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Block 3; Week 5 Michelle > TBL Prep > Flashcards

TBL Prep Flashcards

1
Q

What are the essential amino acids?

A 
HILL My PT TV
Histidine
Isoleucine
Leucine
Lysine
Methionine
Phenylalanine
Threonine
Tryptophan
Valine
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2
Q

What is the weird reason that we need amino acids?

A

substrate for heme, purine, pyrimidine, melanin

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3
Q

What are the 5 important cofactors in amino acid metabolism?

A
  1. THF
  2. SAM
  3. Biotin
  4. THB
  5. Pyridoxal Phosphate (PLP)
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4
Q

Where is THF from? What does it do?

A

synthesized by bacteria

transfers single carbons

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5
Q

How is SAM synthesized?

A

Synthesized from ATP & Methionine

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6
Q

What does SAM do?

A

transfers methyl groups

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7
Q

What does biotin do?

A

transfers CO2

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8
Q

What is THB involved in?

A

tyrosine synthesis
involved in oxidation reaction
Remember: “think outside the BOX”

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9
Q

What does PLP do? What types of reactions is it involved in? What is it a coenzyme for?

A

holds nitrogen–>how cute
involved in transaminase reaction
coenzyme for vitamin B6

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10
Q

Once again, what are the energy results of the TCA cycle?

A

3 NADH=9 ATP
1 GTP=1 ATP
1 FADH2=2 ATP

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11
Q

Which enzyme of TCA is bound to the inner mitochondrial membrane?

A

succinate dehydrogenase

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12
Q

What part of the TCA cycle does excess EtOH feed in to? How?

A

Acetyl CoA!

EtOH–>Acetaldehyde–>acetic acid–>acetyl CoA

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13
Q

What are the 2 effects of excess citrate? Where does it go?

A

Gets out of the mitochondria and inhibits glycolysis & goes into Fatty Acid Synthesis.

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14
Q

What is the reaction for the synthesis of glutamate?

A

alpha-KG + NH4+ + NADPH–>Glutamate +NADP+ + H2O

Enzyme: glutamate dehydrogenase

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15
Q

When does the synthesis of glutamate occur? When does it occur?

A

when there are toxic amount of ammonia, mainly in the liver…

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16
Q

What is the reaction for the formation of glutamine?

A

Glutamate + ATP + NH3–>Glutamine

Enzyme: glutamine synthetase

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17
Q

What is the reaction for the formation of glutamate from glutamine?

A

Glutamine –> Glutamate + NH4+

Enzyme: glutaminase

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18
Q

How is non-toxic version of ammonium transferred around?

A

thru glutamine

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19
Q

What is the most abundant circulating AA?

A

glutamine!

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20
Q

Glutamine is _____ donor in many ____ reactions.

A

nitrogen donor

many synthesis reactions

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21
Q

Which of the following can move across a cell membrane:
glutamine
glutamate?

A

glutamine!!

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22
Q

What is the reaction for making alanine?

A

Pyruvate + AA –>Alanine + alpha keto acid

Enzyme: ALT: alanine transaminase

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23
Q

T/F Transaminases are used in irreversible reactions.

A

FALSE

they are reversible reactions, highly reversible

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24
Q

What cofactor do all transaminases require?

A

PLP found in Vitamin B6

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25
Q

Which enzyme’s levels are checked if you suspect liver damage?

A

ALT

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26
Q

What is the reaction for the formation of aspartate?

A

OAA + Glutamate–>Aspartate + alpha KG

Enzyme: GOT: glutamate-OAA transaminase

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27
Q

What is the reaction for the formation of asparagine?

A

Aspartate + ATP + Glutamine–>Asparagine + Glutamate

Enzyme: Asparagine Synthetase

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28
Q

Is there a reverse reaction for asparagine? If so, what is it?

A

YES, glad you asked.
Asparagine –> Aspartate + NH4+
Enzyme: asparaginase

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29
Q

Leukemia patients are sometimes unable to synthesize _____. Thus, _____ is sometimes used as a treatment.

A

asparagine

asparaginase is used as a treatment

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30
Q

Asparagine is often ________.

A

glycosylated

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31
Q

What is an enzyme that humans don’t express involved in AA synthesis?

A

asparaginase

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32
Q

What is the reaction for the formation of serine?

A

3PG + Glutamate –> Serine + alpha KG + NADH

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33
Q

What is the reaction for the formation of glycine?

A

Serine + THF–> Glycine

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34
Q

What is the reaction for the formation of methionine?

A

Homocysteine + methyl-THF –> Methionine + THF

uses Vit B12

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35
Q

How do you make homocysteine?

A

via Met + ATP–>SAM–>SAHcys–>Homocysteine

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36
Q

What is the intermediate b/w homocysteine & Cysteine?

A

cystathionine

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37
Q

Which AA must be added in to make cystathionine?

A

Serine!

