IPAP Class 21-2 > Block 3 Biochem > Flashcards

Block 3 Biochem Flashcards

(117 cards)

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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
What forms the ES Complex
Enzyme Substrate Complex The combination of an enzyme and a substrate provides an alternative pathway for the reaction with lower activation energy.
26
What is the EP Complex
Enzyme Product Complex Within the active site, amino acid R groups catalyze the reaction
27
Lock and Key Model
has a rigid substrate binding to a | rigid enzyme, much like a key fitting into a lock.
28
Induced-fit model,
more dynamic model of enzyme action, states that the active site is flexible enough to adapt to the shape of the substrate
29
How does the substrate enzyme relationship affect induced fit models
They work together to acquire a geometrical arrangement that lowers the activation energy
30
Where is the active site?
In a section of the enzyme
31
In the induced-fit model, what happens to the shape of the enzyme when the substrate binds?
adapts to the shape of the substrate
32
6 Main Classes of Enzymes
``` Oxidoreductase Transferase Hydrolase Lyase Isomerase Ligase ```
33
Ligase MOA
Catalyzes the joining of two substrates using ATP energy
34
Liyase MOA
Catalyze the addition or removal of a group w/o hydrolsis
35
Isomerase MOA
Catalyze the rearrangement of atoms within a substrate
36
Transferase MOA
Catalyze the transfer of a functional group between two compounds
37
Hydrolase MOA
Catalyze the hydrolysis reactions that split a compound into two products
38
Oxidoreductase MOA
Catalyze the oxidation-reduction reactions
39
What converts a cis fatty acid to a trans-fatty acid?
Isomerase
40
What removes two H atoms to form a double bond?
dehydrogenase
41
What combines two molecules to make a new compound?
Synthetase
42
What adds NH3?
Aminase
43
What three factors affect enzyme activity?
Temp pH Concentration of enzyme and substrate
44
V0 =
velocity of reaction
45
Vmax =
maximum rate achieved by the system (think saturated)
46
[S]
substrate concentration
47
Km=
Michaelis constant (1/2 of the Vmax)
48
Competitive Inhibition in relation to Michaelis menten and Vmax
Km increases; no change in Vmax
49
Non-Competitive Inhibition in relation to Michaelis menten and Vmax
No change in Km; Vmax decreases
50
Allosteric enzymes bind where?
with a regulator molecule at the allosteric site that is | different from the active site.
51
What do allosteric enzymes do to the shape of the enzyme?
change the shape of the enzyme, which causes a | change in the shape of the active site.
52
Allosteric Positive Regulator
changes the shape of the | active site to allow the substrate to bind more effectively
53
Allosteric Negative Regulator
changes the shape of the active site to prevent the proper binding of the substrate, which decreases the rate of the catalyzed reaction.
54
High concentration of end product can do what
act as a negative regulator and binds to the allosteric site
55
Covalent Modification
Enzyme activity is modified by covalent bonds to a group | on the polypeptide chain that are formed or broken.
56
Zymogen
or proenzymes, are produced in their inactive form and can be activated at a later time when they are needed
57
Zymogen mechanism
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
reversible inhibitor
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
Reversible Competitive inhibitors
compete for the active site.
60
Reversible Noncompetitive inhibitors
act on another site that is | not the active site.
61
competitive inhibitor
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
Some bacterial infections are treated with what?
antimetabolites. Ex: Sulfanilamide competes with p-aminobenzoic acid (PABA),
63
noncompetitive inhibitor characteristics? | 4
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
irreversible inhibition
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
3 examples of irreversible inhibitors
Cyanide Parathion Penicillin
66
simple enzyme
an active enzyme that consists only of protein.
67
coenzyme
a cofactor that is a small organic molecule such as a vitamin.
68
Many active enzymes | require what?
A metal ion
69
Characteristics of Vitamins
