Amino Acid Metabolism I Flashcards

1
Q

What is the difference between essential amino acids and nonessential amino acids?

A
  • Essential: cannot be synthesized in you body & have to come from the diet
  • Nonessential: they can be synthesized by the body & do not have to come from the diet
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2
Q

What are the 11 non-essential amino aids?

Which 2 are synthesized from essential amino acids?

What molecule are the rest synthesized from?

A
  • Synthesized from Glucose
    1. Alanine
    2. Arginine
    3. Asparagine
    4. Aspartate
    5. Cysteine (from Methionine)
    6. Glutamate
    7. Glutamine
    8. Glycine
    9. Proline
    10. Serine
  • Tyrosine (from phenylalanine)
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3
Q

What are teh 10 essential amino acids?

A
  1. Histidine
  2. Isoleucine
  3. Leucine
  4. Lysine
  5. Metionine
  6. Phenylalanine
  7. Threonine
  8. Tryptophan
  9. Valine
  10. Arginine (not required by adults, but required for growth)
    • enough is synthesized in the liver by adults, but not for infants
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4
Q

Where are dietary proteins digested to amino acids?

Amino acids are used to synthesize what products?

A
  • Dietary proteins are digested to amino acids in the stomach & intestine
  • amino acids are used to synthesize proteins & other nitrogen-containing compounds (nucleic acids, hormones, heme of hemoglobin)
    • in the fed state, amino acids can be stored in the form of glycogen or triacylglycerols
  • The carbon skeleton is oxidized for energy & the nitrogen is converted to urea
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5
Q

Which cells secrete pepsinogen?

It is the precursor for what enzyme?

How is it activated?

What is the activated enzymes function?

A

Chief cells

pepsin

Activated by HCl in the stomach

Pepsin starts digesting proteins in the stomach, turning them into polypeptides

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6
Q

Which cells secrete HCl?

What is the function of HCl in the process of protein digestion?

A

Chief cells

HCl denature proteins in the stomach (inactivates & partially unfolds) so they are better substrates for proteases

HCl also activates pepsinogen to pepsin

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7
Q

What zymogens are secreted from the pancreas for protein digestion?

What are their active forms & what enzymes facilitate this activation?

What is the combined function of these enzymes?

A

These enzymes convert the polypeptides into oligopeptides

  • Trypsinogen – enteropeptidase
    • ACTIVE: Trypsin
  • Chymotrypsinogen – trypsin
    • ACTIVE: Chymotrypsin
  • Proelastase – trypsin
    • ACTIVE: elastase
  • Procarboxypeptidase A – trypsin
    • ACTIVE: carbodypeptidase A
  • Procarboxypeptidase B – trypsin
    • ACTIVE: carbodypeptidase B
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8
Q

How are oligopeptides absorbed?

A

Aminopeptidases in the brush border of the intestinal epithelial cells act on the oligopeptides, converting them to free amino acids that are absorbed by the epithelial cells & transferred to the blood stream

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9
Q

The coenzyme tetrahydrofolate FH4 is derived from what vitmin?

What is its function in the amino acid pathway

A

Derived from folate (B9)

FH4 is the primary one-carbon carrier in the body & is required to either accept or donate a on-carbon group in the amino acid pathway

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10
Q

What are the sources of one-carbon units for tetrahydrofolate?

Once combined, what are they called? What are the 3 stages of oxidation for the carbon?

Ultimately forming what products?

A

serine, glycine, histidine, formaldehyde, formate

once combined with FH4, they are called the “one-carbon pool”

The carbon can be formyl (H) methylene (H2) –> methyl (H3)

And when combined with a precursor, can form products such as dTMP, serine, purines & B12 CH3

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11
Q

Pyridoxal phosphate (PLP) is the active form of what vitamin?

It is required for what types of reactions?

A

vitamin B6

PLP is the quintessential coenzyme of amino acid metabolism & is required for transamination, deamination, decarboxylation, beta-elimination, and gamma-elimination reactions involving amino acids

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12
Q

What is transamination?

