

Answer 36

Krebs cycle and citric acid cycle

Question 37

The second stage of cellular respiration. the three-stage process by which living cells break down organic fuel molecules in the presence of oxygen to harvest the energy they need to grow and divide.

Answer 37

tricarboxylic acid cycle, (TCA cycle)

Question 38

An enzyme that catalyzes an oxidation-reduction reaction involving molecular oxygen (O2) as the electron acceptor.

Answer 38

Oxidase

Question 39

An enzyme that catalyzes a type of reaction between an amino acid and alpha-keto acid.

Answer 39

Transaminase

Question 40

an enzyme that transfers phosphate groups from high-energy molecules, such as ATP, to specific substrates.

Answer 40

Kinase

Question 41

a water-soluble enzyme that catalyzes the hydrolysis of ester chemical bonds in water-soluble substrates. It helps your body digest fats.

Answer 41

Lipase

Question 42

• an enzyme that breaks starch down into sugar.
• an enzyme, or special protein, that helps you digest carbohydrates

Answer 42

Amylase

Question 43

an enzyme that catalyzes (increases reaction rate or “speeds up”) proteolysis, breaking down proteins into smaller polypeptides or single amino acids, and spurring the formation of new protein products.

Answer 43

Peptidase

Question 44

enzymes that catalyze decarboxylation of amino acids, beta-keto acids, and alpha-keto acids.

Answer 44

Decarboxylases

Question 45

an enzyme that catalyzes the structural rearrangement of isomers.

Answer 45

Isomerase

Question 46

an enzyme that catalyzes the shifting/movement of a functional group from one position to another within the same molecule.

Answer 46

Mutase

Question 47

Other enzymes contain nonprotein portions called?

Answer 47

cofactors

Question 48

The protein (polypeptide) portion of the enzyme is called an?

Answer 48

apoenzyme

Question 49

Organic cofactors are called

Answer 49

coenzymes

Question 50

Enzyme along with its
cofactor?

Answer 50

Holoenzyme

Question 51

When cofactor Is
Removed Enzyme is?

Answer 51

Apoenzyme

Question 52

What vitamins are important group of coenzymes which are essential to the activity of many enzymes.

Answer 52

B vitamins

Question 53

Another important coenzyme which is part of several oxidoreductases as well as part of hemoglobin.

Answer 53

heme

Question 54

• The compound on which the enzyme works, and whose reaction it speeds up, is called the?

Answer 54

substrate

Question 55

usually binds to the enzyme surface while it undergoes the reaction.

Answer 55

Substrate

Question 56

The substrate binds to a specific portion of the enzyme during the reaction, called the?

Answer 56

active site

Question 57

is any process that initiates or increases the action of an enzyme. It can be the simple addition of a cofactor to an apoenzyme or the cleavage of a polypeptide chain of a proenzyme.

Answer 57

Activation

Question 58

A process that makes an active enzyme less active or inactive.

Answer 58

Inhibition

Question 59

bind to the active site of the enzyme surface, thereby preventing the binding of substrate.

Answer 59

Competitive inhibitors

Question 60

bind to some other portion of the enzyme surface and sufficiently alter the tertiary structure of the enzyme so that its catalytic effectiveness is eliminated. That is, the enzyme cannot catalyze while the inhibitor is bound.

Answer 60

Noncompetitive inhibitors

Question 61

The nonprotein part of an enzyme necessary for its catalytic function.

Answer 61

Cofactor

Question 62

A nonprotein organic molecule, frequently a B vitamin, that acts as a cofactor.

Answer 62

Coenzyme

Question 63

A three-dimensional cavity of the enzyme with specific chemical properties that enable it to accommodate the substrate.

Answer 63

Active site

Question 64

A compound that binds to an enzyme and lowers its activity.

Answer 64

Inhibitor

Question 65

This person suggested that catalysts speed up reactions by combining with the substrate to form some kind of intermediate compound. In an enzyme- catalysed reaction, this intermediate is called the enzyme substrate complex.

Answer 65

Arrhenius

Question 66

Arrhenius suggested that catalysts speed up reactions by combining with the substrate to form some kind of intermediate compound. In an enzyme- catalysed reaction, this intermediate is called the?

Answer 66

enzyme-substrate complex.

Question 67

This model assumes that the enzyme is a rigid three-dimensional body.
The surface that contains the active site has a restricted opening into which only one kind of substrate can fit, just as only the proper key can fit exactly into a lock and turn it open.

