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LEC 40 Amino Acid Metabolism Flashcards

Describe the basic principles of amino acid biosynthesis, including key synthetic pathways, enzymes, and co-factors. Describe the flow of nitrogen from proteins in peripheral tissues to the liver and through the urea cycle. Explain how amino acids are catabolized to glucogenic and ketogenic intermediates.

1
Q

What’s the acronym for the 9 essential amino acids?

A

“PVT Tim Hall”
Phenylalanine
Valine
Threonine
Tryptophan
Isoleucine
Methionine
Histadine
Arginine* (only during +nitrogen balance)
Lysine
Leucine

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2
Q

What’s the difference b/w essential and nonessential amino acids?

A

essential amino acids must be obtain from the diet. nonessential can be synthesized

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3
Q

What enzyme converts b/w alpha-ketoglutarate and glutamate?

A

glutamate dehydrogenase

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4
Q

What enzyme directly converts glutamate to glutamine?

A

glutamine synthetase

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5
Q

What is the common required substrate for the enzymes glutamate dehydrogenase and glutamine synthetase?

A

NH4+

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6
Q

What is an important cofactor for transamination reactions?

A

Pyridoxal phosphate (B6)

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7
Q

What enzyme type catalyzes a transamination reaction?

A

aminotransferase

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8
Q

What are transamination reactions?

A

amine groups are transferred from one amino acid to the alpha-keto precursor of another

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9
Q

What enzyme catalyzes the reversible reaction of pyruvate & glutamate to form alanine & alpha-ketoglutarate?

A

alanine aminotransferase

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10
Q

Most transamination reactions involve which 2 compounds?

A

alpha-ketoglutarate and glutamate

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11
Q

What is coupled transamination?

A

transfer of amine groups b/w other amino acids is coupled to the glutamate/α-ketoglutarate reaction

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12
Q

What enzyme catalyzes the rxn b/w oxaloacetate/glutamate and aspartate/alpha-ketoglutarate?

A

aspartate aminotransferase

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13
Q

What enzyme converts glutamate to glutamic semialdehyde?

A

pyrroline-5-carboxylate synthetase

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14
Q

Glutamic semialdehyde can convert to which two compounds?

A

Ornithine & Pyrroline-5-carboxylate (to proline)

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15
Q

Pyrroline-5-carboxylate reductase converts pyrroline-5-carboxylate to which amino acid?

A

Proline

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16
Q

Ornithine and carbamoyl phosphate form citrulline using which enzyme?

A

ornithine transcarbamoylase

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17
Q

Citrulline and aspartate form argininosuccinate using which enzyme?

A

argininosuccinate synthetase

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18
Q

What enzyme converts argininosuccinate to fumarate and arginine?

A

argininosuccinate lyase

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19
Q

What enzyme forms carbamoyl phosphate?

A

carbamoyl phosphate synthetase I

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20
Q

What is carbamoyl phosphate’s purpose?

A

donates a carbamoyl group to citrulline
is also an entry point for nitrogen into the urea cycle

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21
Q

What cofactor is essential for the enzyme carbamoyl phosphate synthetase I that forms carbamoyl phosphate?

A

N-acetylglutamate

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22
Q

What enzyme catalyzes the rxn of aspartate & glutamine to form asparagine & glutamate?

A

asparagine synthetase (requires ATP)

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23
Q

Which amino acids are derived from 3-phosphoglycerate?

A

serine, cysteine, & glycine

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24
Q

Which amino acids are derived from Phosphoenolpyruvate and erythrose-4-phosphate?

