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?

A

pyruvate

25
Q

what is formed when glutamate transfers its amine group?

A

Alpha ketoglutarate and alanine

26
Q

Alanine Aminotransferase

A

catalyzes the conversion of glutamate and pyruvate to alpha ketoglutarate and alanine

27
Q

Glutamine Synthetase

A

Glutamate reacts with ammonia group (and ATP) to form Glutamine +ADP + Pi + H+

28
Q

how many glucogenic amino acids are there?

A

14

29
Q

how many ketogenic amino acids are there? what are they?

A

2 (leucine, lysine)

30
Q

how many glucogenic and ketogenic amino acids are there? what are they?

A

4 (isoleucine, phenylalanine, tryptophan, tyrosine)

31
Q

What does the Urea Cycle begin with?

A

carbamoyl phosphate

32
Q

What is Carbamoyl phosphate

A

Compound of high phosphoryl transfer potential formed by combining ammonia, bicarbonate and a phosphoryl group

33
Q

Carbamoyl phosphate synthetase

A

Enzyme responsible for the formation of carbamoyl phosphate

34
Q

how many ATP are expended in the formation of carbamoyl phosphate?

A

2

35
Q

What is the only amino acid to donate an amine group in the urea cycle?

A

Aspartate