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Biochem 2 > Protein Metabolism (mini-test 2) > Flashcards

Protein Metabolism (mini-test 2) Flashcards

1
Q

What percent of our bodies energy comes from AA oxidation?

A

10-15% (even more if starving)

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2
Q

Amino acids undergo oxidative degradation under 3 different situations. What are they?

A

1) normal recycling of cellular proteins
2) protein rich diet (AAs cannot be stored)
3) during starvation or in uncontrolled DM, AAs are used for fuel (ATP production) or for gluconeogenesis

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3
Q

Dietary proteins are absorbed during….

A

Digestion

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4
Q

What are the 2 instances of tissue proteins getting degraded?

A

1) proteins are old
2) starvation

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5
Q

What enzyme is used to synthesize tissue proteins from AAs?

A

Peptidotransferase

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6
Q

Which AAs can be synthesized by the body?

A

The 10 nonessential AAs

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7
Q

Eating lots of dietary proteins will help build muscle if the person exercises and has physical demands, but if not, then the body will break down the protein through deamination rather than becoming tissue protein. So this will generate lots of urea and can turn to ATP, but if ATP is enough then it will change to….

A

Fat

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8
Q

What makes up a general AA?

A

Amino group, R group, carboxyl group, H, and alpha carbon

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9
Q

What is transamination?

A

Transfer of amino group from AA to an alpha keto acid

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10
Q

What is deamination?

A

Removal of amino group from AA, which creates alpha keto acid and the amino group becomes ammonia

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11
Q

Why are AAs not the preferred energy source?

A

Bc breaking down AAs creates ammonia which is a toxic compound and can only be processed in the liver

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12
Q

Ammonia is a converted to what in the liver to be excreted through kidneys in the urine?

A

Urea

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13
Q

Alpha keto acids will be used to build up what 3 things?

A

1) glucose (through gluconeogenesis)
2) make ATP in TCA
3) ketone bodies (fasting state)

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14
Q

AAs within the AA pool can undergo decarboxylation. What is this?

A

Carboxyl group of AA is removed and the AA is now known as an amine

Ex: glutamate is a neurotransmitter activator and after decarboxylation it becomes GABA which is an amine

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15
Q

AAs within the AA pool of the body can become biologically active compounds like….

A

Neurotransmitters and hormones

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16
Q

Deamination is done with what enzyme?

A

Glutamate dehydrogenase

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17
Q

Removing the amine group of an AA is called….

A

Deamination

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18
Q

Where does deamination occur?

A

In the liver

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19
Q

T/F: any tissue besides the liver cannot do deamination

A

TRUE, so muscles and other tissues only do transamination

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20
Q

Does transamination synthesize ammonia?

A

NO

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21
Q

Is transamination reversible or irreversible?

A

Reversible

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22
Q

Which AA cannot be transaminated?

A

Lysine

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23
Q

ALL aminotransferases use a coenzyme. What is it and what is it derived from?

A

Pyridoxal phosphate, which is derived from, vit B6

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24
Q

What are the 3 aminotransferase pairs we should know?

A

1) alpha KG and glutamate
2) pyruvate and alanine
3) aspartate and OAA

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25
Q

If alanine donates NH2 to alpha KG what enzyme is used and what are the products?

A

Enzyme= glutamate pyruvate aminotransferase (GPT) OR alanine aminotransferase (ALT)

Products= pyruvate and glutamate

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26
Q

What vitamin is required with ALT, AST, GPT, or GOT?

A

Vit B6

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27
Q

If aspartate donates NH2 to alpha KG, what enzyme is used and what are the products?

A

Enzyme= glutamate OAA aminotransferase (GOT) or aspartate aminotransferase (AST)

Products= OAA and glutamate

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28
Q

The alanine cycle begins in the muscles with pyruvate. Pyruvate will undergo transamination and become what?

A

alanine

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29
Q

The alanine cycle begins in the muscles with pyruvate. Pyruvate will undergo transamination and become alanine. Alanine will be transported out of the muscle to blood and then to the liver. From here, alanine will convert back to pyruvate, while an alpha KG can undergo transamination here at the same time and make glutamate. Glutamate is the collecting point. Glutamate will undergo deamination to make ammonia and urea with what enzyme?

A

glutamate DH

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30
Q

In muscle tissues, alpha KG can undergo transamination and become glutamate. Glutamate is too acidic to be transported in the blood so it first has to convert to glutamine. What enzyme does this?

