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Anatomy and Physiology 1 > Macromolecules (exam 2) > Flashcards

Macromolecules (exam 2) Flashcards

1
Q

functions of carbohydrates

A
  1. energy
  2. storage
  3. structure (matrix of connective tissue in our joints)
  4. cell recognition/communication: (AB blood type, this protein has a carbohydrate chain which is what distinguishes it from other types)
  5. modifies proteins affecting…. (glycosylating something can affect how it folds, how long it lasts…)
    - structure/folding
    - enzyme kinetics: Vmax and Km
    - Turnover/degradation: turnover can be faster or slower depending on the carbohydrate chain
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2
Q

alpha 1-4 glycosidic bond

A
  • more common

- easily broken down for energy and modified for storage

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3
Q

examples of alpha 1-3 glycosidic bonds

A
  • sucrose

- starch

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4
Q

what kinds of bonds does glycogen have?

A
  • both alpha 1-4 and alpha 1-6 glycosidic bonds

- this gives glycogen its characteristic branched structure

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5
Q

glycogen

A

the primary carbohydrate storage molecule

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6
Q

what kinds of bonds does lactose have?

A

Beta 1-4 glycosidic bond

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7
Q

how are common alpha glycosidic bonds processed?

A

they’re hydrolyzed by amylase

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8
Q

What does lactose require?

A
  • the beta bond of lactose requires lactase
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9
Q

where is lactase only produced?

A

in the cells of mucosa of the small intestine

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10
Q

when does lactose intolerance occur?

A

when the body stops producing lactase

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11
Q

Lactose intolerance can be ______ or ______

A

temporary

genetic/developmental

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12
Q

_____ is a common filler in pharmaceuticals

A

lactose

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13
Q

where is amylase produced?

A

pancreas

saliva

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14
Q

how are sugar alcohols formed?

A

by the reduction of the carbonyl group

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15
Q

when do sugar alcohols occur?

A

polyol pathway

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16
Q

Sorbitol function

A
  • sugar alcohol
  • used for storage
  • can be metabolized forward to fructose
  • can be metabolized back to glucose
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17
Q

Sorbitol is an _____

A

effective osmole

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18
Q

Inositol function

A
  • signaling
  • myelin attachment
  • nerve function
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19
Q

what are the forms of cyclic carbohydrates?

A

alpha or beta isomers

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20
Q

how is glucose transported into cells?

A

by either

  1. insulin dependent transporters
  2. insulin independent transporters
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21
Q

importance of insulin independent transporter proteins?

A

they maintain the basal level of glucose required for cell survival

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22
Q

what happens to excess glucose?

A

it enters the polyol pathway

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23
Q

where can you find a high percentage of insulin-independent transporters?

A
  • kidney
  • retinal
  • nerve tissue (retina)
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24
Q

where can you find insulin dependent transporters?

A
  • liver
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25
Q

what is the liver efficient in doing?

A
  • handling high levels of blood sugar and bringing it back down
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26
Q

insulin independent transporters

A
  • no inhibition

- doesn’t bind insulin

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27
Q

insulin dependent transporters?

A
  • limited inhibition
  • binds insulin (limited)
  • shoots up and down according to blood sugar levels
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28
Q

how are acidic sugars formed?

A

by the oxidation of the 6’ OH group or the 1’ carbonyl group to a carboxyl group

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29
Q

where does formation of acidic sugars occur?

A
  • in many tissues

- highest in the liver, kidney, and RBC

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30
Q

what does the liver use acidic sugar formatio for?

A

for conjugation (to change solubility)

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31
Q

example of an acidic sugar

A

Glucuronic acid

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32
Q

Functions of Glucuronic acid

A
  • used as a detoxifying agent
  • conjugates with molecules to increase solubility, transport, or excretion
  • makes it easier to get rid of toxins and waste
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33
Q

dietetic candy

A

uses sorbitol as a sweetener. goes right through the digestive system

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34
Q

Bilirubin

A

byproduct of RBCs being broken down

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35
Q

how are amino sugars formed?

A

by the replacement of an OH group with an NH2

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36
Q

examples of amino sugars and their functions

A

glucosamine and galactosamine

- compose the matrix in connective tissue

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37
Q

what increases the structural nature of amino sugars?