are organic molecules that are essential for normal health and growth. need to be obtained from the diet.
70
Example of an aldose polysaccharide vs. ketose (What does it look like?)
Aldose = terminal C=0-H Ketose = C=0 anywhere on the chain
71
Key characteristic of sugar
It likes to cyclize
72
3 properties of achiral carbons
mirror is identical can be superimposed 2 or more identical atoms bonded to the same atom
73
structural isomers
they have the same | molecular formula but different bonding arrangements
74
stereoisomers
bonded in the same sequence but differ in the way they are arranged in space
75
Chiral carbon mirror image=
Enantomer
76
L= D=
HO , LEFT OH, RIGHT
77
what is the most important monosaccharide and form for the body?
d-Glucose
78
what are the most stable forms of pentose or hexoses sugars?
cyclic 5 or 6 ring carbons
79
a-Isomer is ___ the ring and b-Isomer is ____ the ring
below, above
80
what is an alditol?
The reduction of the carbonyl group in monosaccharides converts an aldehyde group to alcohol producing sugar
81
Common disaccharide
Lactose
82
characteristics of lactose
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
characteristics of sucrose
Glucose + Fructose has an α,β-(1 2)-glycosidic bond between carbon 1 of glucose and carbon 2 of fructose.
84
what are the two polysaccharides that make up starch
amylose and | amylopectin.
85
amylose makes up ___ % of starch and amylopectin ___%
20, 80
86
Amylose
α-D-glucose molecules connected by α-(1 4)-glycosidic bonds in a continuous chain longer chains are coiled in helical fashion
87
Amylopectin
contains glucose molecules connected by α-(1 -4)-and α-(1-6)-glycosidic bonds.
88
how do humans break β-(1 4)-glycosidic bonds?
They dont.
89
Difference between nucleotide and nucleoside
Side -Base + deoxyribose or ribose Tide -Base + deoxyr. or ribose + phosphate
90
Name the corresponding DNA nucleotide for the nucleoside of (A,G,C,T).
A- Deoxyadenosine Monophosphate (dAMP) G- Deoxyguaninosine Monophosphate (dGMP) C- Deoxycytodine Monophosphate(dCMP) T-Deoxythymodine Monophosphate(dTMP)
91
Most abundant RNA type
rRNA
92
What is the nucleotide sequence connecting the tRNA Anticodon to the mRNA?
ACC at the 3' end
93
When tRNA binds mRNA what type of bond is formed?
ester bond wiht the free -OH group
94
Difference between exons and introns
exons posses DNA code, introns do not and are removed before mature mRNA is produced.
95
How many stop codons , how many start codons
3-stop, 1 -start
96
How does viral RNA infiltrate DNA
Reverse Transcriptase --retrovirus
97
Central carbon of an amino acid
alpha carbon
98
Parts of an amino acid
Ammoniom Group R Group Carboxylate Group
99
An amino acid is non polar when ______________
the R group is H, Alkyl, or aromatic
100
An amino acid is polar when the R group is ______
Alcohol, thiol, or amide
101
Polar acidic amino acid r group
COO-
102
Polar basic amino acid r group is ?
Ammonium group
103
what forms a peptide bond ?
when the COO- group forms an amide with NH3+
104
First Polypeptide to have its primary structure determined, two polypeptide chains linked by disulfide bonds.
insulin
105
polypeptide chains held side by side by H bonds
β-pleated sheet
106
corkscrew shape with H bonds between amino acids
a-Helix
107
three peptide chains woven like a rope
triple helix
108
Hydrophobic interactions
2 internal non polar r groups form a nonpolar center at the interior of the protein
109
Hydrophilic interactions
2 external aqeuos R groups are pulled to the outer surface of most proteins
110
Salt bridges
ionic attractions between ionized | R groups of polar basic and polar acidic amino acids
111
Disulfide bonds
are covalent bonds that form between the —SH groups of cysteine residues in a polypeptide chain
112
how many o2 molecules does hemoglobin carry vs. myoglobin
4 vs. 1
113
What happens in hydrolysis reactions
Peptides are broken by H20
114
How does denaturing affect the amide bonds of amino acids?
IT doesnt
115
Two things that happen when residues are interrupted
Globular protein unfolds Protein is no longer biologically active
116
At what temp. are proteins denatured
above 50 degrees.
117
How does changing the pH affect protein denaturing?
Breaks H bonds Disrupts ionic and salt bridges
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