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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
What does a synthase do?
consumes 2 substrates
26
What does a synthetase do?
consumes 2 substrates, uses ATP
27
What does a phosphatase do?
breaks phosphate bond
28
What does a lyase do?
cuts C-C bonds with ATP
29
What does a dehydrogenase do?
removes H with a cofactor
30
What does a thio do?
breaks S bonds
31
What is diffusion?
from high to low concentration
32
What is active transport?
goes against concentration gradient
33
What is zero-order kinetics?
metabolism independent of concentration
34
What is first-order kinetics?
constant drug percentage metabolism over time, depends on drug concentration
35
What is efficacy?
max effect regardless of dose (lower with non-competitive antagonist)
36
What affects efficacy?
Vmax
37
What is potency?
amount of drug needed to produce effect (lower with competitive antagonist)
38
What affects potency?
Km
39
What is Kd?
concentration of drug that binds 50% of receptors
40
What is EC 50?
concentration of drug that produces 50% of maximal response
41
What is competitive inhibition?
fights for active sit, no change in Km, potency decreases
42
What is non-competitive inhibition?
binds a regulatory site, no change in Km, efficacy decreases, Vmax decreases
43
What is an endothermic reaction?
consumes heat
44
What is an exothermic reaction?
gives off heat
45
What is the peak level?
4 hrs after dose (if too high, decrease dose)
46
What is the trough level?
2 hrs before dose (if too high, give less often)
47
What is t 1/2?
half-life, the time it takes for the body to use half of the drug ingested
48
What is von Gierke? (3)
glucose-6-phosphatase deficiency hypoglycemia hepatosplnomegaly
49
What is Pompe's?
cardiac alpha-1, 4-glucosidase deficiency/DIE early
50
What is Cori's?
debranching enzyme deficiency/short branches of glycogen
51
What is Anderson's?
branching enzyme deficiency/long chains of glycogen
52
What is McArdle's? (2)
muscle phophorylase deficiency | muscle cramps with exercise
53
What is Essential Fructosuria? (2)
``` fructokinase deficiency excrete fructose (still have hexokinase) ```
54
What is Fructosemia? (2)
"fructose intolerance" (aldolase B deficiency) | liver damage
55
What does a galactokinase deficiency cause?
cataracts
56
What does galactosemia cause? (4)
galactose-1-uridyl-transferase deficiency cataracts mental retardation liver damage
57
What does the citrate shuttle do?
FA transport out of mitochondria
58
What does the carnitine shuttle do?
FA transport into mitochondria
59
What lysosomal diseases have a cherry-red spot?
Tay-Sachs and Niemann-Pick
60
Whay lysosomal diseases have a gargoyle-face?
Gaucher's and Hurler's
61
What is Tay Sachs? (4)
hexosaminidase A deficiency blindness incoordination dementia
62
What is Sandhoff's?
hoxosaminidase A/B deficiency
63
What is Gaucher's? (3)
glucocerebrosidase deficiency wrinkled tissue bone pain
64
What is Niemann-Pick? (2)
sphingomyelinase deficiency | zebra bodies
65
What is Fabry's? (4)
alpha-galactosidase deficiency corneal clouding attacks baby's kidneys X-linked
66
What is Krabbe's? (2)
beta-galactosidase deficiency | globoid bodies
67
What is Metachromatic Leukodystrophy? (2)
arylsulfatase deficiency | childhood MS
68
What is Hunter's?
iduronidase deficiency, milder form
69
What is Hurler's?
iduronidase deficiency, worse form
70
What is Lesch-Nyhan? (4)
HGPRT deficiency gout neuropathy self-mutilation
71
What do white diaper crystals suggest?
excess orotic acid
72
What does biotin donate methyl groups for?
carboxylation
73
What does THF donate methyl groups for?
nucleotides
74
What does SAM donate methyl groups for?
all other reactions (not for carboxylation or nucleotides)
75
What is the difference between heterochromatin and euchromatin?
heterochromatin is tightly coiled while euchromatin is loose (10 nm fibers)
76
What are the purines?
A and G
77
What are the pyrimidines?
C, U, T
78
What is a silent mutation?
changes leave the same amino acid
79
What is a point mutation?
changes one base
80
What is a transition?
changes one purine to another purine
81
What is a traversion?
changes one purine to a pyrimidine
82
What is a frameshift mutation?
insert or delete 1-2 bases
83
What is a missense mutation?
mistaken amino acid substitution
84
What is a nonsense mutation?
early stop codon
85
What does a southern blot detect?
DNA
86
What does a northern blot detect?
