Protein and Amino Acid Metabolism I Flashcards
what secretes HCl
parietal cells
what secretes pepsin
chief cells
endopeptidase
it cleaves internal peptide bons within proteins
what is the optimal pepsin activity pH
2
waht does secretin stimulate
acinar cells of pancreas to release HCO3- rich fluid
function of cholecystokinin
release of bile from gall bladder
release of digestive enzymes from pancrease
how does trypsinogen get converted to active trypsin
enteropeptidase
what is the liminal surface of epithelical cells of small intestine rich in
endopeptidase and aminopeptidase activity
waht are teh small neutral AA
gly, ser, ala
waht are teh alrge neurtral amino acids
leu, ile, phe, try, al, met, trp, gln
what are teh basic amino acids
arg, lys
what are teh acidic amino acids
asp, glu
what happesn when peptides get inside the epithelial cell
get rapidly hydrolysed by peptidases
how do free amino acids in epithhalial cells get to portal circualtion
facilitated diffusion into capillaries
how does hartnup disease work
blocks acitivty of AA transport that is responsible for uptake of large neutral amino acids
symptoms of hartnup disease
pellagra
how do you treat hartnup disease
niacin
what is celiac caused by
immune response to alpha-gliadin
how does nitrogen get into the body
dietary protein
how is nitrogen excreted
urea in urine
when would you get a negiatve nitrogen balance
not enough protein intake
when do you get a positive nitrogen balance
net increase in body protein (prengnat women, growing kids)
what does PvT Tim Hall stand for
pheny valine threonine tryptophan isoleucine methionine histidine arg leu lys
what is the is the essential AA for infants
arginine
aKG and OAA are precursors of waht
glutamate glutamine proline argingine aspartate asparagine
pyruvate and 2-phosoglycerate are precursors of waht
alanine
serine
tyrosine is formed from waht
phenylalaine
what is cysterine formed from
serine and methionine
how can glutamate be gerneated
tranaminatino of aKG
deamidation of glutamine
what does the transaminatino of glutamate require
vit B6
how do you get glutamine from glutamate
glutamine synthetase
why is glutamine productio nin peripheral tissues important
removal of ammonium ions
glutamine produced in peripheral tissues is aborbed by what
kidney, liver, gut
what hydrolyzes the amide group in glutamine
glutaminase
what happens to glutamine that goes to kidney
gets eliminated
what happens to glutamine tha tgoes to liver
urea cycle
what happens to glutamine tha tgoes to gut
goes from portal circulation into liver
functino of aminotransferases
catalyze interconvertion of AA and theri corresponding alpha ketoacids
what amino acids don’ thave correspondign aminotransferase enzymes
threonine and lysine
how is glutamate related to alpha keto acid
servers as an amino group donor
how is alpha ketoglutarate realted to glutamate
serves as an amino group acceptor
what do all amino transferases require
PLP - vit B6
are the reactions catalyzed by aminotransferases reversible
yes
what do you use to syntheize alanine from pyruvate
ALT
what does the ALT reaction play an important role in
connect muscle and liver metabolism during early fasting
