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Biochemistry > Exam 3 Ford > Flashcards

Exam 3 Ford Flashcards

1
Q

passive transport

A

without energy, down [ ] gradient

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2
Q

active transport

A

ATP hydrolysis, against [ ] gradient

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3
Q

3 modes of transport

A

antiporter, symporter, uniporter

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4
Q

3 categories of transport

A

pump, carrier: active

channel: passive

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5
Q

P type ATPase has 4 domains

A

main: PHOSPHORYLATES ITSELF
transmembrane
actuator - links cytosolic and transmembrane domains
nucleotide binding - binds ATP
phosphorylation - accepts phosphate from ATP

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6
Q

P type ATPase mechanism

A

E1 open to cytosol and binds A –> self phosphorylation –> E2 open to “outside” and release A and bind B (eversion) –> reset to E1 and release B

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7
Q

ABC transporters

A

2 transmembrane domains
2 nucleotide binding domains - bind ATP
extra piece if importer is: substate binding protein (in bacteria, NOT humans

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8
Q

ABC transporter mechanism

A

NO PHOSPHORYLATION

bind molecule –> bind ATP, dimerize ABC motif –> eversion –> release molecule and ATP and Pi –> reset

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9
Q

F type ATP synthase

A

makes ATP (phosphorylation factor)

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10
Q

2 active transport mechanism

A

[ ] gradient of A made by 1 AT –> release of A powers B movement against gradient

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11
Q

factors affecting diffusion rates (7)

A 
[ ] gradient magnitude 
molecule size 
surface area (volume ratio) 
temperature
solvent density/viscosity 
solute solubility
distance to destination
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12
Q

selectivity filter

A

restricts WHAT can pass

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13
Q

gate

A

restricts WHEN can pass

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14
Q

ion channels have

A

gate and selectivity filter

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15
Q

aquaporins have

A

only selectivity filter, no gate

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16
Q

gap junctions have

A

no gate or selectivity filter

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17
Q

voltage ion channel

A 
opens when membrane potential changes 
helix 4 repeated: 
V shaped; closed; helices closer
X shaped; helices towards extracellular side 
ex. voltage gated K channel
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18
Q

ligand gated ion channel

A

similar to signal transduction proteins
bind –> change shape –> go through
ex. acetylcholine receptor

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19
Q

mechanical stress gating ion channel

A

change in pressure
stresses distort membrane and protein itself
used on sensory cells

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20
Q

leakage ion channels

A

gates open randomly and continuous ion movement

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21
Q

selectivity filter examples

A
  • bacterial K channel = voltage gated ion channel
  • aquaporins - no gate, narrow single file line of water molecules via H bonds, Arg at narrowest repels cations
  • gap junctions: size is the only limitation
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22
Q

adherens junctions

A

actin and cell to cell

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23
Q

desmosomes

A

intermediate filaments and cell to cell

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24
Q

actin linked cell matrix junctions

A

actin and cell to ECM

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25
Q

hemidesmosomes

A

intermediate filaments and cell to ECM

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26
Q

ionophores

A

biggest class of carriers (common antibiotics)

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27
Q

purines (2)

A

two rings
adenine
guanine

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28
Q

pyrimidines (3)

A

one ring
thymine
uracil
cytosine

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29
Q

nucleotide and nucleoside

A

nucleotide: sugar + base + phosphate
nucleoside: sugar + base (NO PHOSPHATE)

all nucleoside X phosphates are nucleotides

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30
Q

DNA (4)

A

2 strands
B helix
pucker: C2 endo
function: storage

growth: 5’ –> 3’

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31
Q

RNA (4)

A

1 strand
A helix
pucker: C3 endo
function: transport, catalysis, regulation

growth: 5’ –> 3’

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32
Q

hairpin/cruciform nontraditional structure

A

need palindromic sequence (inverted repeat)

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33
Q

triplexes nontraditional structure

A 
homopurine-homopyrimidine duplex 
Hoogsteen H bonds 
artificially add a 3rd strand 
binds to MAJOR groove
makes H bones 
only binds PURINES!
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34
Q

quadruplexes nontraditional structure

A

GUANINES only

occur at telomeres and promotors

35
Q

induced mutations (6)

A 
base analogs 
alkylating agents
intercalating agents
adduct forming agents 
UV light 
ionizing radiation
36
Q

N end rule

A

N terminal AA identity determines rate of ubiquination

small and nonpolar: long
large: now
polar and charged: modified before then degraded

37
Q

ammonia lyase

A

deamination
dehydration –> serine deamination –> pyruvate

others:
threonine –> a-ketobutyrate (via threonine dehydratase)
histidine –> trans urocanic (via histidase)

38
Q

2 step deamination process

A

AA + a ketoglutarate –> glutamate (via aminotransferase)

glutamate –> a-ketoglutarate (via glutamate dehydrogenase)

39
Q

AST/GOT

A

aspartate aminotransferase (in cells)
glutamate oxaloacetate transaminase (in serum)
aspartate –> oxaloacetate

alanine aminotransferase (in cells)
glutamate pyruvate transaminase (in serum)
alanine –> pyruvate

40
Q

muscle vs other cells in urea cycle

A

muscle uses alanine and ALT –> liver

other cells use glutamate –> liver

41
Q

urea molecule comes from what… (4)

