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Block 3 Week 6 > TBL Amino Acid Metabolism > Flashcards

TBL Amino Acid Metabolism Flashcards

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1
Q

This is made in bacteria, it is the reduced form of folate and transfers single carbons

A

THF

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2
Q

This made from ATP and methionine and transfers methyl groups and makes SAhcys and hcys

A

SAM

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3
Q

This transfers CO2.

A

biotin

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4
Q

This is involved in oxidation reactions (tyrosine synthesis)

A

tetrahydrobiopterin

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5
Q

This holds nitrogen and is the coenzyme form of B6 and cofactor for tranaminase reaction.

A

PLP (pyridoxal phosphate)

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6
Q

Why do we need A.As?

A

energy source
substrate for proteins
substrate for heme, purine, pyrimidines, melanine

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7
Q

What part of the TCA cycle inhibits glycolysis?

A

citrate

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8
Q

Whenever you see the word dehydrogenase with the word of the substrate in it what do you make?
If you see dehydrogenase with the word of the product in it what does it make?

A

NADH
(except with succinate dehydrogenase you make FADH2)
NAD+ or NADP+

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9
Q

How much energy do you get from TCA cycle?

A

12 ATP

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10
Q

What can malate turn into?

A

oxaloaceteate

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11
Q

What is the breakdown of alcohol?

A

alcohol->ADH acetalaldehyde-> acDH acetic acid-> acetyl coA

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12
Q

In the TCA cycle when you see a synthetase what do you get?

A

ATP

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13
Q

What is made in the liver and is driven by too much ammonia?

A

glutamate synthesis

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14
Q

If you see an enzyme with synthetase or dehydrogenase with the word of the substrate in it (i.e succinyl coa -> succinate; uses succinyl CoA synthetase) then do you gain or lose energy?

A

you gain energy

you will use energy if the enzyme has the name of the product i.e glutamate-> glutamine using glutamine synthase

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15
Q

Why would you want to turn glutamate into glutamine?

A

because glutamate doesnt transport across cell membranes and glutamine does

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16
Q

What is the most abundant amino acid and it allows the movement of untoxic NH4 and donates nitrogens?

A

glutamine

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17
Q

Are transaminases reversible and what do they require?

A

yes!

PLP (B6)

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18
Q

What are serum ALT used for?

A

as a liver diagnositic test

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19
Q

What is a side product of the creation of glutamine back to glutamate and what do we do with it?

A

NH4+

goes to urea cycle

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20
Q

Where is the glucose-alanine cycle?

A

in the muscle and the liver

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21
Q

What does cortisol do?

A

it stimulates alanine aminotransferase and gluconeogenesis and breakdown of proteins in the muscle

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22
Q

Where does the glucose-glutamine cycle take place?

A

in the kidney and the muscle

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23
Q

What A.A is often glycosylated?

A

ASN

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24
Q

DO humans express asparaginase?

