Lecture 28 Flashcards

(37 cards)

1
Q

How are amino acids consumed in the diet?

A

As proteins

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2
Q

What does protein digestion involve?

A

Hydrolysis of peptide bonds by different proteases / peptidases

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3
Q

What are the two types of peptidases?

A

Endopeptidase and exopeptidase

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4
Q

What do endopeptidases do?

A

Attack peptide bonds within the protein polymer

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5
Q

What do exopeptidase do?

A

Attack the last peptide bond near the end of the protein polymer

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6
Q

How do endopeptidases work?

A

Different endopeptidases act sequentially to produce smaller peptides each round

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7
Q

What is endopeptidase specificity determined by?

A

Adjacent amino acid side chain in the protein substrate

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8
Q

Where do carboxypeptidases cut?

A

Near the carboxyl-terminal residue

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9
Q

Where do aminopeptidases cut?

A

Near the amino-terminal residue

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10
Q

What are proteases produced as?

A

Zymogens

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11
Q

What are zymogens?

A

Inactive precursors to the peptidase / protease

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12
Q

Why are zymogens needed?

A

To prevent peptidase activity before reaching the GIT and breaking down the proteins within cells

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13
Q

How are zymogens activated?

A

Through cleavage of peptides from their structure

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14
Q

What are the two forms of zymogen activation?

A

Autolytic activation and catalytic activation

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15
Q

What is autolytic activation?

A

Change in chemical composition (e.g. pH) causing self activation (cleavage)

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16
Q

What is catalytic activation?

A

An active form acting as a catalyst to activate the inactive form

17
Q

How are di- and tri-peptides absorbed into the SI?

A

By co-transport with H+ ions via a membrane transporter

18
Q

How are amino acids absorbed into the SI?

A

Through an amino/Na+ cotransporter as amino acids are moving against their concentration gradient

19
Q

What happens to absorbed di- and tri-peptides?

A

They are further digested into individual amino acids by cytoplasmic peptidases

20
Q

How do amino acids enter the blood?

A

Through a facilitative transporter into the interstitial fluid and then to the blood

21
Q

What are the different Na+ dependent carriers for amino acids across the SI?

A

Neutral AA, proline & hydroxyproline, acidic AA and basic AA & cysteine

22
Q

What is deamination of amino acids?

A

The process of removing an amino group

23
Q

What does deamination of amino acids generate?

A

A carbon skeleton and a free amino group

24
Q

What can a carbon skeleton be used for?

A

Energy capture

25
What happens to a free amino group?
Is generally excreted
26
What are the two way amino acids can be deaminated?
Through releasing their amino group to solution or transferring it to a keto acid
27
What is the transfer of amino group to a keto acid known as?
Transamination
28
What is transamination catalysed by?
Aminotransferase enzymes
29
What is PLP?
Pyridoxal phosphate derived from vitamin B6, a co-enzyme required for transamination reactions
30
What are the two forms PLP exists as?
Pyridoxal phosphate with no amino group and pyroxamine phosphate with an amino acid
30
What is the first step of transamination?
Amino group is transferred from the amino acid to the PLP to form pyridoxamine phosphate
31
What is the second step of transamination?
Amino group is transferred from the pyridoxamine phosphate to the keto acid to form pyridoxal phosphate
32
What is the keto acid pair for glutamate?
alpha-ketoglutarate
33
What is the keto acid pair for aspartate?
Oxaloacetate
34
What is the keto acid pair for alanine?
pyruvate
35
What can happen to keto acids?
They can be fed into metabolic pathways either directly or after modification
36
Why are transamination reactions required in the liver?
To remove excess nitrogen through converting it to urea