A

water, glutamate, HCO3, aspartate

42
Q

CPS1 (carbamoyl phosphate synthetase 1)

A

urea cycle
CO2 + NH3 –> carbamoyl phosphate

COMMITTED STEP IN UREA CYCLE

activated by NAG (N-acetyl glutamate)

43
Q

gluconeogenic AA (13)

A 
TCA cycle
alanine
arginine 
asparagine
aspartate
cysteine 
glycine 
glutamate
glutamine
histidine
methionine
proline
serine
valine
44
Q

ketogenic AA (2)

A

leucine
lysine

used to create ketone bodies

45
Q

both gluconeogenic and ketogenic AA (5)

A 
I, P, T, T, T
isoleucine
phenylalanine
tyrosine
threonine
tryptophan
46
Q

precursors for AA synthesis (3)

A

glycolysis
TCA cycle
PPP

47
Q

what are the derivatives of glutamate (3)

A

glutathione
polyamines
GABA

48
Q

what are the derivatives of glycine (1)

A

heme

49
Q

what are the derivatives of arginine (2)

A

NO

creatinine phosphate

50
Q

what are the derivatives of methionine (1)

A

SAM

51
Q

what are the derivatives of histidine (1)

A

histamine

52
Q

what are the derivatives of tryptophan (1)

A

serotonin –> melatonin

53
Q

what are the derivatives of tyrosine (1)

A

L-DOPA
if decarboxylation –> epinephrine/NE/dopamine
if oxidation –> melanin pigments

54
Q

activation of glutamine synthesis

A

deadenylylation of P-UMP + AT –> active glutamine synthetase

55
Q

inhibition of glutamine synthesis

A

P-AT –> adenylylation –> inactive glutamine synthetase

56
Q

liver on metabolism

A

only organ able to carry out all pathways
MVP of metabolism
depends on b-oxidation of FA for own needs

57
Q

preferred energy source of RBC

A

glucose only

58
Q

preferred energy source of brain

A

glucose and ketone bodies

59
Q

preferred energy source of adipose

A

glucose and FA

60
Q

preferred energy source of liver

A

FA

61
Q

preferred energy source of muscle

A

glucose / FA / AA

most flexible

62
Q

adipose tissue

A

TAG synthesis and storage

release FA and glycerol to blood (albumin)

63
Q

brain

A

biggest energy user
no storage
uses 20% of total o2

64
Q

heart

A

aerobic
uses glucose, lactate, FA, ketone bodies
no glycogen stores

65
Q

skeletal m

A

lots of glycogen
no glucose 6 phosphatase SO cannot export glucose
uses FA and ketone bodies

66
Q

anaerobic glycolysis

A

glycogenolysis
lactate formation: glycogen –> G6P –> pyruvate –> lactate

with lactate buildup,
decrease muscle power
increase muscle fatigue

67
Q

fate of lactate after anaerobic glycolysis

A

clucose regeneration

cori cycle - between muscle and liver

68
Q

oxidative phosphorylation

A

production of energy from oxidation of coenzymes
NADH –> 3 ATP
FADH2 –> 2 ATP

69
Q

energy charge of cell =

A

ATP : ADP ratio

70
Q

reducing power of cell =

A

NADH : NAD+ ratio

also called potential energy

71
Q

T/F:

ATP:ADP and NADH:NAD+ ratio are irreversibly proportional.

A

correct.

72
Q

GLP1 (glucagon like peptide 1)

A

signal molecule from intestine

  • goes to pancreas –> increase insulin synthesis and secretion
  • goes to brain –> increase satiety, decrease food intake and body weight
73
Q

CCK (cholecystokinin)

A

goes to brain –> increase satiety, decrease food intake and body weight

74
Q

Ghrelin

A
  • stimulates appetite
  • increases before meal, decreases after meal
  • secreted by stomach
75
Q

leptin

A

secreted by adipose tissue in direct proportion to fat mass

-inhibits food intake and stimulates energy expenditure

76
Q

energy sensor in cells

A

AMPK (AMP activated protein kinase)
increase ATP –> AMP inactive
decrease ATP –> AMP active –> phosphorylation

77
Q

regulators of AMPK

A

upregulation: food, FA oxidation, increase glucose uptake, glycolysis
downregulation: lipolysis, FA synthesis, glyconeogenesis, insulin

78
Q

calorie content

A 
1kJ = 239 cal 
1kcal = 4.184 kJ
79
Q

kcal =

A

amount of energy needed to raise temp of 1g of water by 1C

80
Q

BMR

A

basal metabolic rate

  • energy involved in normal body functions
  • depends on body weight
81
Q

BMR =

A

24 x body weight (kg)
units: kcal/day

1kg = 2.2 lb

82
Q

BMI =

A

weight (kg) / height (m2)

83
Q

marasmus

A

protein-calorie malnutrition

  • acute malnutrition
  • severe fat/muscle wasting
  • severely low food intake
84
Q

cachexia

A

related to malnutrition

  • predominant loss of muscle
  • increase muscle catabolism
  • decrease muscle protein synthesis
  • increase proinflammatory cytokines

Biochemistry (5 decks)

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