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IPAP Class 21-2 > Block 3 Biochem > Flashcards

Block 3 Biochem Flashcards

1
Q

Water-soluble vitamins Characteristics

A

must come from our food each day;
cannot be stored in the body.
cofactors for many enzymes.
excreted in urine each day.

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2
Q

Many water-soluble vitamins are precursors required for what?

A

to carry out certain aspects of catalytic action

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3
Q

Thiamine (alternate name) and characteristics

A

B1

Thiamine, associated with coenzyme thiamine pyrophosphate (TPP),

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4
Q

Riboflavin, (alternate name) and characteristics

A

B2
Riboflavin, associated with coenzymes flavin adenine dinucleotide (FAD) and flavin mononucleotide (FMN),

can turn urine a bright yellow when excreted!!

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5
Q

Niacin, (alternate name) and characteristics

A

B3

Niacin, associated with coenzymes nicotinamide adenine dinucleotide (NAD2+) and nicotinamide adenine dinucleotide phosphate (NADP2+),

can cause a “niacin flush”

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6
Q

Pantothenic Acid, (alternate name) and characteristics

A

B5

Pantothenic acid, associated with coenzyme A,

is necessary to avoid fatigue, retarded growth, muscle cramps, and
anemia.

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7
Q

Pyridoxine, (alternate name) and characteristics

A

B6

Pyridoxine, associated with pyridoxal phosphate (PLP),

is necessary to avoid dermatitis, fatigue, anemia, and retarded growth.

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8
Q

Folic Acid, (alternate name) and characteristics

A

B9

Folic acid, associated with tetrahydrofolate (THF),

is necessary to avoid abnormal red blood cells, anemia, intestinal tract
disturbances, loss of hair, growth impairment, and depression.

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9
Q

Cobalamin, (alternate name) and characteristics

A

B12

Cobalamin (cyanocobalamin), associated with methylcobalamin,

is necessary to avoid pernicious anemia, malformed red blood
cells, and nerve damage.

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10
Q

Ascorbic Acid, (alternate name) and characteristics

A

C
is necessary to avoid scurvy: bleeding gums, weakened connective
tissues, slow-healing wounds, and anemia.

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11
Q

Biotin, (alternate name) and characteristics

A

H/B7

associated with biocytin,

is necessary to avoid dermatitis, loss of hair, fatigue,
anemia, and depression.

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12
Q

What are the Fat-Soluble Vitamins?

A

include A, D, E, and K and are not involved as

coenzymes in catalytic reactions.

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13
Q

Characteristics of Fat-Soluble Vitamins (3)

A

are soluble in lipids but not in aqueous solutions.

are stored in the body and not eliminated in urine.

are important in vision, bone formation, antioxidants, and blood clotting.

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14
Q

Retinol, (alternate name) and characteristics

A

Vitamin A,

an antioxidant,
is needed for retinol (vision) and synthesis of RNA.

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15
Q

Cholecalciferol, (alternate name) and characteristics

A

Vitamin D

regulates the absorption of phosphorus and calcium
during bone growth.

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16
Q

Tocopherol, (alternate name) and characteristics

A

Vitamin E

is an antioxidant in cells.

is found in whole grains and vegetables.

is necessary to avoid hemolysis and anemia.

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17
Q

Menaquinone, (alternate name) and characteristics

A

Vitamin K

is needed for the synthesis of zymogens for blood
clotting.

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18
Q

Characteristics of Enzymes

A

biological catalysts,

increase the rate of a reaction

are not changed in the process
of the reaction.

lower the activation energy of the reaction.

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19
Q

Definition of Substrate

A

globular proteins with a unique three-dimensional shape that recognizes and binds a small group of reacting molecules

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20
Q

Explain the Active Site

A

tertiary structure

where one or more small groups of substrates bind to create a chemical reaction

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21
Q

3 Types of Specificity

A

Absolute, Group, Linkage

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22
Q

Absolute Specificity

A

Catalyze only one type of reaction for only one substrate

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23
Q

Group Specificity

A

Catalyze one type of reaction for similar substrates

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24
Q

Linkage Specificity

A

Catalyze one type of reaction for a specific type of bond

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25
Q

What forms the ES Complex

A

Enzyme Substrate Complex

The combination of an enzyme and a substrate

provides an alternative pathway for the reaction with
lower activation energy.

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26
Q

What is the EP Complex

A

Enzyme Product Complex

Within the active site, amino acid R groups catalyze the reaction

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27
Q

Lock and Key Model

A

has a rigid substrate binding to a

rigid enzyme, much like a key fitting into a lock.

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28
Q

Induced-fit model,

A

more dynamic model of enzyme action, states that the active site is flexible enough to adapt to the shape of the substrate

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29
Q

How does the substrate enzyme relationship affect induced fit models

A

They work together to acquire a geometrical arrangement that lowers the activation energy

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30
Q

Where is the active site?

