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29 Cards in this Set
- Front
- Back
8 dietary essential AA
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Phenylalanine
Valine Threonine Tryptophan Isoleucine Methionine Histadine Arginine Lysine Leucine |
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Transaminases use what as a coenzyme
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pyridoxal phosphate
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Oxidative deamination rxn
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glutamate + NAD + H2O -> alpha ketoglutarate + aammonia + NADH .............. the enzyme is glutamate dehydrogenase
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L and D AA oxidases produce which toxic chemical
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hydrogen peroxide
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glucogenic metabolism of AA
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AA whose metabolism yields an intermediate of TCA or gluconeo
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glucogenic AA increase levels of what
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blood glucose levels
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Ketogenic metabolism of AA
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yields acetyl coA
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ketogenic AA increase levels of what
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ketone bodies
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which molecules go directly into gluconeo from gluc AA
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pyruvate and oxaloacetate
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cystinuria
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membrane transport defects
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phenylketonuria
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phenylalanine hydroxylase deficiency so phenylalanine does not get converted into tyrosine
increases ketones phenylpyruvate can be detected in urine |
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MSUD
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branched chain alpha ketoacid dehydrogenase deficiency
increases the branched chain AA or alpha keto acid Neurological problems and death common |
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Alkaptonuria
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homogentisate oxidase deficiency (intermediate of tyrosine metabolism)
urine darkens on standing arthritis common |
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1 carbon metabolism used for
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purine and pyrimidine synthesis (5,10 methylene THF)
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methane carried by
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s-adenosylmethionine (used for methylating DNA and histones)
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methanol, formaldehyde and FA carried by
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THF
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CO2 carried by
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biotin
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5,10 methylene THF can be produced by
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serine and glycine
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5,10 methylene THF reduced to 5 methyl THF which is used for the conversion of
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homocysteine to methionine
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bacterial chemotherapy
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sulfonamides are structural analogs to p-aminobenzoic acid, which inhibits them from making folic acid
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cancer chemotherapy
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methotrexate an analog of dihydrofolate and inhibits reduction of dihydrofolate to THF
no folic acid means no DNA synthesis and decrease in cancer |
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zymogen
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inactive proteases
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pepsin is located where and liberates what
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stomach, large fragments of proteins
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trypsinogen is converted to what by what
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enteropeptidase and trypsin
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can trypsin autocatalytically convert more trypsinogen to trypsin?
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yes
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regulatory and structural proteins (collagen) have what kinds of turnovers
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rapid and slow
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glucocorticoids have which influence on protein turnover
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rapid turnover for muscle energy
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insulin has what effect on protein turnover
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decreased turnover
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UBI process
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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 |