What co-enzyme is required for this reaction? Is this a reversible step?

A

the process of removing nitrogen from amino acids

it is transferred as an amino group to a-keto acid forming different amino acid

The reactions are reversible & use pyroxal phosphate (PLP)

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13
Q

The carbon skeleton of all non-essential amino acids (other than tyrosine) is derived from what precursor?

Tyrosine is derived from what precursor?

Cysteine requires what additional essential amino acid?

A

All aa except tyrosine: glucose

Tyrosine: phenylalanine

cysteine: requires methionine for its sulfur

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14
Q

What 4 non-essential amino acids are directly derived from glucose & intermediates of glycolysis?

Which 6 non-essential amino acid are derived from the TCA cycle? Which specific components of the TCA cycle?

A
  • Glucose & its glycolysis intermediates
    • Glycine
    • Serine
    • Alanine (pyruvate)
  • TCA
    • Citrate
      • Glutamate
      • glutamine
      • proline
      • arginine
    • a-ketoglutarate
      • aspartate
      • asparagine
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15
Q

As amino acids are degraded, their carbons can be converted to what two structures?

A
  1. compounds that produce glucose in the liver (pyruvate and the TCA-cycle intermediates a-ketoglutarate, sucinyl-CoA, fumarate, and oxaloacetate )
    • glucogenic
  2. ketone bodies or their purecursors (acetoacetate and acetyl-CoA)
    • ketogenic
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16
Q

All amino acids are glucogenic EXCEPT -

A

EXCLUSIVELY ketogenic

lysine & leucine

17
Q

What amino acids are both glucogenic & ketogenic?

A
  • tyrosine
  • phenylalanine
  • threonine
  • isoleucine
  • tryptophan
18
Q

Which amino acids can be converted into pyruvate?

A
  • Pyruvate
    • threonine
    • tryptophan
    • glycine
    • alanine
    • serine
    • cysteine
19
Q

What amino acids can be converted to a-ketoglutarate?

A
  • a-ketoglutarate
    • glutamate
    • arginine
    • histidiine
    • glutamine
    • proline
20
Q

What amino acids can be converted to Succinyl CoA

A
  • Succinyl CoA
    • Valine
    • Threonine
    • Isoleucine
    • Methionine
21
Q

What amino acids can be converted to fumarate?

A
  • Fumarate
    • Asparatate
    • Tyrosine
    • Phenylalanine
22
Q

What amino acids can be converted to oxaloacetate?

A
  • oxaloacetate
    • aspartate
    • asparagine
23
Q

What amino acids are degraded to acetyl CoA?

What amino acids are degraded to HMG CoA?

What amino acids are degraded to Acetoacetate?

A
  • Acetyl CoA
    • threonine
    • lysine
    • isoleucine
    • tryptophan
  • HMG CoA
    • leucine
  • Acetoacetate
    • phenylalanine
    • tyrosine
24
Q

Describe the process of serine synthesis from glucose.

and the degradation of serine to glucose

What are the two regulatory steps?

A
  • When serine levels are high, it represses the production of 3-phosphoglycerate that converts 3-phosphoglycerate to 3-phosphyhydroxypyruvate
  • When serine levels are high it also inhibits the phosphoserine phosphatase that is responsible for the conversion of 3-phospho-L-serine to serine
25
Q

Glycine can be synthesized from what two precursors?

A
  • serine (requires PLP & FH4)
  • threonine (to lesser extent, also requies PLP)
26
Q

How can glycine cause kidney stones?

A
  • Glycine can be oxidized by D-amino acid oxidase to glyoxylate
  • glyoxylate can be oxidized to oxalate
  • oxalate is not very soluble & tends to precipitate in kidney tubules, leading to formation of kidney stones
27
Q

How is energy derived from glycine?

A

through a dehydrogenase (glycien cleavage enzyme) that oxidizes glycine to CO2 and ammonia