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mcm > Protein and AA Metabolism > Flashcards

Protein and AA Metabolism Flashcards

1
Q

AA pools come from many different places

A
  1. body proteins
  2. dietary proteins ***most come from
  3. synthesized non AA
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2
Q

AA pools are supplied from

A
  1. Food we eat
  2. protein turnover
  3. de novo synthesis
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3
Q

AA are depleted by

A
  1. creation of nitrogen containing products
  2. creation of body proteins
  3. degradation to enter different metabolic pathways or urine
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4
Q

What happens to a majority of the non recoverable AA?

A

excreted in urine

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5
Q

Defects in AA resportion will cause

A
  1. Hartnups Dz

2. Cystinuria

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6
Q

Exopeptidases

A

attack at the C- or N- (aminopeptidase) terminus

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7
Q

Endopeptidase

A

attacks with the protein at a specific site by breaking internal peptide bonds

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8
Q

__________ is a SELECTIVE method of intracellular proteolytic control

A

lysosome/autophagy system

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9
Q

NON-SELECTIVE methofs of intracellular proteolytic control

A
  1. macroautophagy
  2. microautophagy
  3. Chaperonin mediated autophage
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10
Q

Proteosomal degradation

A

large proteosomes cleave polyubiquitinated proteins.

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11
Q

is proteosomal degradation selective?

A

Yes. Because they must be tagged with Ubiquitin.

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12
Q

How does ubiquiton tag a protein?

A

It needs a carrier protein so that it can tag it.

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13
Q

Method of ubiquitation:

A
  1. [ubiquiton ligase] will bind to the protein
  2. signals [ubqition carrier] to come and drop off UB.
  3. More are brought over
  4. the proteosome will now recognize for degradation
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14
Q

Proteosomes are located in

A

cytoplasmic

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15
Q

do proteolyitic enzymes roam around our body?

A

YES. they roam around our body as zymogens

they’re activated via proteolytic cleavage

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16
Q

Essential AA

A 
Phenylalanine
Valine
Trp
Threonine
Isoleucine
Methionine
Histidine
Argining
Lysine
Leucine
*glutamine
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17
Q

At certain times, ____ and ____ can be considered essential

A

glutamine

arginine

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18
Q

ketogenic AA (7)

A

Lysine and leucine

IPTT

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19
Q

Both ketogenic and glucogenic (5)

A

IPTTT(all of the ones that begin with T)

Isoleucine
Phe
Truptophan
Threonine
Tyrosone
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20
Q

There are ____ glucogenic AA

A

18.

13 true glucogenic
then there are 5 that can be both (IPTTT)

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21
Q

OAA can make what AA

A

aspartate

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22
Q

Aspartate can make what AA

A

Asparagine
methionine
Threonine
Lysine

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23
Q

DIRECT biosynthetic precursor of isoleucine

A

threonine

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24
Q

Pyruvate makes which AA?

A

Alanine
valine
leucine

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25
Q

R5P can make

A

histidine

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26
Q

Alpha keto glutarate can make

A

Glu–> Glu, Arg, Pro

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27
Q

3-phosphoglycerate can make

A

Serine

Serine can then make cysteine and glycine

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28
Q

What makes cysteine and glycine?

A

Serine will make both cysteine and glycine

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29
Q

Proteoylsis

A

the degradation of proteins so that they can be absorbed.

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30
Q

Proteins that are misfolded will be discarded in wha tways

A
  1. microautophagy
  2. macroautophagy
  3. chaperonin assisted autophagy
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31
Q

How do we activate trypsinogen

A

enterokinase will convert trypsinogen–> tryspin

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32
Q

Howe do we activate chymotrypsinogen

A
  1. First, we active trysinogen using enterokinase

2. trypsin that is made will then come and active chymotrypsinogen

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33
Q

What is the P and T in PVT TIM HALL

A

Phenylalanine

Tryptophan and Threonine.

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34
Q

What is transanimation?

A

Transanimation is the shuffling of amine groups

an amino group is transferred to a keto-acid.

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35
Q

What kinds of enzymes facilitate transanimations?

A

transaminases

aminotransferases

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36
Q

Transaminases require what co-enzyme?

A

PLP

pyridoxyl-5-phosphate

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37
Q

PLP is a derivative of what?

A

vitamine b6

38
Q

____ and ___ are tests of liver function. They must have coenzyme ____

A

ALT- alanine transaminase
AST- aspartate transaminase

PLP (pyridoxyl-5-phosphate.

39
Q

Metabolism of Gln, Glu, Arg, Pro, and His

A

They are all converted to Glu.

Glu is converted alpha ketoglutarate in 3 ways

40
Q

What 3 ways are Glu converted to alpha ketoglutarate?

A
  1. Release NH4+ via oxidative deamination by glutamate DH
  2. Transfer amino group to [pyruvate] by ALT
  3. Transfer amino group to [OAA] by AST
41
Q

Gln–> glutamate loses a amino group because of what?

A

nitrogen trap method.

42
Q

What is PLP

A

pyridoxyl 5 phosphate.

It is a coenzyme for transaminases.

It is a derivative of vitamin b6

43
Q

Methionine is converted to _____ and eventually _______.

A

Methionine is converted to HOMOCYSTEINE and eventually succinyl co-A

44
Q

Homocysteinuria

A

Homocystinuria occurs when there is a buildup of homocysteine

45
Q

Homocysteinuria is due to

A
  1. defect in cystathione B synthase (an enzyme that needs PLP)
  2. vita B6, B12 and folic acid deficiencies
46
Q

Defects in cystathione b synthase can cause

A

homocystenuria.

