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S. One > Biochemistry > Flashcards

Biochemistry Flashcards

1
Q

What is the most common intracellular buffer?

A

Protein

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2
Q

What is the most common extracellular buffer?

A

Bicarbonate

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3
Q

What is a zwitterion?

A

A molecule with one negative and one positive end

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4
Q

What is the isoelectric point?

A

The pH at which there is no net charge

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5
Q

What is the rate limiting enzyme in glycolysis?

A

PFK-1

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6
Q

What is the rate limiting enzyme in gluconeogenesis?

A

Pyruvate carboxylase

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7
Q

What is the rate limiting enzyme in the HMP shunt?

A

G-6PD

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8
Q

What is the rate limiting enzyme in glycogenesis?

A

Glycogen synthase

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9
Q

What is the rate limiting enzyme in glycogenolysis?

A

Glycogen phosphorylase

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10
Q

What is the rate limiting enzyme in fatty acid synthesis?

A

AcCoA carboxylase

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11
Q

What is the rate limiting enzyme in beta oxidation?

A

CAT-1

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12
Q

What is the rate limiting enzyme in cholesterol synthesis?

A

HMG CoA reductase

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13
Q

What is the rate limiting enzyme in ketogenosis?

A

HMG CoA synthase

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14
Q

What is the rate limiting enzyme in purine synthesis?

A

PRPP synthase

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15
Q

What is the rate limiting enzyme in pyrimidine synthesis?

A

Aspartate transcarbamoylase

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16
Q

What is the rate limiting enzyme in the TCA cycle?

A

Isocitrate dehydrogenase

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17
Q

What is the rate limiting enzyme in the urea cycle?

A

CPS-1

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18
Q

What is the rate limiting enzyme in heme synthesis?

A

Delta-ALA synthase

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19
Q

What are the catabolic pathways that create energy?

A

ABC
Acetyl CoA production
Beta-oxidation
Citric acid cycle

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20
Q

What are the anabolic pathways that store energy?

A 
EFGH
ER
Fatty acid synthesis 
Glycolysis 
HMP shunt
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21
Q

What are the anabolic and catabolic pathways?

A

HUG
Heme synthesis
Urea cycle
Gluconeogenesis

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22
Q

Isomerase

A

Creates an isomer

Glucose fructose

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23
Q

Epimerase

A

Creates an epimer

Glucose galactose

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24
Q

Mutase

A

Moves side chain from one carbon to another carbon

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25
Q

Transferase

A

Moves side chain from one substrate to another

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26
Q

Transaminase

A

Moves amino group

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27
Q

Kinase

A

Phosphorylates using ATP

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28
Q

Phosphorylase

A

Phosphorylates using Pi

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29
Q

Carboxylase

A

Forms C-C bonds using CO2, ATP, and biotin

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30
Q

Synthase

A

Stacks substrates, does not use ATP

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31
Q

Synthetase

A

Stacks substrates, uses ATP

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32
Q

Phosphatase

A

Breaks phosphate bond

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33
Q

Hydrolase

A

Breaks a bond with water

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34
Q

Lyase

A

Cuts C-C bond with ATP

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35
Q

Dehydrogenase

A

Removes H with a cofactor (NADH, FADH2)

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36
Q

Thio-

A

Breaks sulfur bonds

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37
Q

Diffusion

A

From high to low concentration

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38
Q

Active transport

A

Goes against concentration gradient

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39
Q

Zero-order kinetics

A

Metabolism independent of concentration

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40
Q

First-order kinetics

A

Constant drug percentage metabolism over time, depends on concentration

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41
Q

Efficacy

A

Max effect regardless of dose

Lower with non-competitive antagonist

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42
Q

What affects efficacy?

A

Vmax

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43
Q

Potency

A

Amount of drug needed to produce effect

Lower with competitive antagonist

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44
Q

What affects potency?

