Protein Metabolism Flashcards

1
Q

What are amino acids

A

building blocks of proteins

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2
Q

Proteolysis

A

protein breakdown through hydrolysis of their peptide bonds

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3
Q

Enzymes that catalyze proteolysis

A

proteases

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4
Q

Where does protein synthesis take place?

A

ribosomes

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5
Q

key points of protein synthesis

A

Translation of mrna from transcription of a gene

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6
Q

Approximation of free amino concentrations in the body

A

Glutamine ~60%
Glutamate ~14%
Alanine ~4%

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7
Q

Where are amino acids typically found in the cell?

A

cytosol

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8
Q

What are the primary uses of free amino acids

A

processing other aminos

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9
Q

What is the glucose alanine cycle?

A

Converts alanine to pyruvate and ultimately glucose

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10
Q

What is the first step of breakdown of all amino acids?

A

removal of the nitrogenous alpha amine group (NH3+)

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11
Q

What is non oxidative deamination?

A

Loss of an amine group uses oxygen

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12
Q

What type of enzyme is required for non oxidative deamination?

A

dehydrogenase

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13
Q

Why is non oxidative deamination unique?

A

Only 2 amino acids go through it

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14
Q

Which two amino acids go through non oxidative deamination?

A

serine and threonine

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15
Q

Through the process of non oxidative deamination what are amine groups released as?

A

ammonia

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16
Q

Serine Deaminase

A

aka serine dehydratase
catalyzes the dehydrogenation of serine into pyruvate and ammonia (NH4)

17
Q

Threonine Deaminase

A

aka theronine dehydratase
catalyzes the dehydrogenation of threonine into pyruvate and ammonia

18
Q

Key difference between oxidative and non oxidative deamination

A

Oxidative deamination occurs via the oxidation of amine group amino acids whereas non oxidative deamination occurs via any other reaction

19
Q

Oxidative deamination

A

Glutamate loses amine group and a H+
oxidized by NAD+ or NADP+

20
Q

Transamination

A

transfer of amine groups to alpha ketoglutarate to form glutamate and alpha keto acid.

Most aminos (excluding glutamate, serine and threonine go through this process)

21
Q

Aminotrasferase

A

Enzyme responsible for catalyzing the transamination of amino acids (ecluding glutamate, threonine and serine)

22
Q

What is the most common fate of Alpha keto acids?

A

conversion to intermediates of carb and fat metabolism

23
Q

Potential fates of alpha keto acids

A

pyruvate
acetyl coA
Acetoaceytl CoA
Succinyl CoA
Fumerate
Oxaloacetate

24
Q

Where does glutamate transer its amine group?

25
what is formed when glutamate transfers its amine group?
Alpha ketoglutarate and alanine
26
Alanine Aminotransferase
catalyzes the conversion of glutamate and pyruvate to alpha ketoglutarate and alanine
27
Glutamine Synthetase
Glutamate reacts with ammonia group (and ATP) to form Glutamine +ADP + Pi + H+
28
how many glucogenic amino acids are there?
14
29
how many ketogenic amino acids are there? what are they?
2 (leucine, lysine)
30
how many glucogenic and ketogenic amino acids are there? what are they?
4 (isoleucine, phenylalanine, tryptophan, tyrosine)
31
What does the Urea Cycle begin with?
carbamoyl phosphate
32
What is Carbamoyl phosphate
Compound of high phosphoryl transfer potential formed by combining ammonia, bicarbonate and a phosphoryl group
33
Carbamoyl phosphate synthetase
Enzyme responsible for the formation of carbamoyl phosphate
34
how many ATP are expended in the formation of carbamoyl phosphate?
2
35
What is the only amino acid to donate an amine group in the urea cycle?
Aspartate