Answer 67

lock-and-key model

Question 68

A model explaining the specificity of enzyme action by comparing the active site to a lock and the substrate to a key.

Answer 68

Lock-and-key model

Question 69

He introduced the induced-fit model,

Answer 69

Daniel Koshland

Question 70

the changes occurring in the shape of the cavity upon substrate binding to the changes in the shape of a glove when a hand is inserted.

Answer 70

induced-fit model

Question 71

forms covalent or very strong noncovalent bonds. The site of attack is an amino acid group that participates in the normal enzymatic reaction.

Answer 71

Irreversible inhibitor

Question 72

forms weak, noncovalent bonds that readily dissociate from an enzyme. The enzyme is only inactive when the inhibitor is present.

Answer 72

Reversible inhibitor

Question 73

A survey of known active sites of enzymes shows that five amino acids participate in the active sites in more than 65% of all cases. They are, in order of their dominance, what are those amino acids?

Answer 73

His > Cys > Asp > Arg > Glu

Question 74

before A and B can become C and D, they must pass through a?

Answer 74

transition state

Question 75

The energy required to climb this hill is the?

Answer 75

activation energy

Question 76

is a protease, an enzyme that cleaves peptide bonds as we saw with trypsin.

Answer 76

papain

Question 77

helps attract the peptide and hold it in the correct orientation via hydrogen bonding

Answer 77

histidine

Question 78

The sulfur on the cysteine side chain performs a type of reaction called a?

Answer 78

nucleophilic attack

Question 79

This enzyme catalyzes the transfer of the phosphate group from phosphoenolpyruvate (PEP) to ADP, an important step in glycolysis.

Answer 79

pyruvate kinase

Question 80

Enzyme activity is regulated by five mechanisms:

Answer 80

• Feedback Control
• Proenzymes
• Allosterism
• Protein Modification
• Isoenzymes

Question 81

• is an enzyme regulation process in which formation of a product inhibits an earlier reaction in the sequence.
• The reaction product of one enzyme may control the activity of another, especially in a complex system in which enzymes work cooperatively. For example, in such a system, each step is catalyzed by a different enzyme:

Answer 81

Feedback control

Question 82

Some enzymes are manufactured by the body in an inactive form. To make them active, a small part of their polypeptide chain must be removed. These inactive forms of enzymes are called?

Answer 82

proenzymes

Question 83

Proenzymes are also called?

Answer 83

Zymogens

Question 84

a protein that becomes an active enzyme after undergoing a chemical change.

Answer 84

Proenzyme (zymogen)

Question 85

Enzyme regulation based on an event occurring at a place other than the active site but that creates a change in the active site.

Answer 85

Allosterism

Question 86

an enzyme regulated by allosterism mechanism is called an

Answer 86

allosteric enzyme

Question 87

an enzyme in which the binding of a regulator on one site on the enzyme modifies the enzyme’s ability to bind the substrate in the active site.

Answer 87

Allosteric enzyme

Question 88

The substance that binds to an allosteric enzyme is called a

Answer 88

regulator

Question 89

the site to which regulator attaches is called a

Answer 89

regulatory site

Question 90

The modulator, also called the? Can have a positive or negative effect on allosteric enzyme activity

Answer 90

regulator or effector

Question 91

can have a postive or negative effect on allosteric enzyme activity

Answer 91

modulator

Question 92

bind with an allosteric site on the enzyme and stabilize the ACTIVE conformation therefore speeding up the reaction rate.

Answer 92

Positive Modulators (activators)

Question 93

bind to an allosteric site that stabilizes the INACTIVE conformation of the molecule therefore slowing the
reaction rate.

Answer 93

Negative Modulators (inhibitors)

Question 94

Binding of a regulator to a site other than the active site changes the shape of the active site.

Answer 94

The allosteric effect

Question 95

In allosterism this more active form is regulators are seen to function by active site changes the referred to as the

Answer 95

R form

Question 96

R form, where “R” stands for?

Answer 96

relaxed

Question 97

In allosterism the less active form is referred to as?

Answer 97

T form

Question 98

T form, where “T” stands for?

Answer 98

taut

Question 99

The modification is usually a change in the primary structure, typically by addition of a functional group covalently bound to the apoenzyme.