A

tryptophan, tyrosine, & phenylalanine

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25
Which amino acids are derived from pyruvate?
alanine, leucine, & valine
26
Which amino acids are derived from alpha-ketoglutarate?
glutamate, arginine, glutamine, proline, histidine (GAG PH)
27
What amino acids are derived from oxaloacetate?
aspartate, asparagine, lysine, methionine, threonine, isoleucine
28
What enzyme catalyzes the rxn of 3-phosphoglycerate to 3-phophopyruvate?
phosphoglycerate dehydrogenase
29
What is the key cofactor in the synthesis of glycine from serine?
Tetrahydrofolate (H4 folate)
30
What enzyme catalyzes the rxn b/w serine and glycine?
serine hydroxymethyltransferase
31
What enzyme converts homocysteine to methionine?
methionine synthase (methyl cycle)
32
What enzyme converts methionine to S-adenosylmethionine using ATP?
methionine adenosyltransferase
33
What enzyme converts homocysteine & serine to cystathionine?
cystathionine synthase
34
What enzyme converts cystathionine to cysteine?
cystathionase
35
What enzyme catalyzes the rxn of phenylalanine to tyrosine?
Phenylalanine hydroxylase
36
What is a key cofactor for hydroxylation of aromatic rings?
tetrahydrobiopterin
37
What disease occurs from a deficiency of phenylalanine hydroxylase?
Phenylketonuria (PKU) ~ Tyr deficient
38
What are the biochemical consequences of PKU?
1. accumulation of phenylalanine and phenylpyruvate 2. tyrosine deficiency
39
What is the fate of the Nitrogen in amino acids?
can be used for biosynthesis OR excreted in the urea cycle
40
What is the fate of the carbon skeletons of amino acids?
they turn into alpha-keto acids which can enter TCA and gluconeogenesis
41
What are the four key processes that characterize the overall flow of nitrogen during amino acid catabolism?
1. transamination 2. ammonia transport 3. oxidative deamination of glutamate (glutamate dehydrogenase rxn) 4. rxns of urea cycle
42
What is the most abundant circulating amino acid and a major carrier of nitrogen to the liver?
Glutamine
43
How is nitrogen transported from the peripheral tissues to the liver?
1. NH4+, Mg-ATP, and L-glutamate react via Glutamine Synthase to form L-glutamine 2. L-glutamine travels to the liver where it is converted back to L-Glutamate by glutaminase releasing NH4+
44
Describe the transport of nitrogen from the muscle to the liver by way of alanine.
Alanine Cycle: 1. Pyruvate (from glycolysis) in the muscle undergoes a transamination rxn and accepts an NH3 to form alanine 2. Alanine moves through the blood to the liver 3. Alanine is converted back to pyruvate in the liver releasing the nitrogen to the urea cycle
45
Describe the steps of the Urea Cycle.
1. Carbamoyl phosphate is formed from HCO3-, NH4+ & ATP by carbamoyl phosphate synthetase I 2. Ornithine & Carbamoyl phosphate form citrulline by ornithine transcarbamoylase 3. citrulline & aspartate form argininosuccinate by argininosuccinate synthetase 4. argininosuccinate forms fumarate and arginine by argininosuccinate lyase 5. Arginine forms urea and regenerates ornithine by arginase
46
What part of the cell does the carbamoyl phosphate rxn and the ornithine transcarbamoylase rxn occur?
Mitochondria The rest of the Urea Cycle occurs in the cytosol
47
After the formation of citrulline, the rest of the urea cycle occurs where in the cell?
Cytosol
48
What happens to glutamine once it enters the mitochondrial matrix?
glutaminase converts it into glutamate & NH4+
49
Amino acids react with alpha-ketoglutarate to form which compound that enters the mitochondria to deliver nitrogen?
glutamate
50
Alanine reacts with alpha-ketoglutarate to form which compound that enters the mitochondria to deliver nitrogen?
glutamate
51
Once inside the mitochondria, glutamate can undergo one of two rxns. What are these two reactions and enzymes involved?
1. glutamate dehydrogenase converts it to alpha-ketoglutarate while releasing NH4+ for carbamoyl phosphate synthesis OR 2. glutamate reacts with oxaloacetate using aspartate aminotransferase to form alpha-ketoglutarate and aspartate (receives the nitrogen). the latter directly enters urea cycle
52
What are the biochemical consequences of carbamoyl phosphate synthetase and N-acetylglutamate synthetase deficiencies?
hyperammonemia due to lack of carbamoyl phosphate required by urea cycle
53
What are the biochemical consequences of ornithine transcarbamoylase deficiency?
hyperammonemia increased orotic acid formed from excess carbamoyl phosphate
54
What are the biochemical consequences of argininosuccinate synthetase deficiency?
hyperammonemia citrullinemia arginine supplementation may be effective
55
What are the biochemical consequences of argininosuccinate lyase deficiency?