A

glutamine synthetase

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31
Q

In muscle tissues, alpha KG can undergo transamination and become glutamate. Glutamate is too acidic to be transported in the blood so it first has to convert to glutamine. From here glutamine will be transported out of the muscles to blood and then to liver. Glutamine will then change back to glutamate (collecting point) + NH3 with what enzyme?

A

glutaminase

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32
Q

What 2 AAs can be transported in the blood and are the major transport form of NH3?

A

alanine and glutamine

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33
Q

When is the alanine cycle most active?

A

starvation

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34
Q

Glutamate and ammonia undergo a reaction with glutamine synthetase to make glutamine. What does it require?

A

2 ATP

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35
Q

Glutamate is the collecting point of….

A

ALL amine groups removed from AAs

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36
Q

Deamination is what type of reaction?

A

oxidative deamination reaction

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37
Q

What does glutamate use to make alpha KG with glutamate DH?

A

NAD+ or NADP+

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38
Q

Urea is a _____________ waste product

A

nitrogenous

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39
Q

Urea is generated in the urea cycle. Where is the urea cycle?

A

mitochondria and cytosol of liver

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40
Q

Urea cycle occurs in the mitochondria and cytoplasm of the liver. What is the only other pathway that is here?

A

gluconeogenesis

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41
Q

Where do the 2 nitrogens come from in urea?

A

1) oxidative deamination of glutamate
2) aspartate

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42
Q

Where does the carbon come from in urea?

A

from the CO2 that was generated in TCA

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43
Q

In the urea cycle, step 1 is in the mitochondria and this is where NH4+ and CO2 combine with __________________________________ to generate carbomoyl phosphate

A

carbamoyl phosphate synthetase I (CPS1)

note: 2 ATP is required for this step

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44
Q

What is the RLE in the urea cycle?

A

carbamoyl phosphate synthetase I (CPS1)

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45
Q

What is the rate limiting step in the urea cycle?

A

step 1

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46
Q

What 2 urea cycle enzymes are in the mitochondria?

A

1) carbamoyl phosphate synthetase I (CPS1)
2) ornithine transcarbamoylase (OTC)

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47
Q

In the urea cycle, step 2 is still in the mitochondria. Ornithine is combined with carbamoyl phosphate by ________________________________ to generate citrulline. Citrulline is then transported into the cytoplasm of the liver

A

ornithine transcarbamoylase (OTC)

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48
Q

What are 2 nonstandard AAs that are also VIP molecules in the urea cycle?

A

1) ornithine (smaller)
2) carbamoyl phosphate (larger)

49
Q

In step 3 of the urea cycle, it is now in the cytoplasm. Citrulline is condensed with aspartate by ______________________________ to create argininosuccinate.

A

argininosuccinate synthetase

note: 2 ATP are required here and the hydrolysis of ATP to AMP DRIVES THIS RXN

50
Q

What are the 3 basic AAs?

A

1) lysine
2) arginine
3) histidine

51
Q

In step 4 of the urea cycle, ______________________ cleaves argininosuccinate to form fumarate (which can enter the TCA cycle) and arginine

A

argininosuccinate lyase

52
Q

In step 5 of the urea cycle, _______________ cleaves arginine to release urea and regenerate ornithine. Ornithine re-enters the mitochondria for further urea cycle rounds. Urea passes into the blood and is excreted by the kidneys

A

arginase

53
Q

How many ATPs are required for 1 round of urea cycle?

A

4

54
Q

What 2 enzymes in urea cycle require 2 ATP (4 in total with both enzymes)?

A

1) carbamoyl phosphate synthetase I (CPS1)
2) argininosuccinate synthetase (ASS)

55
Q

T/F: the body does not like using AAs for energy

A

true

56
Q

What 2 organs have to work hard bc of urea cycle?

A

liver and kidneys

57
Q

What does BUN stand for?

A

blood urea nitrogen

58
Q

What does increased BUN indicate?

A

kidney dysfunction (kidneys are unable to excrete waste products)

59
Q

What markers indicate liver damage (cannot form urea)?

A

1) increased ALT or AST
2) decreased BUN

60
Q

What are the 10 essential AAs?

A

-phenylalanine
-valine
-threonine
-tryptophan
-isoleucine
-methionine
-histidine
-arginine
-leucine
-lysine

PVT TIM HALL

note: this is only in a positive nitrogen balance (growth in kids or pregnant moms, recovery after injury or surgery, etc)

Otherwise there are 8 essential AAs (his and arg are conditionally essential)

61
Q

Which 8 AAs are essential all the time?

A

-phenylalanine
-valine
-threonine
-tryptophan
-isoleucine
-methionine
-leucine
-lysine

62
Q

Which 2 AAs are conditionally essential, only during positive nitrogen balance?