A

In a section of the enzyme

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31
Q

In the induced-fit model, what happens to the shape of the enzyme when the substrate binds?

A

adapts to the shape of the substrate

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32
Q

6 Main Classes of Enzymes

A 
Oxidoreductase 
Transferase 
Hydrolase
Lyase 
Isomerase 
Ligase
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33
Q

Ligase MOA

A

Catalyzes the joining of two substrates using ATP energy

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34
Q

Liyase MOA

A

Catalyze the addition or removal of a group w/o hydrolsis

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35
Q

Isomerase MOA

A

Catalyze the rearrangement of atoms within a substrate

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36
Q

Transferase MOA

A

Catalyze the transfer of a functional group between two compounds

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37
Q

Hydrolase MOA

A

Catalyze the hydrolysis reactions that split a compound into two products

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38
Q

Oxidoreductase MOA

A

Catalyze the oxidation-reduction reactions

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39
Q

What converts a cis fatty acid to a trans-fatty acid?

A

Isomerase

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40
Q

What removes two H atoms to form a double bond?

A

dehydrogenase

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41
Q

What combines two molecules to make a new compound?

A

Synthetase

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42
Q

What adds NH3?

A

Aminase

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43
Q

What three factors affect enzyme activity?

A

Temp
pH
Concentration of enzyme and substrate

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44
Q

V0 =

A

velocity of reaction

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45
Q

Vmax =

A

maximum rate achieved by the system (think saturated)

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46
Q

[S]

A

substrate concentration

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47
Q

Km=

A

Michaelis constant (1/2 of the Vmax)

48
Q

Competitive Inhibition in relation to Michaelis menten and Vmax

A

Km increases; no change in Vmax

49
Q

Non-Competitive Inhibition in relation to Michaelis menten and Vmax

A

No change in Km; Vmax decreases

50
Q

Allosteric enzymes bind where?

A

with a regulator molecule at the allosteric site that is

different from the active site.

51
Q

What do allosteric enzymes do to the shape of the enzyme?

A

change the shape of the enzyme, which causes a

change in the shape of the active site.

52
Q

Allosteric Positive Regulator

A

changes the shape of the

active site to allow the substrate to bind more effectively

53
Q

Allosteric Negative Regulator

A

changes the shape of the active site to prevent the proper binding of the substrate, which decreases the rate of the catalyzed reaction.

54
Q

High concentration of end product can do what

A

act as a negative regulator and binds to the allosteric site

55
Q

Covalent Modification

A

Enzyme activity is modified by covalent bonds to a group

on the polypeptide chain that are formed or broken.

56
Q

Zymogen

A

or proenzymes, are produced in their inactive form and can be activated at a later time when they are needed

57
Q

Zymogen mechanism

A

Once a zymogen is formed, it is
transported to where the active form is needed.
converted to its active form by a covalent modification.

58
Q

reversible inhibitor

A

cause a loss of enzyme activity that can be restored.

can act in different ways but do not form covalent bonds
with the enzyme.

59
Q

Reversible Competitive inhibitors

A

compete for the active site.

60
Q

Reversible Noncompetitive inhibitors

A

act on another site that is

not the active site.

61
Q

competitive inhibitor

A

has a chemical structure and polarity similar to the substrate.
competes with the substrate for the active site.
has its effect reversed by increasing substrate concentration.

62
Q

Some bacterial infections are treated with what?

A

antimetabolites.

Ex: Sulfanilamide competes with
p-aminobenzoic acid (PABA),

63
Q

noncompetitive inhibitor characteristics?

4

A

has a structure that is much different from that of the substrate.

does not compete for the active site.

distorts the shape of the enzyme, which prevents the catalyzing of the substrate at the active site.

cannot have its effect reversed by adding more substrate.

64
Q

irreversible inhibition

A

enzyme activity is destroyed when
the inhibitor covalently bonds with R groups of an amino acid that
may be near the active site

the inhibitor changes the shape of the enzyme, which prevents the
substrate from entering the active site.

65
Q

3 examples of irreversible inhibitors

A

Cyanide
Parathion
Penicillin

66
Q

simple enzyme

A

an active enzyme that consists only of protein.

67
Q

coenzyme

A

a cofactor that is a small organic molecule such as a vitamin.

68
Q

Many active enzymes

require what?

A

A metal ion

69
Q

Characteristics of Vitamins

A

are organic molecules that are essential for normal health and growth.
need to be obtained from the diet.

70
Q

Example of an aldose polysaccharide vs. ketose (What does it look like?)

