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29 Cards in this Set

  • Front
  • Back
8 dietary essential AA
Phenylalanine
Valine
Threonine
Tryptophan
Isoleucine
Methionine
Histadine
Arginine
Lysine
Leucine
Transaminases use what as a coenzyme
pyridoxal phosphate
Oxidative deamination rxn
glutamate + NAD + H2O -> alpha ketoglutarate + aammonia + NADH .............. the enzyme is glutamate dehydrogenase
L and D AA oxidases produce which toxic chemical
hydrogen peroxide
glucogenic metabolism of AA
AA whose metabolism yields an intermediate of TCA or gluconeo
glucogenic AA increase levels of what
blood glucose levels
Ketogenic metabolism of AA
yields acetyl coA
ketogenic AA increase levels of what
ketone bodies
which molecules go directly into gluconeo from gluc AA
pyruvate and oxaloacetate
cystinuria
membrane transport defects
phenylketonuria
phenylalanine hydroxylase deficiency so phenylalanine does not get converted into tyrosine

increases ketones

phenylpyruvate can be detected in urine
MSUD
branched chain alpha ketoacid dehydrogenase deficiency

increases the branched chain AA or alpha keto acid

Neurological problems and death common
Alkaptonuria
homogentisate oxidase deficiency (intermediate of tyrosine metabolism)

urine darkens on standing

arthritis common
1 carbon metabolism used for
purine and pyrimidine synthesis (5,10 methylene THF)
methane carried by
s-adenosylmethionine (used for methylating DNA and histones)
methanol, formaldehyde and FA carried by
THF
CO2 carried by
biotin
5,10 methylene THF can be produced by
serine and glycine
5,10 methylene THF reduced to 5 methyl THF which is used for the conversion of
homocysteine to methionine
bacterial chemotherapy
sulfonamides are structural analogs to p-aminobenzoic acid, which inhibits them from making folic acid
cancer chemotherapy
methotrexate an analog of dihydrofolate and inhibits reduction of dihydrofolate to THF

no folic acid means no DNA synthesis and decrease in cancer
zymogen
inactive proteases
pepsin is located where and liberates what
stomach, large fragments of proteins
trypsinogen is converted to what by what
enteropeptidase and trypsin
can trypsin autocatalytically convert more trypsinogen to trypsin?
yes
regulatory and structural proteins (collagen) have what kinds of turnovers
rapid and slow
glucocorticoids have which influence on protein turnover
rapid turnover for muscle energy
insulin has what effect on protein turnover
decreased turnover
UBI process
ATP needed to attach UBI to E1

UBI from E1 to E2

E3 recognizes target protein

UBI transferred from E2 to target

More UBI added

Polyubiquinated protein marked for degradation by proteases