A

beta bonds between alternating amino sugars

*other organisms do this in beta bonds but humans always use alpha bonds

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38
Q

hyaluronic acid

A
  • weakest crosslinking, much more fluid

- proper

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39
Q

Chondroitin sulfate

A
  • cartilage

- supplements for joint health because it’s the building block for the matrix of cartilage

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40
Q

matrix for connective tissue

A
  • where the cells live in fluid, gel or a solid environment

- cells secrete/make the matrix

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41
Q

purposes of glycosylation

A
  1. modify/regulate protein function (change their Vmax and Km with their enzymes)
  2. stabilization of proteins in the serum (antibody Fc fragment)
  3. may aid in initial protein folding
  4. aids in cell recognition and binding to membrane proteins (type A, B, O blood type)
  5. increases hydration of molecules (mucus has a lot of carbohydrate moieties in it)
  6. involved in stabilizing structure like connective tissue
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42
Q

how do you do fatty acid nomeclature

A

of carbons: # of double bonds + the position of the double bond

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43
Q

eicosanoids

A
  • diverse group of hormones and signaling molecules
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44
Q

how are eicosanoids produced

A

by the oxidation of fatty acids-particularly arachidonic and similar molecules

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45
Q

what are the primary enzymes involved in eicosanoid synthesis?

A
  • cyclooxygenase (COX)

- lipoxygenases (LOX)

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46
Q

what does COX produce

A

prostaglandins and thromboxanes (prostanoids)

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47
Q

what does LOX produce

A

leukotrienes and lipoxins

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48
Q

what does the COX pathway result in

A

molecules with a cyclical structure

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49
Q

Prostanoids

A
  • locally active hormones/signals which are rapidly degraded
  • type of eicosanoids
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50
Q

what do prostanoids often exhibit

A
  • opposing functions which are kept in balance during homeostasis and can change/be induced during pathological conditions
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51
Q

functions of prostanoids

A
  • inflammation mediation
  • cardiovascular homeostasis
  • reproductive function
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52
Q

what does the LOX pathway produce

A
  • complex molecules without a cyclic component
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53
Q

Acylglycerol/glycerides

A
  • ester of glycerol and fatty acids that occurs naturally as fats and fatty oils
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54
Q

how do phospholipids start out?

A
  • as diacylglycerol with a phosphate group covalently bonded to the third site of the glycerol molecule
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55
Q

how are phospholipids formed

A
  • presence of phosphate group changes the diacylglycerol to phosphatidic acid (same thing as phospholipid)
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56
Q

functions of phospholipids

A
  1. membrane structure (phospholipid bilayer)
  2. signaling
  3. fatty reservoir for hormone production (COX pathway)
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57
Q

fatty acid chains

A

diacylglycerol

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58
Q

Phosphatidylcholine

A
  • component of HDLs
  • increases fluidity
  • yields fatty acids for signaling
  • (example of phospholipid modification)
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59
Q

Phosphatidylinositol

A
  • high concentration in nerve cells
  • cell attachment/organization
  • signaling, PIP2
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60
Q

where is cholesterol

A

embeds in the hydrophobic region

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61
Q

function of cholesterol

A
  • stabilizes the transition state (fluidity)
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62
Q

Steroidogenic pathway

A
  1. cholesterol entering the mitochondria and undergoing conversion to pregnenolone
  2. then can turn into other things
63
Q

once cholesterol turns into pregnenolone, what happens?

A

can be converted into

  • mineralocorticoids
  • glucocorticoids
  • estrogens/androgens
64
Q

can steroids enter any cell?

A

yes

65
Q

what happens if a receptor is present when the steroid enters the cell

A

the complex becomes a transcription factor

66
Q

what happens if when the steroid enters the cell, there’s no receptor?

A
  • steroid broken down
67
Q

what happens if there’s an excess of steroid

A

stored in the membrane

68
Q

what happens when there’s increased sterols in the membrane

A
  • increased membrane rigidity
  • makes membrane less fluid (can’t transport things)
  • decreases cell reactivity
69
Q

bile salts

  • function
  • where is it produced
A

liver produces bile salts to aid in the emulsification of fat in the small intestine

70
Q

how are bile salts formed

A

bile acids interact with Na+

71
Q

what are fat soluble vitamins based on?