Answer 99

protein modification

Question 100

Enzymes that catalyze such
phosphorylation go by the common name of

Answer 100

kinases

Question 101

catalyzes the oxidation of lactate to pyruvate, and vice versa.

Answer 101

Lactate dehydrogenase (LDH)

Question 102

Two kinds of subunits in isoenzymes, called?

Answer 102

H and M

Question 103

The enzyme that dominates in the heart is an

Answer 103

H4 enzyme

Question 104

In the liver and skeletal muscles, what type of subunit dominates?

Answer 104

M-type

Question 105

Other types of tetramer combinations exist in different tissues:

Answer 105

H3M, H2M2 and HM3

Question 106

Other types of tetramer combinations exist in different tissues:
H3M, H2M2, and HM3. These different forms of the same enzyme are called?

Answer 106

isozymes or isoenzymes

Question 107

enzymes that perform the same function but have different combinations of subunits and thus different quaterary structures.

Answer 107

Isozymes (Isoenzymes)

Question 108

LDH is used to convert lactate to? in the heart.

Answer 108

pyruvate

Question 109

The M4 isozyme favors the production of?

Answer 109

lactate

Question 110

The distribution of LDH isozymes can be seen using the technique of?

Answer 110

electrophoresis

Question 111

The distribution of LDH isozymes can be seen using the technique of electrophoresis, where samples are separated in a gel using an?

Answer 111

electric field

Question 112

a molecule that mimics the transition state of a chemical reaction and that is used as an inhibitor of an enzyme.

Answer 112

Transition-state analog

Question 113

catalyzes a reaction that converts L-proline to D-proline.

Answer 113

Proline racemase

Question 114

it has been over 50 years since the last of the known vitamins was discovered. What is the vitamin?

Answer 114

Vitamin B12

Question 115

Solubility characteristics divide the vitamins into two major classes:

Answer 115

the water-soluble vitamins and the fat (lipid)-soluble vitamins.

Question 116

must be constantly replenished in the body because they are rapidly eliminated from the body in the urine. They are carried in the bloodstream, are needed in frequent, small doses, and are unlikely to be toxic except when taken in unusually large doses.

Answer 116

Water-soluble vitamins

Question 117

are found dissolved in lipid materials. They are, in general, carried in the blood by protein carriers, are stored in fat tissues, are needed in periodic doses, and are more likely to be toxic when consumed in excess of need.

Answer 117

The fat-soluble vitamins

Question 118

Water-soluble vitamins function as?

Answer 118

coenzymes

Question 119

has the simplest structure of the 13 vitamins

Answer 119

Vitamin C

Question 120

Vitamin C, which has the simplest structure of the 13 vitamins, exists in two active forms in the human body:

Answer 120

an oxidized form and a reduced form

Question 121

Vitamin C also functions as a? for water-soluble substances in the blood and other body fluids.

Answer 121

General antioxidant

Question 122

Vitamin C’s biosynthesis involves?

Answer 122

L-gulonic acid

Question 123

L-gulonic acid, an acid derivative of the monosaccharide?

Answer 123

L-gulose

Question 124

An intake of what mg/day? of vitamin C saturates all body tissues with the compound.

Answer 124

100 mg/day

Question 125

Vitamin B involves four topics:

Answer 125

nomenclature, function, structural characteristics, and dietary sources.

Question 126

Water-soluble vitamins:

Answer 126

• Thiamin (vitamin B1)
• Riboflavin (vitamin B2)
• Niacin (nicotinic acid, nicotinamide, vitamin B3)
• Vitamin B6 (pyridoxine, pyridoxal, pyridoxamine)
• Folate (folic acid)
• Vitamin B12 (cobalamin)
• Pantothenic acid (vitamin B5)
• Biotin
• Vitamin C

Question 127

Fat-solube vitamins

Answer 127

• Vitamin A
• Vitamin D
• Vitamin E
• Vitamin K

Question 128

B vitamin structure is very diverse. The only common thread among structures is that all structures, except that of ? , involve heterocyclic nitrogen ring systems.

Answer 128

pantothenic acid

Question 129

B vitamin structure is very diverse. The only common thread among structures is that all structures, except that of pantothenic acid, involve?

Answer 129

heterocyclic nitrogen ring systems

Question 130

The element sulfur is present in two structures, what are those?

Answer 130

(thiamin and biotin) and B12

Question 131

vitamin B12 contains a?

Answer 131

metal atom

Question 132

have been linked positively to improvement in cardiovascular health.