A

histidine and arginine

63
Q

What is the allosteric activator for carbamoyl phosphate synthetase I (CPS1) in step 1 of urea cycle?

A

N-acetylglutamate (it indicates a buildup of glutamate and amino groups, so its time to make urea)

64
Q

AAs can be glucogenic, ketogenic, or both. What is the fate of the carbon skeletons for glucogenic AAs?

A

will become glycolytic or TCA cycle intermediates

65
Q

AAs can be glucogenic, ketogenic, or both. What is the fate of the carbon skeletons for ketogenic AAs?

A

will become acetyl CoA or acetoacetate

66
Q

18 of the standard AAs are glucogenic, and 2 are ketogenic. Which 2 AAs are ketogenic?

A

leucine and lysine (so these are the only 2 standard AAs that CANNOT change to glucose)

67
Q

18 of the standard AAs are glucogenic, and 2 are ketogenic. BUT, 4 are both ketogenic and glucogenic. What are these 4 AAs?

A

1) tyrosine
2) isoleucine
3) phenylalanine
4) tryptophan

PITT

68
Q

What are the 3 branch chain AAs (BCAAs)?

A

1) valine
2) leucine
3) isoleucine

69
Q

What 2 BCAAs can change to glucose?

A

valine and isoleucine

70
Q

Which 2 BCAAs can change to ketone bodies?

A

leucine and isoleucine

71
Q

Ala carbon skeleton will be converted to…

A

pyruvate

72
Q

Arginine carbon skeleton will be converted to…

A

alpha KG

73
Q

Asparagine carbon skeleton will be converted to….

A

aspartate and then OAA

74
Q

Cysteine carbon skeleton will be converted to…

A

pyruvate

75
Q

Glutamine carbon skeleton will be converted to…

A

glutamate and then alpha KG

76
Q

Glycine carbon skeleton will be converted to…

A

pyruvate

77
Q

Proline carbon skeleton will be converted to…

A

alpha KG

78
Q

Histidine carbon skeleton will be converted to…

A

alpha KG

79
Q

Methionine carbon skeleton will be converted to…

A

SCoA or

homocysteine which can then be converted to cysteine and then back to methionine

80
Q

Threonine carbon skeleton will be converted to…

A

SCoA

81
Q

Valine carbon skeleton will be converted to…

A

SCoA

82
Q

Isoleucine carbon skeleton will be converted to…

A

SCoA

83
Q

Phenylalanine carbon skeleton will be converted to…

A

tyrosine and then fumarate

84
Q

What enzyme converts phenylalanine to tyrosine?

A

phenylalanine hydroxylase

85
Q

Tryptophan carbon skeleton will be converted to…

A

pyruvate

86
Q

Serine carbon skeleton will be converted to…

A

pyruvate

or

cystiene

or

glycine and then heme or collagen

87
Q

AAs can change to what 4 TCA intermediates?

A

SOFA

1) succinyl CoA (SCoA)
2) OAA
3) fumarate
4) alpha KG

and some AAs can change to pyruvate

88
Q

Asparagine (Asn) will be converted to aspartate. Aspartate (Asp) and alpha KG will undergo reaction with _______ to make OAA

A

AST

89
Q

What 2 AAs can make OAA?

A

Asn and Asp

90
Q

What 2 AAs can make fumarate?

A

Phe and Tyr

91
Q

What coenzyme is required to convert Phe to Tyr?

A

biopterin/ tetrahydrobiopterin (produced by humans from GTP)

92
Q

When Phe converts to Tyr and then to Fumarate, what is also made with fumarate?

A

acetoacetate

93
Q

What is PKU (phenyloketonuria)?

A

in normal situations phe should be able to convert to tyr but here patients are:

-deficient in phe hydroxylase
-causes mental retardation and odor in urine
-need to restrict phe intake
-need to completely avoid artificial sweeteners like aspartame because its asp + phe
-tyrosine is essential here

94
Q

What does tyrosine synthesize?

A

-pigment
-catecholamines
-thyroid hormones

95
Q

What enzyme converts tyrosine to melanin?

A

tyrosinase

96
Q

What is albinism?

A

-tyrosine cannot convert to melanin because theres a tyrosinase deficiency
-causes lack of pigmentation in the eyes, skin, and hair

97
Q

Tyrosine can be converted to homogentistate. Homogentistate can then be converted to fumarate with what enzyme?

A

homogentistate oxidase

98
Q

What is alcaptonuria?