hyperammonemia citrullinemia increased argininosuccinate levels arginine supplementation may be effective
56
What are the biochemical consequences of arginase deficiency?
Hyperammonemia* Citrullinemia* increased argininosuccinate levels* increased arginine levels *less severe than other urea cycle disorders
57
Which amino acids are strictly ketogenic?
Leucine and Lysine
58
Which 5 amino acids are converted to alpha-ketoglutarate?
1. Arginine 2. Histidine 3. Proline 4. Glutamate 5. Glutamine
59
How is glutamate converted to alpha-ketoglutarate?
Deamination by glutamate dehydrogenase OR Transamination
60
How is glutamine converted to alpha-ketoglutarate?
1. converted to glutamate by glutaminase 2. deamination/transamination of glutamate
61
What common intermediate do arginine and proline both break down into in their path to alpha-ketoglutarate?
glutamic semialdehyde
62
Proline catabolism is the reverse of its synthesis and involves which enzyme?
proline oxidase
63
Which two amino acids are converted to oxaloacetate?
Asparagine & Aspartate
64
What enzyme converts asparagine to aspartate?
asparaginase
65
What enzyme converts aspartate to oxaloacetate?
aspartate transaminase (using pyruvate) --> forms alanine and oxaloacetate
66
Which 6 amino acids are converted to pyruvate?
Threonine Glycine Serine Cysteine Tryptophan Alanine
67
How is alanine converted to pyruvate?
transamination (alanine aminotransferase) producing pyruvate and glutamate
68
How is serine converted to pyruvate?
serine dehydratase
69
How is glycine converted to pyruvate?
1. converted to serine by serine hydroxymethyltransferase (tetrahydrofolate dependent) 2. serine-->pyruvate (serine dehydratase)
70
What is the alternate path for glycine other than conversion to pyruvate?
can be cleaved to CO2 and NH4+ while producing an NADH by glycine cleavage enzyme
71
How is threonine converted to pyruvate?
1. converted to 2-amino-3-ketobutyrate by threonine dehydrogenase 2. 2-amino-3-ketobutyrate is converted to glycine and acetyl-CoA 3. follows glycine steps to get to pyruvate
72
What is the other path that threonine can take besides converting to pyruvate?
1. can convert to alpha-ketobutyrate by serine dehydratase 2. alpha-ketobutyrate then converts to propionyl-CoA then to succinyl-CoA (into TCA)
73
Describe the catabolism of methionine to propionyl-CoA.
methionine is converted to homocysteine through the activated methyl cycle, then metabolized to propionyl-CoA; Homocysteine--(Cystathionine beta-synthase)-->Cystathionine--(Cystathionase)-->cysteine+alpha-ketobutyrate-->propionyl-CoA
74
Which amino acids are important sources of energy in muscle?
branched chain aminos (valine, isoleucine, leucine)
75
Valine is metabolized to _____, so valine is _______.
propionyl-CoA/succinyl-CoA; glucogenic
76
Isoleucine is metabolized to _____ & _____ making it both ______ & ______
propionyl-CoA & Acetyl-CoA; glucogenic & ketogenic
77
Leucine breaks down into ______ & ______, making it strictly _______.
Acetyl-CoA & Acetoacetate; ketogenic
78
What is maple syrup urine disease and its biochemical consequences?
branched chain ketoacid dehydrogenase deficiency resulting in accumulation and excretion of branched chain alpha-keto acids and related metabolites
79
What do phenylalanine and tyrosine break down into?
fumarate (glucogenic) and acetoacetyl-CoA (ketogenic)
80
What enzyme is deficient in Tyrosinemia Type I?
Fumarylacetoacetase
81
What are the biochemical consequences of Tyrosinemia type I?
Fumarylacetoacetate Hydrolase Deficiency: -tyrosinemia -accumulation of fumarylacetoacetate & maleylacetoacetate and their derivatives succinyl acetone and succinyl acetoacetone -succinyl acetone inhibits porphobilinogen synthase (aminolevulinic acid dehydratase) -acute hepatic porphyria and accumulation of amino levulinic acid
82
What enzyme is deficient in tyrosinemia type II?
Tyrosine aminotransferase
83
What are the biochemical consequences of tyrosinemia type II?
Tyrosine Aminotransferase Deficiency: -tyrosinemia -elevated tyrosine metabolites
84
What enzyme is deficient in tyrosinemia type III?
Hydroxyphenylpyruvate Dioxygenase
85
What are the biochemical consequences of tyrosinemia type III?
Hydroxyphenylpyruvate Dioxygenase Deficiency: -tyrosinemia -elevated tyrosine metabolites (same as tyrosinemia type II)
86
What enzyme is deficient in Alkaptonuria?
Homogentisate-1,2-Dioxygenase
87
What are the biochemical consequences of alkaptonuria?
-tyrosinemia -elevated homogentisate levels
88
Tryptophan is metabolized to _____ & _____, so tryptophan is both ________ & ________.
pyruvate & acetyl-CoA; glucogenic & ketogenic
89
Lysine is metabolized entirely to _______, so lysine is strictly ________.
acetyl-CoA; ketogenic

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