RNA
87
What does a western blot detect?
protein
88
What are the essential amino acids?
PVT TIM HALL ``` P: phenylalanine V: valine T: tryptophan T: threonine I: isoleucine M: methionine H: histidine A: arginine L: lysine L: leucine ```
89
What are the essential fatty acids? (2)
linolenic | linoleic
90
What are the acidic amino acids? (2)
aspartate | glutamate
91
What are the basic amino acids? (2)
lysine and arginine (cut by trypsin)
92
What are the sulfur containing amino acids? (2)
cysteine and methionine (cut by beta-ME)
93
What are the O-bond amino acids? (3)
serine threonine tyrosine
94
What are the N-bond amino acids? (2)
asparagine and glutamine (denatured by acid hydrolysis)
95
What are the branched amino acids? (3)
leucine isoleucine valine
96
What are the aromatic amino acids? (3)
phenylalanine, tyrosine, tryptophan (cut by chymotrypsin)
97
What is the smallest amino acid?
glycine
98
What amino acids make disulfide bonds? (2)
cysteine | methionine
99
What amino acid is excitatory for the CNS?
asparagine
100
What amino acid makes catecholamines?
tyrosine
101
What amino acid causes kinks?
proline
102
What amino acid is used to make cysteine?
methionine
103
What does ketogenic mean?
made from and broken into Acetyl-CoA
104
What does glucogenic mean?
made from and broken into anything but Acetyl-CoA
105
What are the ketogenic amino acids? (2)
lysine | leucine
106
What are the glucogenic + ketogenic amino acids?
PITT P: phenylalanine I: isoleucine T: threonine T: tryptophan
107
What are the hydrophobic amino acids? (3)
valine alanine isoleucine
108
What amino acids does trypsin cut? (2)
lysine and arginine (the basic amino acids)
109
What amino acids does beta-ME cut? (2)
cysteine and methionine (the sulfur-containing amino acids)
110
What amino acids does acid hydrolysis denature? (2)
asparagine and glutamine (the N-bond amino acids)
111
What amino acids does chymotrypsin cut? (3)
phenylalanine, tyrosine, tryptophan (the aromatic amino acids)
112
What amino acid turns yellow on Nurhydrin reaction?
proline
113
What does carboxypeptidase cut?
left of any amino acid on the carboxy terminal
114
What does aminopeptidase cut?
right of methionine
115
What does mercaptoethanol cut? (2)
right of cysteine and methionine (the sulfur-containing amino acids)
116
What does elastase cut? (3)
right of glycine alanine serine
117
What does alpha 1-AT do?
inhibit trypsin from getting loose
118
What is PKU? (7)
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
What is albinism?
no tyrosine to melanin (via tyrosinase)
120
What is Maple Syrup Urine disease? (2)
defective metabolism of branched chain amino acids | defect in a nephron transport protein
121
What is Homocystinuria? (2)
no homocysteine to cysteine results in "COLA" stones C: cysteine O: ornithine L: lysine A: arginine
122
What is Pellagra? (5)
``` niacin deficiency (vit B3) diarrhea dermatitis dementia death ```
123
What is Hartnup's? (3)
no tryptophan to niacin + serotonin presents like pellegra can mimic a corn-rich diet
124
What causes anterior leg bowing?
neonatal syphilis
125
What causes lateral leg bowing?
rickets
126
What is Kwashiorkor? (3)
``` malabsorption big bell (ascites) protein deficiency ```
127
What is Marasmus? (3)
starvation skinny calorie deficiency
128
Where does the Pre label send stuff to?
ER
129
Where does the Pro label send stuff to?
Golgi
130
Where does the Mannose-6-P send stuff to?
Lysosome
131
Where does the N-terminal sequence send stuff to?
mitochondria
132
What are the 4 types of collagen?
SCAB Type I: Skin, bone Type II: Connective tissue, aqueous humor Type III: Arteries Type IV: Basement membrane
133
How does Scleroderma present?
tight skin
134
How does Ehlers Danlos present?
hyperstretchable skin
135
How does Marfan's present? (6)
``` 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
How does Homocystinuria present?
dislocated lens from top of eye (look down)
137
How does Minky Kinky hair disease present? (2)
hair looks like copper wire (Cu deficiency) | hair cuts face
138
How does Scurvy present? (2)
bleeding gums | bleeding hair follicles
139
How does Takayasu arteritis present? (2)
Asian female with very weak pulses | granulomatous arteritis
140
How does Osteogenesis Imperfecta present? (2)
shattered bones | blue sclera

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