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38
Q

How do you make cystathionine?

A

Homocysteine + Serine –> Cystathionine
Enzyme: Cystathionine Synthase
Requires: PLP

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39
Q

How do you make cysteine from cystathionine?

A

Cystathionine –> Cysteine
Enzyme: cystathionase
Requires: PLP

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40
Q

What causes homocystinuria? What are the effects of this condition? What are its treatments?

A 
deficiencies in cystathionine synthase
or cystathionase
mental deficiency
vascular thrombosis
thinning & lengthening of long bones
osteoporosis
Treatments: dietary, vitamin
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41
Q

What is the reaction for the formation of tyrosine?

A

Phenylalanine + THB–>Tyrosine + DHB

Enzyme: Phenylalanine hydroxylase

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42
Q

What does tyrosine go on to form? Which enzyme is required for this to happen?

A

goes on to form melanin

Enzyme: tyrosinase

43
Q

Once THB–>DHB how do you renew it again?

A

DHB–>THB
Requires: NADH
Enzyme: DHB reductase

44
Q

What happens when you have too much phenylalanine?

A

You get formation of phenylketones

Then you can get PKU

45
Q

What are the symptoms of PKU? What are the treatments?

A

Symptoms: mental retardation, light skin color
Treatments: dietary, no aspartame

46
Q

What is proline made from? What feed in does it require?

A

made from glutamate

requires NADH

47
Q

What types of ubiquination make for urgent degradation?

A

longer chains

48
Q

What type of ubiquination makes for fast degradation?

A

when the N-terminus has destabilizing things
LADS are FAST
leucine
arginine

49
Q

What type of ubiquination makes for slow degradation?

A

when the N-terminus has stabilizing things
PMS makes you SLOW
proline
methionine

50
Q

What causes Alzheimer’s & Parkinson’s?

A

formation of protein structures in neurons

51
Q

What causes cystic fibrosis?

A

rapid degradation of chloride channels

52
Q

What causes Liddle’s Syndrome? What is the significance of this?

A

the sodium channel that is inserted into the nephron isn’t degraded…
this leads to excess sodium absorption
this causes early-onset HTN

53
Q

What 2 things cause negative nitrogen balance?

A

stress hormones

cytokines

54
Q

Which 3 types of people will have a positive nitrogen balance?

A

children
pregnant women
body builders

55
Q

What is nitrogen balance?

A

Nitrogen balance is when Nitrogen Intake = Nitrogen loss

56
Q

What defect leads to oxaluria type I?

A

a deficiency of glycine transaminase

Can’t take glyoxylate–>glycine

57
Q

What defect leads to nonketotic hyperglycinemia?

A

A lack of glycine cleavage enzyme

Can’t break down glycine!

58
Q

What defect leads to homocystinuria?

A

A lack of cystathionine synthase
Can’t make cysteine
get a buildup of homocysteine

59
Q

What enzyme deficiency leads to PKU?

A

phenylalanine hydroxylase

60
Q

What causes tyrosinemia type II?

A

a defect in tyrosine aminotransferase

61
Q

What causes tyrosinemia Type I?

A

a defect in fumarylacetoacetate hydroxylase

get a buildup of an intermediate instead of fumarate!

62
Q

WHat cause alkaptonuria?

A

deficiency in homogentisate oxidase

get a buildup of an intermediate instead of fumarate

63
Q

What causes histidinemia?

A

a deficiency of histidase

64
Q

What intermediate accumulates w/ a folate deficiency?

A

FIGLU

formimino glutamic acid

65
Q

What defect leads to methylmalonic aciduria?

A

a defect in methylmalonyl CoA mutase

can’t make succinyl CoA

66
Q

What causes maple syrup urine disease?

A

a deficiency of branched chain alpha keto acid dehydrogenase complex

67
Q

How do you degrade branched AA?

A

transamination & then oxidative decarboxylation

68
Q

What are some examples of breakdown products of branched AA catabolism?

A

propionyl CoA
Acetyl CoA
Acetoacetate

69
Q

Which AA are catabolized in the intestinal mucosal cells?

A

glutamate

glutamine

70
Q

Where are most AA metabolized?

A

in the liver

71
Q

How are branched chain AA metabolized?

A

they leave the liver & go to muscle for the transamination reaction; then they return to the liver for oxidative decarboxylation

72
Q

What is the major source of AA during fasting?

A

muscle protein!

73
Q

2 AA go to glucose thru gluconeogenesis during fasting…which AA? Where do they go to do this?

A

glutamine–>kidneys & intesines

alanine–>liver

74
Q

In the degradation of phenylalanine…what bad things can happen? What accumulates in each case?

A

deficiency of phenylalanine hydroxylase
deficiency of DHB reductase
**In both cases: phenylalanine accumulates

75
Q

What condition does a deficiency of phenylalanine hydroxylase cause? What are the symptoms?