A

Km

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45
Q

Km

A

Concentration of drug that binds 50% of receptors

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46
Q

EC50

A

Concentration of drug that produces 50% of maximal response

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47
Q

Competitive inhibition

A

Fights for active site
No change in Vmax
Decreases potency

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48
Q

Non-competitive inhibition

A

Binds regulatory site
No change in Km
Decreases Vmax
Decreases efficacy

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49
Q

Endothermic reaction

A

Consumes heat

Feels cold

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50
Q

Exothermic reaction

A

Gives off heat

Feels warm

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51
Q

Peak level

A

4 hours after dose

Too high —> decreases dose

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52
Q

Trough level

A

2 hours before dose
Too high —> give less often

(Unless q6 hour drug, then 1 hour before dose)

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53
Q

t1/2

A

Half-life

Time it takes for the body to use half of the drug ingested

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54
Q

von Gierke

A

G-6Pase deficiency
Hypoglycemia
Hepatosplenomegaly

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55
Q

Pompe’s

A

Cardiac alpha-1,4-glucosidase deficiency

DIE early

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56
Q

Cori’s

A

Debranching enzyme deficiency

SHORT branches of glycogen

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57
Q

Anderson’s

A

Branching enzyme deficiency

LONG chains of glycogen

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58
Q

McArdle’s

A

Muscle phosphorylase deficiency

Muscle cramps with exercise

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59
Q

Essential fructosuria

A

Fructokinase deficiency
Excrete fructose
Still have hexokinase so benign (incidental finding usually)

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60
Q

Fructosemia

A

“Fructose intolerance”
Aldolase B deficiency
Liver damage

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61
Q

Galactokinase deficiency causes?

A

Cataracts

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62
Q

Galactosemia causes?

A

Cataracts
Mental retardation
Liver damage

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63
Q

What does the citrate shuttle do?

A

Fatty acid transport out of the mitochondria

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64
Q

What does the carnitine shuttle do?

A

Fatty acid transport into the mitochondria

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65
Q

What lysosomal diseases have a cherry-red macula? (2)

A

Tay-Sachs

Neimann-Pick

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66
Q

What lysosomal diseases have a gargoyle face? (2)

A

Gaucher’s

Hurler’s

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67
Q

Tay-Sachs

A

Hexosaminidase A deficiency
Blindness
Incoordination
Dementia

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68
Q

Sandhoff’s

A

Hexosaminidase A/B deficiency

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69
Q

Gaucher’s

A

Glucocerebrosidase deficiency
Wrinkled tissue macrophage
Bone pain

70
Q

Neimann-Pick

A

Sphingomyelinase deficiency

Zebra bodies

71
Q

Fabry’s

A

Alpha-galactosidase deficiency
Corneal clouding
Attacks baby’s kidneys
X-linked

72
Q

Krabbe’s

A

Beta-galactosidase deficiency

Globoid bodies

73
Q

Metachromatic leukodystrophy

A

Arylsulfatase deficiency

Childhood multiple sclerosis

74
Q

Hunter’s

A

Iduronidase deficiency

Milder form

75
Q

Hurler’s

A

Iduronidase deficiency

Worse form

76
Q

Lesch-Nyhan

A

HGPRT deficiency
Gout
Neuropathy
Self-mutilation

Hypoxanthine guanine phosphoribosyltransferase

(Herbert self mutilates)

77
Q

What do white diaper crystals suggest?

A

Excess orotic acid

78
Q

What does biotin act as a cofactor for by donating CO2?

A

Carboxylation

79
Q

What does THF donate methyl groups for?

A

Nucleotides

80
Q

What does SAM donate methyl groups for?

A

All other reactions (not nucleotides - THF)

81
Q

What is the difference between heterochromatin and euchromatin?

A

Heterochromatin — tightly coiled

Euchromatin — loose (10nm fibers), active

82
Q

What are the purines?

A

Pur As Gold

83
Q

What are the pyrimidines?

