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20 Cards in this Set
- Front
- Back
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Nutritional Marasmus
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A general malnutrition state in which there is a deficiency in BOTH protein and calories
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Kwashiorkor
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A condition with only a protein deficiency but sufficient calories
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What are the ketogenic amino acids and what do they lead to?
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Leucine and Lysine --> become ketones/acetyl CoA
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What are the glucogenic amino acids
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All except leucine and lysine --> become glucose
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Which amino acids are both glucogenic and ketogenic
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The three aromatic amino acids and leucine:
Tryptophan Tyrosine Phenylalanine Isoleucine TIP/TB (B = both) |
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Transamination - catalyzed by? reversible or irreversible? can be used for what 2 processes? what alpha-keto acid is made to what AA by the aminotransferase?
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-Most common way to remove the amino group
-Catalyzed by number of aminotransferases and PLP as the coenzyme (pyridoxal phosphate) -Reactions are freely reversible -Can be used for either the removal of the amino group or for the synthesis of the amino acid from the appropriate alpha-keto acid -Most aminotransferases use alpha-ketoglutarate as the acceptor of the amino forming glutamic acid. process: amino acid --> alpha-keto acid. the removed amino group turns for alpha-KG to glutamic acid |
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what amino acids are converted to what alpha - keto acids
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aspartic acid --> OAA
alanine --> pyruvate glutamate --> alpha-ketoglutaric acid |
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Which amino acids make pyruvate via deamination
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serine, cysteine, alanine
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Non-oxidative Deamination: which amino acids can be deaminated this way? what are the end products?
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Cysteine, Serine, Threonine can be deaminated by the removal of H2S or H2O. A deHase is used on them to form the alpha-keto acid and NH3
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What are the 2 oxidative deamination methods?
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1) Glutamic DeHase (GDH)
2) Amino Acid Oxidases |
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Amino Acid Oxidases are also what? what do they yield upon rxn?
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They are flavoproteins. They yield hydrogen peroxide and the alpha-keto acid
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GDH - yields what, uses what AA
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catalyzes the oxidative deamination of GLUTAMIC ACID. Uses NAD or NADP and yields alpha-ketoglutaric acid and NH3. THIS IS THE ONLY AMINO ACID DEHASE FOUND IN HUMANS!
-it is freely reversible |
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the 2 amino groups of urea come from what? what else is needed?
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carbamoyl-phosphate donates the NH2. GDH is needed for the conversion from glutamate to alpha-KG, which gives one NH3 for urea. this is why GDH is so important.
aspartic acid donates the NH3. OAA is needed for the production of aspartic acid from asp-transaminase going in reverse. |
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N-acetyl-glutamate
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is an allosteric activator for CPS-1. its concentration increases upon ingestion of a high protein meal so that the catabolic process of the urea cycle can begin
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rate limiting step for urea cycle
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the reaction of NH3+CO2+ATP --> carbamoyl-P via CPS-1
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start products of urea cycle?
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carbamoyl-P and ornithine
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end products of urea cycle?
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urea and ornithine
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which enzymes of urea cycle are found in matrix and which are found in cytosol?
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CPS-1 and OTC are found in matrix.
Argininosuccinate sythetase, lyase, and arginase are all found in cytosol |
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If ammonia is generated in peripheral tissues, like the brain and muscle, what happens?
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Glutamic acid reacts with the NH3 and through GLUTAMINE SYNTHETASE it forms glutamine. This glutamine then travels in the blood fo the kidney, lovery, or intestinal cells, all of which contain the enzyme GLUTAMINASE which converts the glutamine back to glutamic acid and NH3. Then urea cycle and excretion
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What kinds of genetic defects happen from errors in urea cycle enzymes?
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from OTC damage, X-linked diseases occur.
all the other enzyme errors cause autosomal recessive diseases |
