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PASS SOUTH CLUES > 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 the best amino acid buffer in the body?

A

histidine

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4
Q

What is the RLE in glycolysis?

A

PFK-1

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5
Q

What is the RLE in gluconeogenesis?

A

pyruvate carboxylase

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6
Q

What is the RLE in the HMP shunt?

A

G6PD

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7
Q

What is the RLE in glycogenesis?

A

glycogen synthase

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8
Q

What is the RLE in glycogenolysis?

A

glycogen phosphorylase

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9
Q

What is the RLE in FA synthesis?

A

acetyl-CoA carboxylase

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10
Q

What is the RLE in beta-oxidation?

A

CAT-1

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11
Q

What is the RLE in cholesterol synthesis?

A

HMG CoA reductase

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12
Q

What is the RLE in ketogenesis?

A

HMG CoA synthase

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13
Q

What is the RLE in purine synthesis?

A

PRPP synthase

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14
Q

What is the RLE in pyrimidine synthesis?

A

ASP transcarbamoylase

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15
Q

What is the RLE in the TCA cycle?

A

isocitrate dehydrogenase

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16
Q

What is the RLE in the urea cycle?

A

CPS-1

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17
Q

What is the RLE in heme synthesis?

A

delta-ALA synthase

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18
Q

What does an isomerase do?

A

creates an isomer

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19
Q

What does an epimerase do?

A

creates an epimer, which differs around 1 chiral carbon

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20
Q

What does a mutase do?

A

moves a sidechain from one carbon to another (intrachain)

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21
Q

What does a transferase do?

A

moves a sidechain from one substrate to another (interchain)

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22
Q

What does a kinase do?

A

phosphorylates using ATP

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23
Q

What does a phosphorylase do?

A

phosphorylates using inorganic phosphate

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24
Q

What does a carboxylase do?

A

forms C-C bonds (with ATP and biotin)

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25
Q

What does a synthase do?

A

consumes 2 substrates

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26
Q

What does a synthetase do?

A

consumes 2 substrates, uses ATP

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27
Q

What does a phosphatase do?

A

breaks phosphate bond

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28
Q

What does a lyase do?

A

cuts C-C bonds with ATP

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29
Q

What does a dehydrogenase do?

A

removes H with a cofactor

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30
Q

What does a thio do?

A

breaks S bonds

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31
Q

What is diffusion?

A

from high to low concentration

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32
Q

What is active transport?

A

goes against concentration gradient

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33
Q

What is zero-order kinetics?

A

metabolism independent of concentration

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34
Q

What is first-order kinetics?

A

constant drug percentage metabolism over time, depends on drug concentration

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35
Q

What is efficacy?

A

max effect regardless of dose (lower with non-competitive antagonist)

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36
Q

What affects efficacy?

A

Vmax

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37
Q

What is potency?

A

amount of drug needed to produce effect (lower with competitive antagonist)

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38
Q

What affects potency?

A

Km

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39
Q

What is Kd?

A

concentration of drug that binds 50% of receptors

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40
Q

What is EC 50?

A

concentration of drug that produces 50% of maximal response

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41
Q

What is competitive inhibition?

A

fights for active sit, no change in Km, potency decreases

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42
Q

What is non-competitive inhibition?

A

binds a regulatory site, no change in Km, efficacy decreases, Vmax decreases

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43
Q

What is an endothermic reaction?

A

consumes heat

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44
Q

What is an exothermic reaction?

A

gives off heat

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45
Q

What is the peak level?

A

4 hrs after dose (if too high, decrease dose)

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46
Q

What is the trough level?

A

2 hrs before dose (if too high, give less often)

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47
Q

What is t 1/2?

A

half-life, the time it takes for the body to use half of the drug ingested

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48
Q

What is von Gierke? (3)

A

glucose-6-phosphatase deficiency
hypoglycemia
hepatosplnomegaly

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49
Q

What is Pompe’s?

A

cardiac alpha-1, 4-glucosidase deficiency/DIE early

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50
Q

What is Cori’s?

A

debranching enzyme deficiency/short branches of glycogen

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51
Q

What is Anderson’s?

A

branching enzyme deficiency/long chains of glycogen

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52
Q

What is McArdle’s? (2)

A

muscle phophorylase deficiency

muscle cramps with exercise

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53
Q

What is Essential Fructosuria? (2)

A 
fructokinase deficiency
excrete fructose (still have hexokinase)
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54
Q

What is Fructosemia? (2)

A

“fructose intolerance” (aldolase B deficiency)

liver damage

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55
Q

What does a galactokinase deficiency cause?

