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258: Physiology > lecture 13: Amino acid metabolism, transamination and deamination > Flashcards

lecture 13: Amino acid metabolism, transamination and deamination Flashcards

1
Q

true or false: aamino acids are all considered esssential

A

false

we have essential and nonessential amino acids

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2
Q

what does it mean to be an essential amino acid

A

means it must be taken in through exogenous sources

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3
Q

give 3 examples of exogenous/essential amino acids

A

lysine/leusin
valine
tryptophan

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4
Q

what are 2 examples of non essential amono acids

A

alanine and glutamate (glutamic acid)

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5
Q

what is alanine

A

3 carbon structure ,very similar to pyruvate with a nh2 group added on

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6
Q

true or false: amino acids come from a carbohydrfate base

A

true

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7
Q

why is glutamic acid improtant

A

it will allow us to form amino acid pool

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8
Q

what are the plamsma proteins formed by liver

A

albumiin
fibrinogen
immunoglubulin

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9
Q

what does the liver create intterms of proteins

A

plasma proteins

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10
Q

what is albumin and its function

A

large plasma protein that is used to transport large free fatty acides to and from tissues

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11
Q

what is functinogen and its function

A

plasma protein that is a primary clotting agent in the blood

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12
Q

what is immunoglobulin

A

plasma protein important for immunie system

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13
Q

true or false: when the old plasma proteins die they get degrades and can non longer nbe used

A

false, they can be degreades and re used

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14
Q

what happens to the old plasma proteins once they are absorbed by the reticuloendtholial cells of spleen bone marrow etc

A

they are absorbed and borkem down and can re manufactured into new proteins

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15
Q

what are thr 4 bodies that can degreae aold plasma proteins

A

spleen
bone marror
connective tissue
lymph

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16
Q

what can the spleen due in terms of absorbing old plasma prpteins

A

removes old red blood cells and produced new ones

also important for antibody

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17
Q

what can the bone marrow due

A

create rbc

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18
Q

once a protein is broken down into amino acids does it rest in tiessues?

A

the amino acids dont rest in the tissie nut rather they go to the blood stream and they travel to the organ that needs it

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19
Q

true or false: skeletal muscle protein tissue can be broken down into amino acids that can then go to the liver and regorme new proteins

A

yes

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20
Q

know the reversility of prottein domains

A

lk

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21
Q

where does the degradation and formation of new proteins occur

A

reticuloendotthelial cells

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22
Q

what form do amino acids travel in

A

ionioned amino acids

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23
Q

what is the concentration of ionized amino acids in the plasma

A

35-65 mg/fl

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24
Q

true or false: after a meal with protein, it takes a long time for the aminos to leave plasms

A

false, plasma levels return to normal levels very rapdily but control is not known

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25
Q

where do the amino acids that anter the blood stream post prandial go

A

in msucle: forms new proteins
in lvier: makes plasma proteins

=reticululendoreticule cells form the new tisssue

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26
Q

is there storage for amino acids

A

no

they move thjrough circualtion to organs and tissues that are depleted of amino acid

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27
Q

when amino acid concreation decreases, what is done to compendate

A

cell protein catabolism compensates

breakdown bodies proteins to provide amino acids

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28
Q

true or false: aminos can go straight through lipid bilayer

A

false

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29
Q

how is traposnport of amino acids done

A 
carrier mediated (need a protein trasnpored)
throught faciliateted diffusion
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30
Q

there is a lot of free amino acids floating in the cell

A

false, there is not a lot of free aminos in the cell

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31
Q

why are tehree not alot of amino acids floating in the cell

A

they rapidly get tkaen up and used for proteins

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32
Q

how are proteins in diferent tissue cells linkes

A

via reversible exchauge with plamsma amino acids

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33
Q

true or false: plasma proteins are not a good srouce of amino acids and why

A

false

they can be degraded by tissue macroh[hages and release the amino acids

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34
Q

what are the 3 compoents you need to make non eseential amino acids

A

1) carbon skeleton
2) amino group
3) need an enzyme, aminotransferance

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35
Q

explain the carbon sketelon backbone needed for making non essential amino acids

A

you need alpha keto acid (ie glucose) that comes from carbs (like glycolysis, PPP, cirtric acid cycle intermediates)