Answer 132

niacin and folate

Question 133

is the most effective treatment currently available to increase low levels of HDL

Answer 133

prescription niacin

Question 134

Another study shows that younger women (26-46 years old) who consume 800 μg of folate per day reduce the risk of developing ? by almost a third compared to those who consume less than 200 μg/day

Answer 134

high blood pressure

Question 135

Many of the functions of the fat-soluble vitamins involve processes that occur in?

Answer 135

cell membranes

Question 136

Normal dietary intake provides a person with both ? forms of vitamin A

Answer 136

preformed and precursor

Question 137

Preformed vitamin A forms are called?

Answer 137

retinoids

Question 138

The retinoids include?

Answer 138

retinal, retinol, and retinoic acid

Question 139

The major carotenoid with vitamin A activity is? which can be cleaved to yield two molecules of vitamin A.

Answer 139

beta-carotene

Question 140

is a yellow to red-orange pigment plentiful in carrots, squash, cantaloupe, apricots, and other yellow vegetables and fruits, as well as in leafy green vegetables (where the yellow pigment is masked by green chlorophyll).

Answer 140

Beta-carotene

Question 141

In the eye, vitamin A (as retinal) combines with the protein opsin to form the visual pigment rhodopsin.

Answer 141

Vision

Question 142

participates in the conversion of light energy into nerve impulses that are sent to the brain.

Answer 142

Rhodopsin

Question 143

is the process whereby immature cells change in structure and function to become specialized cells.

Answer 143

Regulating Cell Differentiation

Question 144

covers outer body surfaces as well as lining internal cavities and tubes.

Answer 144

Epithelial tissue

Question 145

Lack of vitamin A (as retinoic acid) causes such surfaces to become?

Answer 145

drier and harder than normal

Question 146

In men, vitamin A participates in?

Answer 146

sperm development

Question 147

In women, normal fetal development during pregnancy requires?

Answer 147

vitamin A

Question 148

The two most important members of the vitamin D family of molecules are?

Answer 148

vitamin D3 (cholecalciferol) and vitamin D2 (ergocalciferol)

Question 149

is produced in the skin of humans and animals by the action of sunlight (ultraviolet light) on its precursor molecule,

Answer 149

Vitamin D3

Question 150

It is produced from the plant sterol ergosterol through the action of light.

Answer 150

Vitamin D2 (ergocalciferol)

Question 151

Both the cholecalciferol and the ergocalciferol forms of vitamin D must undergo two further hydroxylation steps before the vitamin D becomes fully functional. The first step, which occurs in the liver, adds a?

Answer 151

-OH group to carbon 25

Question 152

Both the cholecalciferol and the ergocalciferol forms of vitamin D must undergo two further hydroxylation steps before the vitamin D becomes fully functional. The first step, which occurs in the liver, adds a -OH group to carbon 25. The second step, which occurs in the kidneys, adds a?

Answer 152

-OH group to carbon 1

Question 153

The rest of the body’s vitamin D supplies are made within the body (skin) with the help of?

Answer 153

sunlight

Question 154

triggers the deposition of calcium salts into the organic matrix of bones by activating the biosynthesis of calcium-binding proteins.

Answer 154

Vitamin D

Question 155

There are four forms of vitamin E:

Answer 155

alpha-, beta-, delta-, and gamma-tocopherol.

Question 156

The tocopherol form with the greatest biochemical activity is?

Answer 156

alpha-tocopherol

Question 157

is the main form of vitamin E in vitamin-E rich foods.

Answer 157

Gamma-tocopherol

Question 158

Plant oils (margarine, salad dressings, and shortenings), green and leafy vegetables, and whole-grain products are sources of?

Answer 158

vitamin E

Question 159

Only a few foods, including liver, fatty fish (such as salmon), and egg yolks, are good natural sources of?

Answer 159

vitamin D

Question 160

Foods derived from plants provide carotenoids, which serve as precursor forms of?

Answer 160

vitamin A

Question 161

The primary function of vitamin E in the body is as?

Answer 161

antioxidant

Question 162

a compound that protects other compounds from oxidation by being oxidized itself

Answer 162

antioxidant

Question 163

is particularly important in preventing the oxidation of polyunsaturated fatty acids in membrane lipids.

Answer 163

Vitamin E

Question 164

Vitamin E’s antioxidant action involves it giving up the hydrogen present on its ? group to oxygen-containing free radicals.