A

cataracts

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56
Q

What does galactosemia cause? (4)

A

galactose-1-uridyl-transferase deficiency
cataracts
mental retardation
liver damage

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57
Q

What does the citrate shuttle do?

A

FA transport out of mitochondria

58
Q

What does the carnitine shuttle do?

A

FA transport into mitochondria

59
Q

What lysosomal diseases have a cherry-red spot?

A

Tay-Sachs and Niemann-Pick

60
Q

Whay lysosomal diseases have a gargoyle-face?

A

Gaucher’s and Hurler’s

61
Q

What is Tay Sachs? (4)

A

hexosaminidase A deficiency
blindness
incoordination
dementia

62
Q

What is Sandhoff’s?

A

hoxosaminidase A/B deficiency

63
Q

What is Gaucher’s? (3)

A

glucocerebrosidase deficiency
wrinkled tissue
bone pain

64
Q

What is Niemann-Pick? (2)

A

sphingomyelinase deficiency

zebra bodies

65
Q

What is Fabry’s? (4)

A

alpha-galactosidase deficiency
corneal clouding
attacks baby’s kidneys
X-linked

66
Q

What is Krabbe’s? (2)

A

beta-galactosidase deficiency

globoid bodies

67
Q

What is Metachromatic Leukodystrophy? (2)

A

arylsulfatase deficiency

childhood MS

68
Q

What is Hunter’s?

A

iduronidase deficiency, milder form

69
Q

What is Hurler’s?

A

iduronidase deficiency, worse form

70
Q

What is Lesch-Nyhan? (4)

A

HGPRT deficiency
gout
neuropathy
self-mutilation

71
Q

What do white diaper crystals suggest?

A

excess orotic acid

72
Q

What does biotin donate methyl groups for?

A

carboxylation

73
Q

What does THF donate methyl groups for?

A

nucleotides

74
Q

What does SAM donate methyl groups for?

A

all other reactions (not for carboxylation or nucleotides)

75
Q

What is the difference between heterochromatin and euchromatin?

A

heterochromatin is tightly coiled while euchromatin is loose (10 nm fibers)

76
Q

What are the purines?

A

A and G

77
Q

What are the pyrimidines?

A

C, U, T

78
Q

What is a silent mutation?

A

changes leave the same amino acid

79
Q

What is a point mutation?

A

changes one base

80
Q

What is a transition?

A

changes one purine to another purine

81
Q

What is a traversion?

A

changes one purine to a pyrimidine

82
Q

What is a frameshift mutation?

A

insert or delete 1-2 bases

83
Q

What is a missense mutation?

A

mistaken amino acid substitution

84
Q

What is a nonsense mutation?

A

early stop codon

85
Q

What does a southern blot detect?

A

DNA

86
Q

What does a northern blot detect?

A

RNA

87
Q

What does a western blot detect?

A

protein

88
Q

What are the essential amino acids?

A

PVT TIM HALL

P: phenylalanine
V: valine
T: tryptophan
T: threonine
I: isoleucine
M: methionine
H: histidine
A: arginine
L: lysine
L: leucine
89
Q

What are the essential fatty acids? (2)

A

linolenic

linoleic

90
Q

What are the acidic amino acids? (2)

A

aspartate

glutamate

91
Q

What are the basic amino acids? (2)

A

lysine and arginine (cut by trypsin)

92
Q

What are the sulfur containing amino acids? (2)

A

cysteine and methionine (cut by beta-ME)

93
Q

What are the O-bond amino acids? (3)

A

serine
threonine
tyrosine

94
Q

What are the N-bond amino acids? (2)

A

asparagine and glutamine (denatured by acid hydrolysis)

95
Q

What are the branched amino acids? (3)

A

leucine
isoleucine
valine

96
Q

What are the aromatic amino acids? (3)

A

phenylalanine, tyrosine, tryptophan (cut by chymotrypsin)

97
Q

What is the smallest amino acid?

A

glycine

98
Q

What amino acids make disulfide bonds? (2)

A

cysteine

methionine

99
Q

What amino acid is excitatory for the CNS?

A

asparagine

100
Q

What amino acid makes catecholamines?