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36
Q

what are some examples of carbon skeletons that can be used to make non essential amino acids

A

pyruvate, alpha ketoglutarate, oxaloacetate

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37
Q

explain the amino group part of making an amino acid

A

you need an amino group that can donate ints NH2 group to the carbon skeleton

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38
Q

what is the most common amino group used for making non essential aminos

A

glutamate/glutamiine

39
Q

what is the amino trandfersage usually needed for making an amino

A

derivator of pyridoxine (vit. b6)

40
Q

explain the example of forning glutamate

A

1) you got an NH2 and combine to make Nh4 fgroup from another amino acid
2) you have carbon skelteon (alpha keto which came from kreb cycle)
3) NADPH (from PPP) and NADH (from kreb) are oxidived
4) glutamate is formed

41
Q

what is the definition of transamination

A

Transamination is the process by which amino groups are removed from amino acids and transferred to acceptor keto-acids

42
Q

explain the process of making alanine (transamination)

A

1) Get pyruvate (carbon skeleton)
2) get glutamic acid (amino group)
3) Transamination occurs: NH2 from glutamic acid is donated to pyruvate to form alanine
4) oxygen that is lost from pyruvate goes to alpha ketoglutarte
5) alpha can go back into the kreb cycle to be borkem down
6) alanine can go back into circualtion and help with gluconeogenesis and can build up msucle proteins

43
Q

what happens to the products of synthesis of alanine by transamination

A

1) left with alanine that can be a precursor for gluconeogenesis and can also be used for msucle protein synthesis
2) left with alpha ketoglutatrate which can then exnter the kreb cycle to be metabolized

44
Q

what enzymes help accesralate the transamination of an essential aminion

A

aminotransferases

transaminases

45
Q

what is deamination

A

the removled of an amine group (nh2) from a molucule.

46
Q

what are the enxymes that catalize the deamination

A

deaminases

47
Q

where is the majority of deamination taking place

A

in the liver (some in the kidney)

48
Q

why would we go through a process of deamination

A

usefull to break down into amino acids when there is an excess of protein intake
=no storage for amino acids therefore liver will deaminate the excess amounts and break it down)

49
Q

what does breaking down amino acids do

A

form an amino pool

50
Q

when the amino group is removed from the amino acid what does it get converted to ?

A

ammonia

51
Q

if there is an excess of glucatmate in the body

A

the liver will break it down and will take the nh4 group away and put it into the urine in kidney to form urea

52
Q

explain deamination of glutamate in the body

A

1) Glutamate gets its NH4 group removed (by deaminanses=glutamate dehydrogenase)
2) this process requires NADP to be regued to NADPH
3) you are left with alpha ketoglutara which can then be used to synthessize atp in kreb cycle
4) the NH4 and Co2 formed from will go to the urea cycle and get converted to urea

53
Q

when would deamination occur

A

increase in protein from meals

breaking down of protein in stavation periods

54
Q

what is the difference between transmaination or deamination

A

trans: invovles synthesis of nonessential amino acids
deam: involved breakdown of non essential amino acids/breakdown of excess protein

55
Q

true orfalse: transamination happens only in the liver

A

false, anywhere in the body

56
Q

whree does deamination occur

A

only in the liver

57
Q

what is the difference in enxymes between trans and deam

A

trans: transaminases/ aminotransferases catalyze
deams: deaminases

58
Q

what is teh result of transamination

A

amino group goes to the keto group

59
Q

what is the result of deamination

A

formation of ammonia

and elemenation of it through urea cycle

60
Q

true or false: glutamic acid/glutate is the amino acid that goes through trans and deam the most

A

true, common for both

61
Q

is transamination reversible

A

yes

62
Q

is deamination reversiblr

A

no

63
Q

what is the prupsoe of the glucose alanine cycle

A

maintain blood glucose levels

64
Q

under what conditions is the glucose alanine cycle usually activatied and why

A

prolongued fasting or stavation

at this point you are breaking down a lot of protetins for energy source and left with excess amino acids

