Amino Acid Catabolism Flashcards

1
Q

What is our source of amino acids?

A

Proteins in our diet

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2
Q

Are there any storage mechanisms for amino acids?

A

No

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3
Q

What are the three roles of amino acids in metabolism?

A

Involved in the synthesis of proteins, metabolised to generate energy and converted to small active molecules.

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4
Q

What does decarboxylation do?

A

Removes a COOH in the form of a CO2

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5
Q

What does transamination do?

A

Takes an amino acid and an a-keto acid and swaps the amine and keto groups to form new molecules.

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6
Q

What is a non-specific transaminase?

A

A transaminase that isn’t specific to a particular amino acid

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7
Q

What are specific transaminases?

A

Those that are specific to a particular donor amino acid and are named after them

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8
Q

What is the most important non-specific transaminase?

A

Glutamate transaminase

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9
Q

What does deamination do?

A

Removes an amine group

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10
Q

What are the two types of deamination?

A

Oxidative and non-oxidative

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11
Q

What is the difference between oxidative and non-oxidative deamination?

A

Oxidative requires NAD+ and FAD whereas non-oxidative does not.

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12
Q

What are the two ketogenic amino acids and how do you remember them?

A

Lucine and Lysine, only two that start with L

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13
Q

What are the four ketogenic and glycogen of amino acids and how do you remember them?

A

Phenylalanine, isoleucine, tryptophan and tyrosine; PITT

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14
Q

What happens when the body comes into contact with ammonia?

A

Ammonia attaches to another molecule to create an amino acid and is then expelled by the urea cycle

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15
Q

Where does protein digestion occur?

A

In the stomach and small intestine.

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16
Q

What do proteolytic enzymes do?

A

Degrade proteins by breaking peptide bonds

17
Q

What are the two types of preteolytic enzymes?

A

Endopeptidases and exopeptidases

18
Q

What is the difference between endopeptidases and exopeptidases?

A

Endopeptidases break bonds from the interior of the chain whereas exopeptidases break bonds from the terminal ends of the chain.

19
Q

What does pepsinogen do?

A

When activated (pepsin) it cleaves COOH

20
Q

What is stomach digestion limited by?

A

Contact time and specificity of pepsin

21
Q

What is the digested stomach mix called?

A

Chyme

22
Q

What two polypeptide hormones does chyme cause the release of?

A

Secretin and cholecystokinin

23
Q

What is the difference between amino acids and carbohydrates/lipids sourced from our diet?

A

We can’t store amino acids.

24
Q

What is the fate of active amines produced from decarboxylation of amino acids?

A

They are used to generate hormones and neurotransmitters

25
Q

What happens to the a-keto acid after transamination or deamination?

A

It is metabolised to generate energy.

26
Q

How are zymogens activated?

A

The enzyme enteropeptidase which is produced in the small intestine