UoM Cell Metabolism Lecture 16-17 Amino acid metabolism (Year 2, Sem 2, 2017)

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Question 1 of 1

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There is no storage for amino acids apart from making them into proteins, meaning body protein is a massive fuel reserve. Amino acid degradation forms either glucose for aerobic/anaerobic metabolism or fatty acids/ketone bodies for b-oxidation. Are used as a fuel in normal synthesis/degradation, when diet formed or during starvation. Match the part of the amino acid with its fate in metabolism.

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Match the text
Amine group
Carboxyl group, carbon background and side chain

Click and drag
Excreted via the urea cycle
Degraded into metabolic intermediates

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240

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Transamination is the transfer of an amino group from one molecule to another (Amino transferases do this). There is also deamination; so what molecule in the liver froms alpha-ketogluterate from glutamate.. removing an NH4+ group.

Select the correct answer(s).

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The liver is the most important organ in the urea cycle, and where the GDH (glutamine dehydrogenase) exists. NH4+ is generated in the mitochondrial matrix as its ion is cytotoxic, whereas urea is generated in the cytosol using 3 ATP equivalents. Where is GDH located?

Select the correct answer(s).

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The urea cycle is an important pathway in degradation of amino acids acting in the cytosol and mitochondrial matrixnunlike the citric acid cycle. Order the steps of cycle, highlighting the area it is in, the enzymes and its connections to the citric acid cycle (important to learn).

Match the text (click and drag)

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Match the Text
1
2
3
4
5
6

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Carbamoyl phosphate joins the Ornithine in the cycle to form Citrulline using Ornithine transcarbamoylase
Arginosuccinate synthetase forms fumarate (converted to malate to join CAC) and arginine
The cycle continues
Arginine is added to H2O by Arginase (hydrolysis) forming urea and Ornithine
Citrulline is added to aspartate from the matrix citric acid cycle malate (aminated by glutamate turning into a-ketoglutarate) forming arginino-succinate
Start - Carbamoyl phosphate is formed from 2ATP, CO2, NH4+ and Carbamoyl phosphate synthetase in matrix

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GDH (glutamate dehydrogenase) is involved in generating alpha-ketogluterate (removing NH4+ for urea), for the generation of keto acids from amino acids in transamination. What doesn't happen to this generated keto acids

Select the correct answer(s).

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300

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The fates of the C-skeletons depends on the type of amino acids, entering the CAC at different places (seen in the picture). Match the molecule of interest with its generated product.

Match the text (click and drag)

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Match the text
Pyruvate
Acetyl CoA
Oxaloacetate
Acetoacetyl CoA

Click and drag
Oxaloacetate and Acetyl CoA
Forms phosphoenol pyruvate then glucose
Forms ketones
Fatty acids and Acetoacetyl CoA

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Glucogenic amino acids are those that are chiefly converted to glucose through gluconeogenesis (usually those who are converted into oxaloacetate then phosphoenol-pyruvate, or any molecule converted into something in the CAC. Ketogenic amino acids are converted into ketone bodies usually through acetoacetyl CoA. Order the steps of basic gluconeogenesis.

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Match the Text
1
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3
4

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Glucose
Pyruvate
Oxaloacetate
Amino acid

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Ketogenic amino acids are important for converting dietary AA into fat, including Leucine and Lysine (learn). Order the steps in fatty acid synthesis from amino acids.

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Match the Text
1
2
3

Click and drag
Acetyl-CoA or Acetoacetyl CoA
Amino acids
Acetyl CoA forms fatty acids and Acetoacetyl CoA forms ketones

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Branched chain amino acids like Valine, Isoleucine and Leucine are not degraded in the liver like normal amino acids, but are oxidized as fuels in muscle, kidney and the brain. How are these BCAA's regualated

Select the correct answer(s).

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Why can't BCAA's (Valine, Isoleucine and Leucine) be degraded by the liver? (its to do with an oxidative decarboxylation molecule an aminotransferase)

Select the correct answer(s).

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Explanation

GDH Is deamination of glutamate to a-ketoglurerate

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There is a genetic disease where the a-keto acid dehydrogenase complex is defective, causing BC a-keto acids to accumulate in the blood, treated by control of BCAA intake. There is another strange side effect which will spoil the question, but what is this disease called?

Select the correct answer(s).

(0/0)

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Transport of nitrogen to the liver to form urea is required as muscles/tissues can oxidise but not synthesise urea (BCAA's are a big problem for those without a liver). There are two mechanisms which are both 1 step reactions, so match the enzyme used and its action in either mechanism.

