proteins and amino acid metabolism Flashcards

1
Q

what are the 7 type and function of proteins?

A

Signalling

Regulatory

Contractile

Hormones

Structural

Immunological

Catalytic

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2
Q

what are some essential amino acids?

A

Histidine (in children)
Isoleucine
Leucine
Lysine

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3
Q

what are some non-essential amino acids?

A
Alanine
Arginine
Asparagine
Aspartic Acid
Glutamic Acid
Glutamine
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4
Q

what are some examples of the plant based proteins?

A

chickpeas (7g protein)
oats (11g protein)
brown rice (3g protein)
avocado (2g protein)

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5
Q

what are some examples of animal based proteins?

A

egg (14g protein)
ribeye steak (19g protein)
chicken breast (25g protein)
salmon (25g protein)

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6
Q

what are proteins made of?

A

amino acids, considered building blocks

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7
Q

how do enzymes work?

A

enzymes allow for less activation energy in comparison to without an enzyme

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8
Q

proteins as enzymes?

A

Oxidoreductases- catalyse oxidation and reduction reactions

Transferases- catalyse the transfer of elements from one molecule to another

hydrolases- catalyse reactions where cleavage of bonds in achieved by adding water

lyases- catalyse reactions in which groups of elements are removed to form a double bond or are added to an existing double bond

Isomerases- catalyse reactions that result in rearrangement of the structure of molecules

Ligases- catalyse bond formation between two substrate molecules

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9
Q

DNA Structure, base pairs and what its made of

A

C= Cytosine
G= Guanine
(1 pair)

A= Adenine
T= Thymine
(1 pair)

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10
Q

Free amino acid pool?

A

digestion—>absorption—>amino acid pool (170 g)—>intracellular amino acids/ proteins—> amino acid pool

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11
Q

Transamination?

A

The initial stage of degradation of amino acids is the removal of nitrogen by removing the amino group. This involves transamination.

Transamination occurs when an amine group from a donor amino acid transfers to an acceptor amino acid to form a new amino acid. A specific transferase enzyme accelerates the transamination reaction.

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12
Q

transamination 3 parts?

A

(1) Gluconeogenesis:
18 of the 20 AA’s can serve as a source for glucose synthesis

(2) Source of Free Energy
The C-skeletons lose electrons (oxidise) & form intermediates in TCA cycle metabolism or related molecules.

(3) Fatty Acid Synthesis
All AA’s provide a potential source of Acetyl Co-A which can be used to make FFA’s

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13
Q

deamination?

A

digestion—>absorption—>amino acid pool (170 g)—>intracellular amino acids—>proteins/deamination—>urea/carbon skeletons—>urine

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14
Q

what is the Glucose-Alanine Cycle?

A

Glutamate can react with pyruvate in a reaction catalyzed by alanine aminotransferase.

The alanine (an amino acid) that is produced can be shuttled to the liver where it can undergo the reverse reaction to pyruvate.

This can serve as a gluconeogenic substrate and allow the production of glucose which may be vital to the body during periods of fasting / starvation.

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15
Q

Lipids=fatty acids and glycerol

A

fatty acids and glycerol—>beta-Oxidation—>Acetyl CoA—>ketones/citrate

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16
Q

carbohydrates=glycogen and glucose

A

glycogen and glucose—>pyruvate—>Acetyl CoA—>ketones/citrate

glycogen and glucose—>pyruvate—>lactate

glycogen and glucose—>pyruvate—>oxaloacetate

glycogen and glucose—>pyruvate—>alanine—>deamination—>NH3—>urea

glycogen and glucose—>pyruvate—>alanine—>deamination—>Acetoacetate

glycogen and glucose—>pyruvate—>alanine—>deamination—>Glycine—>ketones

glycogen and glucose—>pyruvate—>alanine—>deamination—>Glutamate—>TCA cycle

17
Q

Proteins=amino acids

A

amino acids—>deamination—>NH3—>urea

amino acids—>deamination—>Acetoacetate

amino acids—>deamination—>Glycine—>ketones

amino acids—>deamination—>Glutamate—>TCA cycle