Amino Acids via digestion
What are the ten essential amino acids
histidine, isoleucine, lysine, methionine, phenylalanine, threonine, tryptophan, valine.
How does the cell know to degrade a protein
Ubiquitin markers
19s 20s (a and b)
What is the first step of amino acid degradation?
What is the commitment step?
The formation of carbamoyl phosphate
DOUBLE JEOPARDY
What is the pathway via digestion of amino acids
It uses its glycine residue to attach to a lysine residue on the protein
What does 19s do?
unfolds proteins and inserts them into the 20s unit.
alanine (aminotransferase makes what and glutamate)
aspartate (aminotransferase makes what and glutamate)
pyruvate and oxaloacetate
where does the cycle take place
cytoplasm and mitochondria
What is the enzyme in the stomach that begins the digestion of amino acids?
pepsin, it operates at a pH of 2
What is the bond called when ubiquitin binds to a protein
isopeptide bond
What is the catalytic amino acid in 19s
threonine
What is glutamate converted to?
Ammonia, which is then degraded in the urea acid cycle
What enzyme converts carbamoyl phosphate into citruline
orthinine transcarbamylase
What is the next enzyme that further digests amino acids?
aminopeptidase N
What happens on E1
the nonactive form of ubiquitin links to e1 via a thioester bond
ubiquitin is then activated via the release of pyrophosphate
How does 20s break down the protein
nucleophiles attack and break apart the molecule.
what forms a Schiff base with the aminotransferases
pyridoxal phosphate
what amino acid does argininosuccinate synthase require?
aspartate
The release of hormones and sodium barcarbonate
What happens on e2 and e3
e2 just transfers it into e2 (middle man) e3 then reads the degron and
what is the molecule that removes ubiquitin?
isopeptidase
What amino acids can be directly converted into NH4+
Serine and threonine
how does arginine leave the cycle?
arginase turns it into urea