Match the text (click and drag)

(0/0)

Match the text
Glutamine synthetase
Serum glutamate-pryruvate transaminase

Click and drag
Adds ammonia to glutamate to produce glutamine
Transamination of pyruvate to alanine (uses glumate, making a-ketogluterate)

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Glutamine is important as it allows ammonia nitrogen to be transported (non toxic), synthesised by glutamine synthetase from glutamate using ATP. What else is glutamines role?

Select the correct answer(s).

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Which of the two mechanism molecules are used to transport nitrogen to the liver for urea synthesis and removal?

Select the correct answer(s).

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UoM Cell Metabolism Lecture 16-17 Amino acid metabolism (Year 2, Sem 2, 2017)

Question 1 of 1

Time Left

Match the text (click and drag)

(0/0)

Amine group

Carboxyl group, carbon background and side chain

Excreted via the urea cycle

Degraded into metabolic intermediates

Transamination is the transfer of an amino group from one molecule to another (Amino transferases do this). There is also deamination; so what molecule in the liver froms alpha-ketogluterate from glutamate.. removing an NH4+ group.

Select the correct answer(s).

(0/0)

The liver is the most important organ in the urea cycle, and where the GDH (glutamine dehydrogenase) exists. NH4+ is generated in the mitochondrial matrix as its ion is cytotoxic, whereas urea is generated in the cytosol using 3 ATP equivalents. Where is GDH located?

Select the correct answer(s).

(0/0)

The urea cycle is an important pathway in degradation of amino acids acting in the cytosol and mitochondrial matrixnunlike the citric acid cycle. Order the steps of cycle, highlighting the area it is in, the enzymes and its connections to the citric acid cycle (important to learn).

Match the text (click and drag)

(0/0)

1

2

3

4

5

6

Carbamoyl phosphate joins the Ornithine in the cycle to form Citrulline using Ornithine transcarbamoylase

Arginosuccinate synthetase forms fumarate (converted to malate to join CAC) and arginine

The cycle continues

Arginine is added to H2O by Arginase (hydrolysis) forming urea and Ornithine

Citrulline is added to aspartate from the matrix citric acid cycle malate (aminated by glutamate turning into a-ketoglutarate) forming arginino-succinate

Start - Carbamoyl phosphate is formed from 2ATP, CO2, NH4+ and Carbamoyl phosphate synthetase in matrix

GDH (glutamate dehydrogenase) is involved in generating alpha-ketogluterate (removing NH4+ for urea), for the generation of keto acids from amino acids in transamination. What doesn't happen to this generated keto acids

Select the correct answer(s).

(0/0)

The fates of the C-skeletons depends on the type of amino acids, entering the CAC at different places (seen in the picture). Match the molecule of interest with its generated product.

Match the text (click and drag)

(0/0)

Pyruvate

Acetyl CoA

Oxaloacetate

Acetoacetyl CoA

Oxaloacetate and Acetyl CoA

Forms phosphoenol pyruvate then glucose

Forms ketones

Fatty acids and Acetoacetyl CoA

Match the text (click and drag)

(0/0)

1

2

3

4

Glucose

Pyruvate

Oxaloacetate

Amino acid

Ketogenic amino acids are important for converting dietary AA into fat, including Leucine and Lysine (learn). Order the steps in fatty acid synthesis from amino acids.

Match the text (click and drag)

(0/0)

1

2

3

Acetyl-CoA or Acetoacetyl CoA

Amino acids

Acetyl CoA forms fatty acids and Acetoacetyl CoA forms ketones

Branched chain amino acids like Valine, Isoleucine and Leucine are not degraded in the liver like normal amino acids, but are oxidized as fuels in muscle, kidney and the brain. How are these BCAA's regualated

Select the correct answer(s).

(0/0)

Why can't BCAA's (Valine, Isoleucine and Leucine) be degraded by the liver? (its to do with an oxidative decarboxylation molecule an aminotransferase)

Select the correct answer(s).

(0/0)

Explanation

There is a genetic disease where the a-keto acid dehydrogenase complex is defective, causing BC a-keto acids to accumulate in the blood, treated by control of BCAA intake. There is another strange side effect which will spoil the question, but what is this disease called?

Select the correct answer(s).

(0/0)

Transport of nitrogen to the liver to form urea is required as muscles/tissues can oxidise but not synthesise urea (BCAA's are a big problem for those without a liver). There are two mechanisms which are both 1 step reactions, so match the enzyme used and its action in either mechanism.

Match the text (click and drag)

(0/0)

Glutamine synthetase

Serum glutamate-pryruvate transaminase

Adds ammonia to glutamate to produce glutamine

Transamination of pyruvate to alanine (uses glumate, making a-ketogluterate)