84
Q

Silent mutation

A

Changes leave the same amino acid

85
Q

Point mutation

A

Changes one base

86
Q

Transition (mutation)

A

Changes one purine to another purine or pyrimidine to pyrimidine

87
Q

Transversion (mutation)

A

Changes one purine to a pyrimidine or vice versa

88
Q

Frameshift mutation

A

Insert or delete 1-2 bases

89
Q

Missense mutation

A

Mistaken amino acid substitution

90
Q

Nonsense mutation

A

Early stop codon

91
Q

Southern blot detects?

92
Q

Northern blot detects?

93
Q

Western blot detects?

94
Q

What are the essential amino acids?

A 
PVT TIM HALL
Phe - phenylalanine 
Val - valine
Trp - tryptophan 
Thr - threonine
Iso - isoleucine 
Met - methionine 
His - histidine 
Arg - arginine 
Lys - lysine 
Leu - leucine

Tyrosine becomes essential if phenylalanine is deficient

95
Q

Essential fatty acids

A

Linolenic

Linoleic

96
Q

Acidic amino acids

97
Q

Basic amino acids

98
Q

Sulfur containing amino acids

99
Q

O-bond amino acids

A

Ser
Thr
Tyr

100
Q

N-bond amino acids

101
Q

Branched chain amino acids

A

Can’t LIV without them

Leu
Iso
Val

102
Q

Aromatic amino acids

103
Q

Smallest amino acid

104
Q

Ketogenic amino acids

105
Q

Glucogenic + ketogenic amino acids

A 
PITT
Phe
Iso 
Thr
Trp
106
Q

Glucogenic amino acids

A

All the rest

107
Q

Trypsin cuts?

A

Tryp to LA
Lys
Arg

108
Q

Beta ME cuts?

A

Sulfur containing amino acids
Cys
Met

109
Q

Chymotrypsin cuts?

110
Q

Carboxypeptidase cuts?

A

Left(!) of any amino acid on the carboxy terminal (right terminal)

111
Q

Aminopeptidase cuts?

A

Right of N terminus

112
Q

CNBr cuts?

A

Right of Met

113
Q

Mercaptoethanol cuts?

A

Right of Cys, Met

114
Q

Elastase cuts?

A

Right of Gly, Ala, Ser

115
Q

What amino acids does acid hydrolysis denature?

116
Q

What amino acid turns yellow on Nurhydrin reaction?

A

Proline

All others turn purple

117
Q

What does alpha1-antitrypsin do?

A

Inhibits trypsin from getting loose

118
Q

PKU

A

No phenylalanine to tyrosine via phenylalanine hydroxylase

Nutrasweet sensitivity
Mental retardation
Pale, blonde hair, blue eyes
Musty odor

Phenylalanine restrictive diet
Tyrosine becomes essential

119
Q

Albinism

A

Tyrosinase deficiency

No Tyr to melanin

120
Q

Maple syrup urine disease

A

Defective metabolism of branched amino acids (Leu, Iso, Val)

Amino acids leak out into urine
Tastes sweet, smells like burnt sugar

121
Q

Homocysteinuria

A 
No homocysteine to cysteine 
COLA stones
Cysteine 
Ornithine
Lysine 
Arginine
122
Q

Pellagra

A

Niacin deficiency

4D’s 
Dermatitis 
Diarrhea 
Dementia
Death
123
Q

Hartnup’s

A

No Trp to make niacin or serotonin
Presents like pellagra
Can mimic corn rich diet

124
Q

What causes anterior leg bowing?

A

Neonatal syphilis

125
Q

What causes lateral leg bowing?

126
Q

What are the names of the B vitamins?