65
Q

true or false: in starvation, your muscle only breaks down skelteal msucle

A

false, it also breaks down smooth and cardiac muscle to form an excess amino pool

66
Q

explain the glucose alanine cycle

A

1) muscle protein breaks down causing an increase in amino acids
2) the amino acids are deaminated leaving you with excess NH4 stores
3) through a process an transamination you can form glutament in the muscle
4) glutatment will donate the NH2 group to pyruvate to form alanine (and aplha which goes to kreb)
5) alanine that is formed i nthe muscle does not remain there but leaves through circualtion and goes to lvier

6) once alanine enters the liver there will be a reverse reaction
7) Alanine will give its nh to alpha keto which formed glutate and oyruvate in excess (which goes to to glucose and is taken back to skelteal=gluconeogenesis )
8) Gluatmeate is deaminated to form ammoinium which is released through urea

67
Q

true or false: during dttarvation we only use fat stored

A

false
we use fat sotres (which can cause ketone bodies)
we used glycogen stores (which will be depleted fast)
we use amino acids

68
Q

what happens to tthe ammonia made from the breakdown of glutamate

A

can go towarde generating more amino acids or it can be extrecreuted via urea

69
Q

how can ammonia because excreted

A

main throough urea (2 ammounia and carbon idioxide )

70
Q

where does urea formaation ofccur

A

mainly in the lvier

71
Q

what are the ammoinia carriers of the urea cycle

A

ornithine citrulline arginine

72
Q

true or false: tthe urea cycle is not linked to the kreb cycle

A

false

73
Q

is ammonia ttoxic tto he body

A

yes, theat is why we excrete it as much as bpossible)

74
Q

why is excess free NH4 toxic

A

depletes alpha ketto glutaratet which will stop the kreb cycle

75
Q

where does amino acid degradeation mostly happen

A

in the liver

76
Q

what is tthe fucntion of breaking down amino acids in the liver

A

to form major metabolic intermiedates can be be converted into glucose or oxidixed by the kreb cycle

77
Q

amino acids that are degreaded to form acetyl coa or acetoacetyl coa are called… and why

A

ketogenic amino acids because they give rise to ketone bodies

78
Q

amino acids tthat are degraded and form glucose or go through kreb cycle are called … and why

A

glucogenic because the gorm glucose

79
Q

making ketone bodies from anino acids is only bad

A

faalse

it can be used for metabolism

80
Q

whaat arae some examples of ketogenic amino acids

A

leusine
lysin
tryptophna
because htey are forming acetyl coa=ketone bodies

81
Q

what are some examples of glucogenic amino acids

A

glutamine
proline
arginine

82
Q

glucogenic amino acids from precors for..

A

glucose

83
Q

ketogenic amono acids form precoursed

A

for ketone bodies

84
Q

what process are ketogenic amino acids important force

A

ketogenesis

85
Q

what process are glucogenic amino acids importatnt for

A

gluconeogenesis

86
Q

glucogenic amino acids are comprised of …

A

most essential and non essential amino acids

87
Q

ketogenic amonos include exclsuively

A

leucine and lysine

88
Q

what hormones increase protein synthesis

A

growth homrone
insulin
testosterone
thryoxine sometimes

89
Q

explain grouth hormones affect on protein

A

increases protein synthesis

unsure what mecanism ,guess is to increased AA transprot

90
Q

explain insulin effect on protein

A

increases protein syntheisis

unknpwn ,AA transprot

91
Q

explain cortisol/glucocorticorids effect on protein

A

causes protein breakdown

breakdowb of extraheptatic tissue proteins

92
Q

explain testosterone

A

increases protetin synthesis

93
Q

explain thyroxine effect on protein

A

no directi effect
if CHO are depleted: increased proteolysis, icnrease metabolism
If CHO are adequate: increased protein synthesis

258: Physiology (25 decks)

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