Lecture 5- Amino Acids and Nitrogen Flashcards
Are amino acids stored by the body? Y/N
No
Where are amino acids obtained from?
Diet
Synthesized de novo
Produced from normal protein degradation
What happens to excess amino acids?
They are rapidly degraded
What is the first phase of amino acid catabolism?
Removal of the a-amino groups forming
- ammonia
- the corresponding a-keto acid
What happens to the free ammonia that is removed in the first phase of amino acid catabolism?
A portion is excreted in the urine,
most is used in the synthesis of urea
What is the second phase of amino acid catabolism?
the carbon skeletons of the a-keto acids are converted to common intermediates of energy producing, metabolic pathways
Nitrogen enters the body in food, but how does the majority of it leave the body?
leaves as urea and ammonia
In the stomach, which enzyme hydrolyzes proteins?
pepsin
What enzymes act on proteins in the small intestine and what do they do?
Pancreatic proteases- cleave polypeptides
Aminopeptidases- produce even smaller peptides and free amino acids (cleave from amino end)
In the small intestines, what happens to the free amino acids?
taken into the enterocytes
What does the presence of the a-amino group on amino acids do?
keeps the amino acids protected from oxidative breakdown
What is the first step in the catabolism of most AA’s?
Transamination (transfer of their a-amino group to a-ketoglutarate), which is catalyzed by
aminotransferases
Which two amino acids do not participate in transamination in their catabolism, but instead use deamination?
Lysine
Threonine
What is the result of deamination?
produces a free ammonia
What is the major disposal form of amino groups derived from amino acids?
urea
What produces urea?
liver
What is the most important rate limiting step in the urea cycle, and what is its essential activator?
The conversion of CO2 and NH3 (ammonia) to carbamoyl phosphate by carbamoyl phosphate synthetase I.
N-Acetylglutamate is the essential activator
Disorder when too much ammonia is found in the blood
hyperammonemia
glucogenic vs. ketogenic AA’s
Glucogenic AAs- whose catabolism yields pyruvate or one of the intermediates of the TCA cycle
Ketogenic AAs- who catabolism yields either acetoacetate or one of its precursors (acetyl CoA or acetoacetyl CoA)
Which AAs are only glucogenic?
Alanine Arginine Asparagine Aspartate Glutamine Glutamate Glycine Proline Serine Histidine Methionine Threonine Valine
What AAs are glucogenic and ketogenic?
Tyrosine
Isoleucine
Phenylalanine
Tryptophan
What AAs are only ketogenic?
Leucine
Lysine
Arginine and proline can be synthesized from what?
Glutamate
Two main disorders of AA metabolism
Phenylketonuria (PKU)- results in over-accumulation of phenylalanine (deficiency of PHENYLALANINE HYDROXYLASE). Can cause mental retardation and other brain damage.
Albinism- lack of TYROSINASE, thus melanin not produced
What are porphyrins and what are the most prevalent in humans?
Cyclic compounds that readily bind metal ions (usually iron)
Heme
Major sites of heme biosynthesis?
Liver
Erythrocyte-producing cells of the bone marrow (~85%)
Which steps of the biosynthesis of heme happen where?
Initial reaction and the last 3 steps occur in the mitochondria.
Intermediate steps in the cytosol