A

no

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25
What does leukemia do to ASN?
makes body unable to make it so you will need ASN injections
26
What is the vehicle for transferring carbons of intermediate oxidation states?
serine hydroxymethyltransferase
27
When 3PGA goes to Ser there are 2 types of intermediates, what are they?
phosphopyruvate and phosphoserine intermediates | this generates NADH
28
Deficiencies in what 2 enzymes cause homocystinuria, characterized by a mentally deficient gumbee like body with fragile bones and blood clots. How do you treat this?
cystathionine synthase (need PLP) cystathionase (PLP) Cuz Sisters need PeePs Good diet and vitamins
29
If you have an enzyme defiency resulting in PKU, what enzyme are you deficient in?
phenylalanine hydroxylase
30
What are the symptoms of PKU and how do you treat it?
light skin, mental retardation | no aspartame, diet
31
Where do you begin digesting proteins and how?
stomach via low pH, gastrin from mucosa triggers pepsin, parietal cells (HCl) and renin (coagulates milk)
32
What happens to proteins in the intestine?
Low ph->bicarb from pancreas | CCK release-> triggers pancreatic enzymes
33
What activates trypsin and where does it come from?
enteropeptidase from the intestine
34
Explain ubiquitin
attaches to lysine to degrade proteins the longer the chain the stronger the degredation signal N terminal determines speed of degredation -arginine and leucine-> fast -methionine and proline-> slow
35
What are PEST sequences?
Pro-Glu-Ser-Thr; this sequence is a target for degredation
36
What digests ubiquitin-tagged proteins?
proteosomes
37
What are diseases associated with ubiquitones?
Alzheimers and Parkinsons Cystic fibrosis Liddle's syndrome
38
(blank) diseases are associated with the formation of proteins structures in neurons
alzeheimers and parkinsons
39
(blank) disease is the rapid degradation of chloride channels
cystic fibrosis
40
(blank) is when Na+ channels in kidney dont get degraded and you get excessive Na absorption and early onset hypertension
Liddles
41
Who have positive nitrogen balance?
children, pregnant women and body builders
42
What give negative nitrogen balance?
stress hormones, cytokines
43
What are ketogenic amino acids?
ones that make Acetoacetyl Coa, Acetyl Coa | the A's :)
44
What are glucogenic amino acids?
ones that make pyruvate, oxaloacetate, fumarate, succinyl coA, alpha ketoglutarate
45
If there is a defect in glycine transaminase what does this lead to?
oxaluria Type I | Too much oxalate (makes kidney stones)
46
If there is a defect in glycine cleavage enzyme that what does this lead to?
nonketotic hyperglycinemia (too much glycine)
47
If you have a defect in cystathionine synthase what does this lead to?
homocystinuria | cant make amino acids
48
What amino acids degrade to pyruvate? | Slide 25
Some Good Children Are Toothless Mean Pirates | Serine, Glycine, Cysteine, Alanine, Tryptophan, methionine, Pyruvate
49
What amino acids degrade to acetyl Coa?
Prostitutes Like Taking In Long Things | Phenylalanine, Leucine, Tyrosine, Isoleucine, Lysine, Tryptophan
50
If you have a deficiency in tyrosine aminotransferase what will you have?
tyrosinemia II (too much tyrosine)
51
If you have a deficiency in homogenitisate oxidase then what will you have?
homogentisic acid intermed. alkaptonuria
52
If you have a deficiency in fumarylacetoacetate hydroxylase then what will happen?
fumarylacetoacetate intermediate tyrosinemia I
53
What amino acids degrade to alpha ketoglutarate?
Gregs Hot Girlfriends Are Pregnant | Glutamate, Histidine, Glutamine, Arginine, Proline
54
If you have a deficiency in histidase then what will you have?
histidinemmia
55
If you have folate deficiency what will accumulate?
formimino glutamic acid | FIGLU
56
What amino acids degrade to OAA?
ASS Asparagine Asparatate
57
Simplify branched chain amino acid degredation
transamination in MUSCLE followed by oxidative decarboxylation in LIVER
58
What happens if you lack alpha keto acid dehydrogenase complex?
maple syrup urine disease
59
What are the products of branched chain amino acid metabolism?
proprionyl CoA Acetyl CoA Acetoacetate
60
What amino acids degrade to succinyl CoA?
I Think My Vagina Sux | Isoleucine, Threonine, Methionine, Valine, Succinyl CoA
61
If you have a deficiency in methylmalonyl CoA mutase what will result?
methylmalonic aciduria
62
Where are glutamine and glutamate metabolized?
the intestinal mucosa
63
Where are amino acids other than glutamine and glutamate metabolized?
the liver
64
Where do branched chain amino acids go to get metabolizd?
Start in liver and go to muscle and then go back to liver
65
What is the major source of amino acids during fasting?
muscle
66
During fasting,Where does alanine go for gluconeogenesis?
liver
67
During fasting where does glutamine go?
to the kidney and intestines
68
In the phenylalanine amino acid degredation pathway, what are the 2 missing enzymes that can result in phenylalanine accumulate and PKU?
phenylalanine hydroxylase -> PKU classical dihydropteridine reductase-> PKU nonclassical Both result in mental retardation
69
Tell me about homogentisate oxidase; | what AA pathway is it in, what accumulates, what is the disease associated with it and what are the symptoms?
tyrosin pathway homogentisic acid accumulates alcaptonuria Black urine, arthritis
70
Tell me about fumarylacetoacetate; | what AA pathway is it in, what accumulates, what is the disease associated with it and what are the symptoms?
tyrosine fumarylacetoacetate tyrosinemia I liver failure, early death
71
Tell me about tyrosine aminotransferase; | what AA pathway is it in, what accumulates, what is the disease associated with it and what are the symptoms?
tyrosine tyrosine tyrosinemia II neurological defects
72
Tell me about cystathionase; | what AA pathway is it in, what accumulates, what is the disease associated with it and what are the symptoms?
methionine cystathionine cystathionura benign
73
Tell me about cystathionine synthase; | what AA pathway is it in, what accumulates, what is the disease associated with it and what are the symptoms?
methionine homocysteine homocysteinuria CV and neurological problems
74
Tell me about glycine transaminase; | what AA pathway is it in, what accumulates, what is the disease associated with it and what are the symptoms?
glycine glyoxylate primary oxaluria Type I Renal failure due to stone formation
75
Tell me about glycine cleavage enzyme; | what AA pathway is it in, what accumulates, what is the disease associated with it and what are the symptoms?
glycine glycine hyper glycinemia mental retardation
76
Tell me about branched chain alpha keto acid dehydrogenase; | what AA pathway is it in, what accumulates, what is the disease associated with it and what are the symptoms?
branched chain amino acids (leucine, isoleucine, valine) alpha ketoacids of the branched chain amino acids maple syrup urine mental retardation
77
(blank) is a neurotoxin so must be converted to carbamoyl phosphate to enter the urea cycle.
ammonia (NH4+)
78
Build up of what leads to orotate in the urine?
carbamoyl phosphate
79
How do you measure Blood urea levels? | When are these levels high?
As BUN | Renal failure
80
What enzyme can cleave urea to alkalize the urine and cause precipitation of magnesium ammonium phosphate (kidney stones)?
bacterial enzyme Urease
81
What can inherited defects in the urea cycle cause?
hyperammonemia and encephalopaty feeding difficulties, vomiting, lethargy, irritiability, aversion to protein rich foods ATP deficiencies (Cuz alpha KG-> glutamine) High glutamine levels
82
How do you treat urea cycle enzyme deficiency?
limit protein intake remove excess ammonia replace intermediates missing from urea cycl liver transplant
83
Where does the urea cycle take place?
the liver
84
How many ATPs are needed in the urea cycle and where do they come from?
4, 2 from carbamoyl synthetase 2 from argininosuccinate synthase

Block 3 Week 6 (6 decks)

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