Protein metabolism Flashcards

1
Q

What are the functions of dietary protein?

A

1) replenishes endogenous amino acids 2) Replenishes glycogen stores (via gluconeogenesis) 3) Excess intake is used for ATP production and lipid synthesis 4) Excess nitrogen is excreted

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2
Q

Steps of protein digestion:

A

1) break the proteins into amino acids 2) split the amino acids into amines and acids (only occurs in the liver) 2.5) Accumulation of excess amines 3) excretion of excess amines.

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3
Q

What cofactor is required for transamination?

A

PLP; pyridoxal phosphate (carrier of amino groups, performs transaminations, decarboxylations, amino acid racemizations.

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4
Q

What is the role of alpha ketoglutarate in transamination reactions?

A

a-ketoglutarate is a nitrogen group acceptor (turns into glutamate or glutamine)

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5
Q

What is the role of glutamate dehydrogenase?

A

transforms glutamate to alpha ketoglutarate without using PLP

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6
Q

What structures serve as temporary storage of NH4+?

A

Glutamate and glutamine

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7
Q

How is free ammonia neutralized?

A

Free ammonia is added to glutamate to form glutamine or pyruvate can be converted into alanine. Both glutamine and alanine transport ammonia to the liver.

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8
Q

Which class of enzyme is glutaminase?

A

Hydrolase

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9
Q

What is the function of glutamate dehydrogenase?

A

glutamate dehydrogenase is an enzyme in liver mitochondria. Its role it to produce NH4+ for the urea cycle while also generating alpha-ketoglutarate from glutamate.

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10
Q

Pyruvate generating-AAs

A

CAST - GT ; Cysteine, Alanine, Serine, Threonine, Glycine, Tryptophan.

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11
Q

What is the preferred cofactor for CH3 transfer?

A

SAM

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12
Q

What cofactor transfers 1-carbon, preferably, Serine

A

THF (works with oxidation states CH3, CH2OH, CHO) It is a redox co-factor, but not a redox cofactor.

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13
Q

Alpha-ketoglutarate generating AAs

A

AP HOGG; Arginine, Proline, Histidine, Ornithine, Glutamine, Glutamte.

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14
Q

Oxaloacetate generating AAs

A

AA - Asparagine, Aspartate

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15
Q

Strategy for forming TCA cycle intermediates from Amino Acids

A

1) If too big, cleave to make smaller amino acid, 2) If too small, add carbon 3) If otherwise correct, amino transferase, if oxidation state needs changing use a more complex strategy.

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