Block 6 amino acid questions from back of packet
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| During protein digestion, the pancreas and stomach secrete zymogens. What is their function? What activates them? | zymogen are inactivaed proteins that are activated by enteropetidase or trypsin. Then the break down proteins to aa parts
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| during the well-fed state, what pathways are active and utilize amino acids? | synthesize proteins, synthesis purines and pyrimidines, heme groups and neurotransmiters
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| What happens to excess amino acids in the well-fed state? | go into TCA cycle and glycolysis to make ATP
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| In the fasting state, what is the source of amino acids (particularly alanine) for support of gluconeogenesis? | muscle proteins are broken down, N transfered to pyruvate which becomes alanine and sent to the liver.
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| What sequesters ammonium ions in peripheral tissues? | glutamine synthase converts it to glutamine so it is not reactive
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| What is present in kidney and induced by metabolic acidosis? | glutaminase does the reverse of glutamine synthase to manage acid base balance
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| What converts alanine to pyruvate? | ALT - alanine aminotransferase
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| What results in the formatin of alpha-ketoglutarate + NADH | AST - asparate aminotransferase
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| What is the difference between glucogenic and ketogenic amino acids? | glucogenic are derived from glucose
Keto-genic are derived from acetyl-CoA
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| What two compounds are responsible for the supplying urea with its N-atoms? | aspartate and ammonium
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| The rate limiting step(s) in urea synthesis are located in which subcellular organelle? | mitochondria
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| An infant in respiratory distress has lab values with depressed BUN. Ammonium and glutamine levels are elevated. What disorder might be suspected? | ? carbamoyl phosphate synthetase-1 deficiency
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| Big Girl consumes a high protein meal. What would expect this person BUN to be 2 hours after the meal compared to a person that consumed a high fat meal? a high carb meal? | BUN - high protein = high
carb and fat = lower
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| mother brings in infant with funny sweet smelling urine and lethargy. What is the problem? What labs should be ordered? | Maple Syrup Urine disease - test by measuring branched chain amino acids, especially valine, isoleucine and leucine
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| What is as a frequent condition that results from homogentisic acid oxidase deficiency | cardiovascular disease
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| What is the cause of homocystinemia / homocystinuria? | defect in cystathionine synthetase
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| If a persons bilirubin and AST are elevated, what might be the condition? | viral hepatisis
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| If you have microvascular occlusion and jaundice with unconjugated bilirubin greater than conjugated bilirubin, what is the disorder? | sickle cell crisis, thalasemia, or G-6PDH deficiency episode
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| When are ferochelatase enzymes inhibited? | lead poisoning
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| what might occur if the Km of UDP-glucuronyl transferase is elevated by missense mutation? | Gilbert syndrome or Criglar-Najar
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| The two substates required for the synthesis of gama-aminolevulinic acid (ALA) and ultimately heme are? | sucinyl-CoA + glycine
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| Before amino acids can be oxidized to CO2 + H2O +ATP, what reaction has to occur? To what is the amino acid converted? | Aminotransferases exchange amino groups on amino acids for keto groups on alpha ketoacids
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| If a patient is have Kussmal breathing what enzyme is cranking hard in the kidneys? | It is metabolic acidosis, so glytamate dehydrogenase?
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| What enzyme requires ATP as a cofactor? glutamine synthetase, glutaminase, glutamate dehydrogenase, aminotransferase | glutamine sythetase
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| What enzyme requires either NAD or NADP as a cofactor? glutamine synthetase, glutaminase, glutamate dehydrogenase, aminotransferase | glutamate dehydrogenase
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| What are the four enzymatic activites and the critical enzymes of amino acid metabolism? | 1. amination by glutamine synthetase
2. deamination by glutaminase
3. transamination by alanine transferase
(ALA)& aspartate transferase (AST)
4. deamination via glutamate dehydrogenase
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