A

“The Rich Never Lie about Panning Pyrite Filled Creeks”

Vitamin B1: Thiamine
Vitamin B2: Riboflavin 
Vitamin B3: Niacin
Vitamin B4: Lipoic acid
Vitamin B5: Pantothenic acid
Vitamin B6: Pyridoxine 
Vitamin B9: Folate
Vitamin B12: Cobalamin
127
Q

Vitamin A

A

Night vision
CSF production
PTH

128
Q

Vitamin B1 Thiamine

A

Cofactor for dehydrogenases and transketolase

129
Q

Vitamin B2 Riboflavin

A

FAD cofactor

130
Q

Vitamin B3 Niacin

A

NAD cofactor

131
Q

Vitamin B4 Lipoic Acid

A

Glycolysis

No known disease

132
Q

Vitamin B5 Pantothenic Acid

A

Part of AcetylCoA

No known disease

133
Q

Vitamin B6 Pyridoxine

A

Cofactor for transaminases

Myelin integrity

134
Q

Vitamin B9 Folate

A

Nuclear division

135
Q

Vitamin B12 Cobalamin

A

Cofactor for HMT and MMM

136
Q

Vitamin C

A

Collagen synthesis

137
Q

Vitamin D

A

Mineralization of bones and teeth

138
Q

Vitamin K

A

Clotting factors

10, 9, 7, 2, C

139
Q

Biotin

A

Cofactor for carboxylation

140
Q

Calcium

A

Neuronal function
Atrial depolarization
Smooth muscle contractility

141
Q

Copper

A

Collagen synthesis

142
Q

Iron Fe2+

A

Hemoglobin function

Electron transport

143
Q

Bronze pigmentation

A

Iron deposit in skin

144
Q

Bronze cirrhosis

A

Iron deposit in liver

145
Q

Bronze diabetes

A

Iron deposit in pancreas

146
Q

Hemosiderosis

A

Iron overload in bone marrow

147
Q

Hemochromatosis

A

Iron deposit in organs

148
Q

Magnesium

A

PTH

Cofactor for kinases

149
Q

Zinc

A

Taste buds
Hair
Sperm function

150
Q

Chromium

A

Insulin function

151
Q

Molebdenum

A

Purine breakdown (xanthine oxidase)

152
Q

Manganese

A

Glycolysis

153
Q

Selenium

A

Heart function
Deficiency —> dilated cardiomyopathy
Smells like garlic

154
Q

Tin

A

Hair growth

155
Q

Fluoride

A

Teeth and bone growth

Excess blocks enolase in glycolysis (low energy state)

156
Q

Iodine

A

Endocrine function

157
Q

Kwashiorkor

A 
Malabsorption 
Big belly (ascites) 
Protein deficiency
158
Q

Marasmus

A

Starvation
Skinny
Calorie deficient

159
Q

Where does the Pre label send stuff?

A

Rough Endoplasmic Reticulum

160
Q

Where does the Pro label send stuff?

161
Q

Where does the Mannose-6-Phosphate send stuff?

162
Q

Where does the N-terminal sequence send stuff?

A

Mitochondria

163
Q

What are the 4 types of collagen?

A

SCAB

1: Skin, bone
2: Connective tissue, aqueous humor
3: Arteries
4: Basement membrane

164
Q

How does scleroderma present?

A

Tight skin

165
Q

How does Ehlers Danlos present?

A

Hyperstretchable skin

166
Q

How does Marfan’s present?

A 
Hyperextensible joints
Arachnodactyly
Wing span longer than height 
Aortic root dilation 
Aortic aneurysm
Mitral valve prolapse 
Dislocated lens from bottom —> look up to Mars
167
Q

How does Homocysteinuria present?

A

Marfan’s in child

Dislocated lens from top —> looking down at child

168
Q

How does Minky’s kinky hair syndrome present?

A

Hair looks like copper wire

Copper deficiency

169
Q

How does Scurvy present?

A

Bleeding gums and hair follicles

170
Q

How does Takasayu’s arteritis present?

A

Asian women with very weak pulse

Granulomatous aortitis

171
Q

How does Osteogenesis Imperfecta present?

A

Blue sclera
Shattered bones
Not child abuse

S. One (24 decks)

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