A

cholesterol

72
Q

list the fat soluble vitamins

A

A, D, E, and K

73
Q

Fat soluble vitamins

A
  • essential nutrients with either the vitamin or the precursor needing to come from a dietary source
74
Q

functions of proteins

A
  1. structure
  2. hormones/signaling
  3. NTs
  4. blood clotting
  5. viscosity
  6. antibodies
  7. transport
  8. enzymes
75
Q

hi

A

hi

76
Q

what is the point of variation between AAs

A

R group

77
Q

how is the rate of reaction impacted:

unlimited substrate

A

increases

78
Q

how is the rate of reaction impacted:

pH

A

affects charge and reactivity of active site, best rate at optimal pH

79
Q

how is the rate of reaction impacted: temperature

A

rate increases until denaturation occurs

80
Q

the reaction continues until _______

A

all the enzyme is in the enzyme-substrate complex

81
Q

Vmax is the

A

point of saturation

82
Q

holoenzyme (functional)

A

apoenzyme + prosthetic group

83
Q

cofactors

A
  • inorganic
  • usually metal ions
  • Mg2+, Fe2+. Zn2+
  • required by certain enzymes
84
Q

example of a cofactor

A
  • ATPases require a Mg2+ cofactor to put stress on the high energy bonds
85
Q

Coenzymes

A
  • organic molecules

- such as vitamins and carrier molecules

86
Q

example of a coenzyme

A
  • the complex, pyruvate dehydrogenase requires thiamine (B1) to act as an electron sink for the carboxylation of pyruvate
87
Q

prosthetic group

A

A tightly bound, specific non-polypeptide unit required for the biological function of some proteins.

88
Q

apoenzyme

A

the protein part of an enzyme

89
Q

holoenzyme

A
  • an active enzyme and can perform the catalytic activity.
90
Q

why are apoenzymes important

A

they are responsible for the specificity of enzymes to their substrates

91
Q

are apoenzymes active? why or why not?

A

Apoenzymes alone are not active enzymes; they must bind to an organic or inorganic cofactor in order to be activated

92
Q

how are holoenzymes made

A
  • After binding to a cofactor, apoenzyme forms a holoenzyme
93
Q

competitive inhibitors

A
  • resemble the substrate and bind to the active site
94
Q

noncompetitive inhibitors

A
  • bind to an allosteric site

- alter the shape of or access to the active site

95
Q

is inhibition reversible?

A

yes inhibition can be reversible or irreversible

96
Q

reversible inhibition

A

the enzyme remains functional after removal of the inhibitor

97
Q

irreversible inhibition

A

the inhibitor permanently alters the enzyme leaving it nonfunctional

98
Q

explain substrate level inhibition

A
  • can occur when an enzyme has 2 binding sites, active and allosteric, for the substrate
  • these 2 sites would have different Km values, with the allosteric binding occurring as [S] increases
99
Q

what does binding at the allosteric site do?

A

decreases the binding/conversion at the active site

100
Q

what does a different kM mean??

A

different affinities

101
Q

Vmax

A

maximum turnover rate for enzyme

102
Q

what catalyzes the first step in the detoxification of alcohol

A

alcohol dehydrogenase

103
Q

what’s an example of toxin mitigation

A

detoxification of alcohol

104
Q

explain the steps of detoxification of alcohol

A
  1. alcohol
  2. acetaldehyde by alcohol dehydrogenase
  3. acetate
105
Q

acetaldehyde

A
  • highly toxic molecule exerting negative effects on the liver and CNS, and complex effects on the cardiovascular system
106
Q

how does toxin mitigation of alcohol work?

A
  • by slowing the conversion to the intermediate, the most negative effects can be somewhat mitigated
107
Q

product level inhibition

A
  • product binds a allosteric site on the enzyme to slow reaction
108
Q

what is product level inhibition involved in? explain how

A

metabolic regulation

- the product inhibition ensures that glucose will not be dedicated to ATP production unless the cell is utilizing it

109
Q

metabolic regulation

A

physiological mechanism by which the body takes in nutrients and delivers energy as required

110
Q

list 2 examples of product level inhibition

A
  1. hexokinase

2. many Krebs cycle enzyme

111
Q

what do the Km and Vmax tell us?