Answer 164

—OH

Question 165

A most important location in the human body where vitamin E exerts its antioxidant effect is the? , where exposure of cells to oxygen (and air pollutants) is greatest.

Answer 165

lungs

Question 166

cells that pass through the lungs, as well as the cells of the lung tissue itself, benefit from vitamin E’s protective effect.

Answer 166

red and white blood cells

Question 167

Infants, particularly premature infants, do not have a lot of vitamin?

Answer 167

Vitamin E

Question 168

is administered to the infant along with oxygen to give antioxidant protection.

Answer 168

vitamin E

Question 169

Vitamin E has also been found to be involved in the conversion of ? to prostaglandins.

Answer 169

arachidonic acid (20:4)

Question 170

is found in animals and humans and can be synthesized by bacteria, including those found in the human intestinal tract.

Answer 170

Vitamin K2

Question 171

are the form of vitamin K found in vitamin K supplements.

Answer 171

Menaquinones

Question 172

is essential to the blood-clotting process.

Answer 172

Vitamin K

Question 173

is sometimes given to presurgical patients to ensure adequate prothrombin levels and prevent hemorrhaging.

Answer 173

Vitamin K

Question 174

is also required for the biosynthesis of several other proteins found in the plasma, bone, and kidney.

Answer 174

Vitamin K

Question 175

In 1969, He proposed that an immunogen (a molecule that elicits an antibody response) would elicit antibodies with catalytic activity if the immunogen mimicked the transition state properties (shape, charge) of the reaction.

Answer 175

William Jencks

Question 176

They created the first catalytic antibodies

Answer 176

Richard Lerner and Peter Schultz

Question 177

is a protein designed to bind to specific molecules on the immunogen

Answer 177

antibody

Question 178

antibody is a protein designed to bind to specific molecules on the immunogen, the antibody will, in essence, serve as a?

Answer 178

fake active site

Question 179

an antibody that has catalytic ability because it was created by using a transition-state analog as an immunogen.

Answer 179

Abzyme

Question 180

an organic compound, essential in small amounts for the proper functioning of the human body that must be obtained from dietary sources because the body cannot synthesize it

Answer 180

Vitamin

Question 181

The site of tremendous biochemical activity called metabolism.

Answer 181

Living cell

Question 182

Enzymes are high molecular weight compounds made up principally of chains of amino acids linked together by

Answer 182

peptide bonds

Question 183

Enzymes catalyze reactions by weakening chemical bonds, which lowers?

Answer 183

Activation energy

Question 184

Another type of regulation of enzyme activity occurs when the same enzyme appears in different forms in different tissues.

Answer 184

Isoenzyme

Question 185

a molecule that elicits an antibody response

Answer 185

immunogen

Question 186

are considered in conjunction with enzymes

Answer 186

Vitamins

Question 187

are often required for women during pregnancy and for people recovering from certain illnesses.

Answer 187

supplemental vitamins

Question 188

manufactured in the laboratory, are identical to the vitamins found in foods.

Answer 188

synthetic vitamins

Question 189

introduces a double bond into the ring, producing L-ascorbic acid.

Answer 189

oxidase

Question 190

contain a higher concentration of vitamin C than any other organ in the body.

Answer 190

adrenal glands

Question 191

B vitamins that have more than one form of the vitamin exists.

Answer 191

niacin and vitamin B6

Question 192

must be chemically modified before they become functional within the coenzymes

Answer 192

B vitamins

Question 193

Foods derived from animals, including egg yolks and dairy products, provide? that are easily hydrolyzed to retinoids in the intestine.

Answer 193

retinyl esters

Question 194

Foods derived from plants provide?

Answer 194

carotenoids

Question 195

Four major functions of Vitamin A in a body:

Answer 195

1. Vision
2. Regulating cell differentiation
3. Maintenance of health of Epithelial tissues
4. Reproduction and Growth

Question 196

Vitamin K1, also called?

Answer 196

phylloquinone

Question 197

Vitamin K2 has several forms, called?

Answer 197

menaquinones

Question 198

has a side chain that is predominantly saturated; only one carbon-carbon double bond is present. It is a substance found in plants.

Answer 198

Vitamin K1

Question 199

This vitamin side chains have several carbon-carbon double bonds, in contrast to the one carbon-carbon double bond present in phylloquinone.

Answer 199

Vitamin K2