A

PKU (classical)

Mental Retardation

76
Q

What condition does a deficiency of DHB reductase cause?

A

PKU (non-classical)

Mental Retardation

77
Q

In the degradation pathway of tyrosine…what can go wrong? What accumulates in each case?

A

a deficiency of homogentisate oxidase (homogentisate acid)
a deficiency of fumarylacetoacetate hydroxylase (fumarylacetoacetate)
a deficiency of tyrosine aminotransferase (tyrosine)

78
Q

What condition does a deficiency of homogentisate oxidase & an accumulation of homogentisate acid cause? What are the symptoms?

A

Alcaptonuria
black urine
arthritis

79
Q

What condition does a deficiency of fumarylacetoacetate hydroxylase & an accumulation of fumarylacetoacetate cause? What are the symptoms?

A

Tyrosinemia I
Liver Failure
Early Death

80
Q

What condition does a deficiency of tyrosine aminotransferase and an accumulation of tyrosine cause? What are its symptoms?

A

Tyrosinemia II

neurological defects

81
Q

In the degradation of methionine…what can go wrong? What accumulates?

A

a deficiency of cystathionase (cystathionine)

a deficiency of cystathionine synthase (homocysteine)

82
Q

What condition does a deficiency of cystathionase & an accumulation of cystathionine cause? What are its symptoms?

A

Cystathionuria

Benign

83
Q

What condition does a deficiency of cystathionine synthase & an accumulation of homocysteine cause? What are its symptoms?

A

homocysteinuria

cardiovascular & neurologic problems

84
Q

In the degradation of glycine…what can go wrong? What accumulates?

A

a deficiency of glycine transaminase (glyoxylate)

a deficiency of glycine cleavage enzyme (glycine)

85
Q

With a deficiency of glycine transaminase & an accumulation of glyoxylate…what condition results? What are its symptoms?

A

Primary Oxaluria Type I

Renal failure w/ stone formation

86
Q

What condition is caused by a deficiency of glycine cleavage enzyme & an accumulation of glycine? What are its symptoms?

A

Hyper Glycinemia

Mental Retardation

87
Q

In the degradation of branched AA what can go wrong & what accumulates?

A

a deficiency of branched chain alpha keto acid dehydrogenase (alpha keto acids)

88
Q

What condition is caused by an accumulation of alpha keto acids? What are its symptoms?

A

Maple Syrup Urine Disease

Mental Retardation

89
Q

What are the 3 branched chain AA?

A

LIV:

Leucine, Isoleucine, Valine

90
Q

What is the purpose of the urea cycle?

A

to get rid of NH4+, which is a neurotoxin.

91
Q

What happens to urea in the case of renal failure?

A

the BUN (urea in the blood) rises sharply: called uremia

92
Q

How can urea cause kidney stones?

A

a bacteria enzyme in the urine can cleave urea…this has 2 effects: alkalinizing the urine & precipitating out magnesium ammonium phosphate

93
Q

If you have an inherited deficiency of some of the urea cycle enzymes…what happens?

A

Hyperammonemia & Encephalopathy

lethargy, vomiting, irritability

94
Q

During failure of the urea cycle…why do you have ATP deficiencies?

A

alpha KG is converted into glutamine

95
Q

What is the therapy for urea cycle enzyme deficiencies?

A

limit protein intake
remove excess ammonia
replace urea cycle intermediates
maybe liver transplant

96
Q

What is the first step in the urea cycle? Where does it occur?

A

Liver, mitochondrial matrix
NH4+ + 2ATP + CO2–>Carbamoyl Phosphate
Enzyme: carbamoyl phosphate synthetase I

97
Q

What does a buildup of carbamoyl phosphate do?

A

leads to orotate in your urine

98
Q

Once you have carbamoyl phosphate in the mitochondrial matrix of the liver…what is the next step?

A

Ornithine combines w/ carbamoyl phosphate in the mitochondrial matrix to make citrulline.
Enzyme: ornitine transcarbamylase

99
Q

What do you do with your citrulline?

A

Citrulline + ATP + Aspartate–>Arginosuccinate

Enzyme: Arginosuccinate Synthetase

100
Q

Where did you get the aspartate for the last step?

A

From the TCA cycle? It was shoved into the cystol from the mitochondrial matrix…

101
Q

After you have arginosuccinate…what is the next step?

A

Arginosuccinate–>Arginine + Fumarate

Enzyme: Arginosuccinate Lyase

102
Q

What happens to the fumarate you just threw off?

A

It is converted into malate & shunted back into the mitochondrial matrix to become a part of the TCA cycle.

103
Q

Now that you have arginine…what happens?

A

Arginine–>Ornithine & kicks off a urea
Enzyme: arginase
**note the ornithine will go & combine w/ the carbamoyl phosphate…

104
Q

HOw many ATP does one urea cycle require?

A

4 ATP

Block 3; Week 5 Michelle (5 decks)

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