A

basic information about the enzyme’s function

112
Q

what does Km refer to?

A
  • affinity of enzyme for substrate

- the [S] at 1/2 Vmax

113
Q

what does lower Km mean?

A

higher affinity

114
Q

what does higher km mean?

A

lower affinity

115
Q

what does Vmax give you insight on?

A

the capacity of the [E] to handle fluctuations in [Substrate[

116
Q

what is this: when all the enzyme is in the ES complex

A

Vmax

117
Q

isoenzymes

A
  • catalyze the same reaction but due to minor structural changes, have different activity levels
118
Q

where are hexokinases found?

A
  • in most tissues

- considered the maintenance enzyme

119
Q

where is glucokinase primarily found

A

in the liver

120
Q

glucokinase is technically a…

A

very specific form of hexokinase

121
Q

medical application of isoenzymes

A
  • because they’re tissue specific, their presece in the blood is indicative of damage to a specific tissue type
  • CREATINE PHOSPHOKINASE (CPK, CK)
122
Q

CPK1

A

brain and lugns

123
Q

CPK2

A

heart

124
Q

CPK3

A

skeletal muscle

125
Q

functions of nucleic acids

A
  1. genetic information
  2. direct protein synthesis
  3. energy
  4. NTs
126
Q

what are nucleic acids made up of?

A

nucleotide monomers

127
Q

2 examples of nucleic acids

A

DNA and RNA

128
Q

what is the monomer of DNA

A

AMP

129
Q

what are the basic components of a nucleotide

A

nitrogenous base
ribose sugar
phosphate group

130
Q

list the pyridimines

A

cytosine
uracil (RNA)
thymine (DNA)

131
Q

list the purines

A

Guanine

Adenosine

132
Q

which is larger: purines or pyrimidines

A

purines

133
Q

in nucleotides: where is the phosphate group bonded to?

A

the 5’ carbon of a sugar

134
Q

in nucleotides: where is the nitrogenous base bonded to?

A

1’ carbon of sugar

135
Q

list the nitrogenous bases

A 
cytosine
uracil
thymine
guaine
adenine
136
Q

composition of nucleotide

A

phosphate group, 5 carbon sugar, nitrogenous base

137
Q

Ribose

A
  • sugar for RNA

- 5-carbon simple sugar

138
Q

Deoxyribose

A
  • sugar for DNA

- has the same 5-carbon formula as that of ribose sugar but loses an oxygen atom

139
Q

_______ reaction forms DNA

A

Condensation

140
Q

how is DNA made?

A

nucleotides bind so that the 3’ OH group of one attaches to the 5’ phosphate of the other

141
Q

In a DNA chain, the polymer will only attach new monomers….

A

to the 3’ end

142
Q

list the DNA forms

A

B DNA
A DNA
Z DNA

143
Q

B DNA

A
  • most common

- right handed helix

144
Q

A DNA

A
  • shorter
  • more dense
  • right handed helix
  • RNA DNA complexes
  • double stranded RNA regions
145
Q

Z DNA

A
  • longer
  • stretched out
  • left handed helix
  • increased methylation
  • shut down
146
Q

list the ribonucleic acid forms

A 
mRNA
rRNA
tRNA
hnRNA
sRNA
147
Q

mRNA

A

coded message that directs peptide synthesis

148
Q

rRNA

A

stabilizes mRNA in the ribosome

149
Q

tRNA

A

transfers AA to ribosome for peptide construction

150
Q

hnRNA

A
  • heterogenous nuclear RNA
  • unedited RNA
  • contains introns that have to be removed
151
Q

snRNA

A
  • small nuclear RNA

- forms complexes with proteins forming snRNPs

152
Q

snRNPs

A

perform splicing of hnRNAs to produce mRNAs

153
Q

energy molecules

A

contain high energy bonds

- nucleic acid modification

154
Q

NT

A
  • adenosine is simply the nucleoside w/o the phosphate group
  • nucleic acid modification

Anatomy and Physiology 1 (4 decks)

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