Flashcards in Intro to aa Deck (26):
Which two amino acids do not have a corresponding tranaminase?
What are the functions of transaminiases?
Tranform amino acids into their alpha-keto acids and back.
What is required for all transaminase reactions?
Vitamin B6 (PLP)
True or false, tranamination reactions are freely reversible
What is the precursor for alanine?
Which reaction does ALT catalyze?
pyruvate to alanine (via E +aKG)
What is a major reason ALT is important?
It allows muscles to transport pryruvate as an alanine to the liver during fasting. Pyruvate can then be used in gluconeogenesis.
What is the enzyme AST used for?
To catalyze the reaction from OAA to D (via E/aKG)
How is asparagine made?
From aspartate via ATP + E and asparagine synthase
Where is AST primarily found?
liver, cardiac and skeletal muscles, kidneys
Where is ALT primarily found?
Liver --this is why it is diagnostic for liver damage.
What does secretin cause the release of?
What does cholecystokinin cause the release of?
Which enzymes are activated by entreopeptidase?
What is the ratio of poly peptides to free amino acids after degradation by pancreatic proteases?
Hartnup disease is the result of what? What are the symptoms? How is it treated>
Cannot uptake large, neutral amino acids
Results in pellegra due to no niacin
Treatment with niacin and large protein diet.
Celiac disease is caused by an immune reaction to what part of gluten?
The body has how much free amino acids in the free amino acid pool?
aKG and OAA are precursors to what amino acids?
pyruvate and 3PG are precursors for which amino acids?
Glutamate dehydroenase gets its amino group from where?
Free ammonium ion
Glutamine synthetase gets its amino group from where?
Free ammonium ion
ALT forms what from what
Alanine from Pyruvate
Where does N get its amine from?
Homocysteine uria is a problem with what enzyme? Symptoms? Treatment?
Lens dislocation, osteoporosis, MR, thromboembolism
Low M, high S diet,