A

in normal cases, Tyrosine can be converted to homogentistate. Homogentistate can then be converted to fumarate with homogentistate oxidase

but here, the enzyme is deficient so there will be an accumulation of homogentistate

this causes:
-black urine and bone disease
-joint pain, organ damage, kidney stones

tx:
-vit C supplementation
-restrict phe and tyr

99
Q

What are the 3 aromatic AA metabolic diseases?

A

1) PKU
2) albinism
3) alcaptonuria

100
Q

What 4 AAs can make succinyl CoA?

A

VITM

1) valine
2) isoleucine
3) threonine
4) methionine

these AAs go through VOMIT pathway- all the letters match up to AA, but O stands for odd chain FA bc the AAs will be broken down to propionyl CoA

101
Q

There are 4 AAs that can make succinyl CoA: valine, isoleucine, threonine, and methionine. This is the VOMIT pathway. They are first broken down to propionyl CoA and then are converted to methylmalonyl CoA with ___________________________. Methylmalonyl CoA is then converted to succinyl CoA with ____________________________

A

propionyl CoA carboxylase and ABC, methylmalonyl CoA mutase and vit B12

note: this is the exact same reactions that happens with odd chain FAs

102
Q

What vitamins are required to convert VITM (valine, isoleucine, threonine, and methionine) into succinyl CoA?

A

vit B7 (biotin) and B12

103
Q

Valine and isoleucine are BCAAs. After transamination, they become branch chain ketoacids. This can be further broken down with branch chain ketoacid DH. The products are then used to generate propionyl CoA. What coenzymes are required for branch chain ketoacid DH?

A

TLCFN

(same coenzymes that are required by pyruvate DH)

104
Q

Maple syrup urine disease is characterized by….

A

branch chain ketoacid DH deficiency

105
Q

Does leucine produce succinyl CoA?

A

NO

106
Q

What 2 AAs contain sulfur?

A

methionine and cysteine

107
Q

Methionine can be converted to S-adenosylmethionine (SAM) which is a….

A

carbon donor

108
Q

methionine can be converted to homo__________

A

cysteine

109
Q

What is maple syrup urine disease? What is the treatment?

A

-caused by branch chain alpha keto acid DH deficency
-causes ketoacids to build up in the urine which gives it a maple syrup smell

tx:
-strict diet with restricted protein but high carb
-thiamine supplements

110
Q

What is homocysteinemia? What is the treatment?

A

-increase of homocysteine in the blood
-associated with neuro and cardiovascular diseases
-could be due to enzyme deficiency (rare)
-usually due to vitamin deficiency with vit B6, B9 (folic acid), or B12

tx:
-restrict methionine intake
-vit B6, B9, and B12 supplements

111
Q

inadequate B12 and B9 (folate) may cause _____________ deficiency

A

methionine

112
Q

Met gets converted to SAM. SAM is a modified met and it donates methyl group to DNA. SAM is then converted to homocysteine. At this point homocysteine can convert back to methionine if theres adequate levels of….

A

vit B12 and B9 (folate)

113
Q

Met gets converted to SAM. SAM is a modified met and it donates methyl group to DNA. SAM is then converted to homocysteine. At this point homocysteine can convert back to methionine if theres adequate levels of vit B12 and B9 (folate). Another option is- homocysteine can make LDL (bad cholesterol). Or another option is homocysteine can be converted to cysteine and propionyl CoA (which will then be converted to succinyl CoA) if theres adequate….

A

serine and vit B6

114
Q

What are the 5 AAs that can make alpha KG?

A

PHAGG

1) proline (cyclic)
2) histidine (basic)
3) arginine (basic)
4) glutamine (neutral)
5) glutamate (acidic)

115
Q

What 5 AAs can make pyruvate?

A

G CAST

1) glycine
2) cysteine
3) alanine
4) serine
5) tryptophan

note: serine, glycine and cysteine are non-essential BUT they are very important for our health
-serine can be converted to cysteine and glycine
-glycine is needed to make collagen for bones, skin, hair and glycine also makes heme (not enough gly= can result in anemia)
-cysteine is an antioxidant bc of the thiol group

116
Q

Which enzyme is used with vit B6 and 9 to catalyze a reversible conversion of serine to glycine?

A

serine hydoxymethyl transferase

117
Q

Tryptophan is the largest AA and in order to make pyruvate, it is cleaved to liberate alanine and _________ group/ring

A

indole

118
Q

What are the products of catabolsim for ketogenic AAs?

A

acetoacetate or acetyl CoA

acetyl CoA can be used in TCA

note: only leucine and lysine are exclusively ketogenic

119
Q

Do ketogenic AAs use pyruvate as an intermediate?

A

no

Biochem 2 (13 decks)

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