A

Aldose = terminal C=0-H

Ketose = C=0 anywhere on the chain

71
Q

Key characteristic of sugar

A

It likes to cyclize

72
Q

3 properties of achiral carbons

A

mirror is identical

can be superimposed

2 or more identical atoms bonded to the same atom

73
Q

structural isomers

A

they have the same

molecular formula but different bonding arrangements

74
Q

stereoisomers

A

bonded in the same sequence but differ in the way they are arranged in space

75
Q

Chiral carbon mirror image=

A

Enantomer

76
Q

L=

D=

A

HO , LEFT

OH, RIGHT

77
Q

what is the most important monosaccharide and form for the body?

A

d-Glucose

78
Q

what are the most stable forms of pentose or hexoses sugars?

A

cyclic 5 or 6 ring carbons

79
Q

a-Isomer is ___ the ring and b-Isomer is ____ the ring

A

below, above

80
Q

what is an alditol?

A

The reduction of the carbonyl group in monosaccharides

converts an aldehyde group to alcohol producing sugar

81
Q

Common disaccharide

A

Lactose

82
Q

characteristics of lactose

A

Glucose + Galactose

β-(1 4)-glycosidic bond because
the —OH group on carbon 1 of β-D-galactose forms a glycosidic bond with the —OH group on
carbon 4 of a D-glucose molecule

83
Q

characteristics of sucrose

A

Glucose + Fructose

has an α,β-(1 2)-glycosidic bond between carbon 1 of glucose and carbon 2 of fructose.

84
Q

what are the two polysaccharides that make up starch

A

amylose and

amylopectin.

85
Q

amylose makes up ___ % of starch and amylopectin ___%

A

20, 80

86
Q

Amylose

A

α-D-glucose molecules connected by α-(1 4)-glycosidic bonds in a continuous chain

longer chains are coiled in helical fashion

87
Q

Amylopectin

A

contains glucose molecules connected by α-(1 -4)-and α-(1-6)-glycosidic bonds.

88
Q

how do humans break β-(1 4)-glycosidic bonds?

A

They dont.

89
Q

Difference between nucleotide and nucleoside

A

Side
-Base + deoxyribose or ribose
Tide
-Base + deoxyr. or ribose + phosphate

90
Q

Name the corresponding DNA nucleotide for the nucleoside of (A,G,C,T).

A

A- Deoxyadenosine Monophosphate (dAMP)

G- Deoxyguaninosine Monophosphate (dGMP)

C- Deoxycytodine Monophosphate(dCMP)

T-Deoxythymodine Monophosphate(dTMP)

91
Q

Most abundant RNA type

A

rRNA

92
Q

What is the nucleotide sequence connecting the tRNA Anticodon to the mRNA?

A

ACC at the 3’ end

93
Q

When tRNA binds mRNA what type of bond is formed?

A

ester bond wiht the free -OH group

94
Q

Difference between exons and introns

A

exons posses DNA code, introns do not and are removed before mature mRNA is produced.

95
Q

How many stop codons , how many start codons

A

3-stop, 1 -start

96
Q

How does viral RNA infiltrate DNA

A

Reverse Transcriptase –retrovirus

97
Q

Central carbon of an amino acid

A

alpha carbon

98
Q

Parts of an amino acid

A

Ammoniom Group
R Group
Carboxylate Group

99
Q

An amino acid is non polar when ______________

A

the R group is H, Alkyl, or aromatic

100
Q

An amino acid is polar when the R group is ______

A

Alcohol, thiol, or amide

101
Q

Polar acidic amino acid r group

A

COO-

102
Q

Polar basic amino acid r group is ?

A

Ammonium group

103
Q

what forms a peptide bond ?

A

when the COO- group forms an amide with NH3+

104
Q

First Polypeptide to have its primary structure determined, two polypeptide chains linked by disulfide bonds.

A

insulin

105
Q

polypeptide chains held side by side by H bonds

A

β-pleated sheet

106
Q

corkscrew shape with H bonds between amino acids

A

a-Helix

107
Q

three peptide chains woven like a rope

A

triple helix

108
Q

Hydrophobic interactions

A

2 internal non polar r groups form a nonpolar center at the interior of the protein

109
Q

Hydrophilic interactions

A

2 external aqeuos R groups are pulled to the outer surface of most proteins

110
Q

Salt bridges

A

ionic attractions between ionized

R groups of polar basic and polar acidic amino acids

111
Q

Disulfide bonds

A

are covalent bonds that form between the —SH groups of cysteine residues in a polypeptide chain

112
Q

how many o2 molecules does hemoglobin carry vs. myoglobin

A

4 vs. 1

113
Q

What happens in hydrolysis reactions

A

Peptides are broken by H20

114
Q

How does denaturing affect the amide bonds of amino acids?

A

IT doesnt

115
Q

Two things that happen when residues are interrupted

A

Globular protein unfolds

Protein is no longer biologically active

116
Q

At what temp. are proteins denatured

A

above 50 degrees.

117
Q

How does changing the pH affect protein denaturing?

A

Breaks H bonds

Disrupts ionic and salt bridges

IPAP Class 21-2 (12 decks)

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