47
Q

what happens if we have a deificieny in PLP

A

defects in PLP can worsen the problem and cause hyperhomocysteinuria, when homocysteine is present in urea.

we will be unable to make cysteine

48
Q

most affected organs of homocysteineuria

A

eye
skeletal muscle
CNS
vascular

49
Q

How is threonine, valine and isoleucine broke down?

A

propionyl coA–> methylmalonyl coA–> succinyl coA

similar to how odd number chain FA are broken down!!!

50
Q

What are the BCAA (branch chain AA)?

A

Valine
Isoleucine
Leucine

51
Q

What are different about branch chain AA?

A

Valine, isoleucine and leucine.

Branch chain AA cannot be metabolized in the liver because there is no aminotransferase.

Instead, they are broken down in the muscle, kidney and brain.

52
Q

What AA enter the TCA cycle at succinyl coA?

A

TIM V

Threonine
Isoleucine
Methionine
Valine

53
Q

When are BCAAs used for NRG?

A

BCAAs are used for energy during prolonged exercise or fasting

54
Q

Maple Syrup Disease

A

Maple syrup disease occurs when we have a defective BCKD.

As a result, BCAAs (valine, isoleucine and leucine) will appear in the urine and cause a syrupy smell.

55
Q

_______________ is high in the jewish and amish population

A

Maple syrup dz

56
Q

Phenylalanine is converted to _______ via ______________

A

Phe is converted to Tyrosine via phenylalanine hydroxylase

57
Q

What enzyme converts Phe to Tyrosine?

A

Phenylalanine hydroxylase

58
Q

What happens when phenylalanine hydroxylase is not working?

A

when phenylanine hydroxylase is not working,

we will have a buildup of Phe. Phe is then broken down to phenylacetate and phenylactate

59
Q

Phenyllactate will cause

A

smelly urine

60
Q

Phenylacetate will cause

A

disruption of neural transmission

61
Q

if you have PKU; you should avoid

A

Phe,

because you cannot process it.

62
Q

What enters the TCA cycle at fumurate?

A

Phe
Tyrosine
Asp

63
Q

What enters the TCA cycle at OAA?

A

Asn

Asp

64
Q

Why is tryptophan so important

A

it makes serotonin, which makes melatonin (sleep)

65
Q

high amounts of _____ is indicative of carcinoid tuumors

A

serotonin

66
Q

What AA derivates makes serotinin and melatonin

A

Trp

67
Q

Tyrosine is important because it particpates in the production of

A

thyroid hormones, DA, NA, Epi

68
Q

If tyrosine hydrolase is inhibited, what happens?

A

we will have deficits in DA, NA and EPi

69
Q

What enzyme converts tyrosine to DA, EPI and NE

A

Tyrosine hydroxylase

70
Q

Parkinsons

A

deficit in DA because of mutation in tyrosine hydroxylase

71
Q

Albanism

A

Albanism is caused by a deficit in tyrocinase, the enzyme that converts tyrosine–> melanin

72
Q

What enzyme converts _______ to melanin?

A

tyrocinase converts tyrosine to melanin

73
Q

______ is a protein made by the thyroid to help with the production of T3 and T4

A

thyroglobulin

74
Q

How can we treat pts with hyperthyroidism?

A

We give patients carbimazole or polythiouracil, which blocks the iodination of thyroglobin to decrease amounts of T3 and T4

75
Q

How do we remove ammonia (NH3) in the brain?

A

Ammonia is removed as Glu and Gln in the brain using [glutamine synthase]

76
Q

What enzyme removes ammonia in the brain

A

glutamine synthase

77
Q

How do we remove ammonia from all other tissue besides the brain?

A

Gln and alanine

78
Q

do we excrete NH3 or NH4

A

NH4

79
Q

Removal of excess NH4 from the brain

A

in the brain:

we have alpha ketoglutarate (ammonium joins)–> Glu (NH3)–> Gln (via glutamine synthase)

leaves the brain and goes to the liver

Gln is processed and NH4 is released

80
Q

Removal of excess NH4 from the muscle

A

RMBR from the muscle it is removed as Ala and Glu

  1. Glucose–> pyruvate in glycolysis
  2. A transanimation reaction will transfer the amino group to alanine

Ala will then go to the liver and a transmino reeaction will cause the NH4 to be released

81
Q

What is a transanimation

A

the transfer of an AA from an alpha AA to a alpha ketoacid

82
Q

What are 2 byproducts of processing AA?

A

ornithine and citrulline

83
Q

Ammonia toxicity

A

excess ammonia because of liver failure or urea cycle disorder.

This is bad because ammonia is very toxic and can permeate membranes. NH4 cannot

84
Q

Ammonia toxicity can cause what?

A
  1. mitochondria dsfx
  2. deplete our glutamate (so no GABA)
  3. pH imbalance leading to swelling of astrocytes in the braing, leading to edema nad HTN
85
Q

What is phosphocreatine

A

the nrg storage in our muscle

86
Q

What is phosphocreatine made up of

A

3 AA:

arginine,
glycine and methionine

87
Q

How is phosphocreatine made

A
  1. in the kidney:
    arginine joins glycine to form guanidinoacetate
  2. In the liver
    methionine will joing guanidinoacetate to form CREATINE!
  3. Creatine is phosphorylated via creatine kinase to make creatine phosphate. .
88
Q

What is the ready to go protein NRG in the muscle?

A

creatine phosphate

89
Q

Do we keep all of our creatine phosphate?

A

no. a small amount of it is converted to creatinine and excrteted in our urine

90
Q

How can we test for kidney dysfunction and muscle degeneration?

A

elevated levels of creatinine in the urine.

91
Q

What enters succinyl coA?

A

Threonine
Iso
Met
Valine

Threonine, met and val are all processed the same way.

met–> homocysteine and eventually succinyl coA

mcm (12 decks)

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