A

tyrosine

101
Q

What amino acid causes kinks?

A

proline

102
Q

What amino acid is used to make cysteine?

A

methionine

103
Q

What does ketogenic mean?

A

made from and broken into Acetyl-CoA

104
Q

What does glucogenic mean?

A

made from and broken into anything but Acetyl-CoA

105
Q

What are the ketogenic amino acids? (2)

A

lysine

leucine

106
Q

What are the glucogenic + ketogenic amino acids?

A

PITT

P: phenylalanine
I: isoleucine
T: threonine
T: tryptophan

107
Q

What are the hydrophobic amino acids? (3)

A

valine
alanine
isoleucine

108
Q

What amino acids does trypsin cut? (2)

A

lysine and arginine (the basic amino acids)

109
Q

What amino acids does beta-ME cut? (2)

A

cysteine and methionine (the sulfur-containing amino acids)

110
Q

What amino acids does acid hydrolysis denature? (2)

A

asparagine and glutamine (the N-bond amino acids)

111
Q

What amino acids does chymotrypsin cut? (3)

A

phenylalanine, tyrosine, tryptophan (the aromatic amino acids)

112
Q

What amino acid turns yellow on Nurhydrin reaction?

A

proline

113
Q

What does carboxypeptidase cut?

A

left of any amino acid on the carboxy terminal

114
Q

What does aminopeptidase cut?

A

right of methionine

115
Q

What does mercaptoethanol cut? (2)

A

right of cysteine and methionine (the sulfur-containing amino acids)

116
Q

What does elastase cut? (3)

A

right of glycine
alanine
serine

117
Q

What does alpha 1-AT do?

A

inhibit trypsin from getting loose

118
Q

What is PKU? (7)

A

no phenylalanine to tyrosine (via phenylalanine hydroxylase)
deficient in tyrosine
build-up of phenyl-pyruvate and phenyl-acetate
nutrasweet sensitivity
mental retardation
pale, blond hair, blue eyes
musty odor

119
Q

What is albinism?

A

no tyrosine to melanin (via tyrosinase)

120
Q

What is Maple Syrup Urine disease? (2)

A

defective metabolism of branched chain amino acids

defect in a nephron transport protein

121
Q

What is Homocystinuria? (2)

A

no homocysteine to cysteine
results in “COLA” stones

C: cysteine
O: ornithine
L: lysine
A: arginine

122
Q

What is Pellagra? (5)

A 
niacin deficiency (vit B3)
diarrhea
dermatitis
dementia
death
123
Q

What is Hartnup’s? (3)

A

no tryptophan to niacin + serotonin
presents like pellegra
can mimic a corn-rich diet

124
Q

What causes anterior leg bowing?

A

neonatal syphilis

125
Q

What causes lateral leg bowing?

A

rickets

126
Q

What is Kwashiorkor? (3)

A 
malabsorption
big bell (ascites)
protein deficiency
127
Q

What is Marasmus? (3)

A

starvation
skinny
calorie deficiency

128
Q

Where does the Pre label send stuff to?

A

ER

129
Q

Where does the Pro label send stuff to?

A

Golgi

130
Q

Where does the Mannose-6-P send stuff to?

A

Lysosome

131
Q

Where does the N-terminal sequence send stuff to?

A

mitochondria

132
Q

What are the 4 types of collagen?

A

SCAB

Type I: Skin, bone
Type II: Connective tissue, aqueous humor
Type III: Arteries
Type IV: Basement membrane

133
Q

How does Scleroderma present?

A

tight skin

134
Q

How does Ehlers Danlos present?

A

hyperstretchable skin

135
Q

How does Marfan’s present? (6)

A 
hyperextensible joints
arachnodactyly
wing span longer than height
aortic root dilation, aortic aneurysm
mitral valve prolapse
dislocated lens from bottom of eye (look up)
136
Q

How does Homocystinuria present?

A

dislocated lens from top of eye (look down)

137
Q

How does Minky Kinky hair disease present? (2)

A

hair looks like copper wire (Cu deficiency)

hair cuts face

138
Q

How does Scurvy present? (2)

A

bleeding gums

bleeding hair follicles

139
Q

How does Takayasu arteritis present? (2)

A

Asian female with very weak pulses

granulomatous arteritis

140
Q

How does Osteogenesis Imperfecta present? (2)

A

shattered bones

blue sclera

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