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amino acid metabolism stack 1

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Question
Answer
Where is protein catalyzed in the body?   show
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What is the first step of breaking down proteins?   show
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show alpha-amino group is removed from the amino acid by a transaminase. This produces alpha-ketoacids  
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What happens to the alpha-ketoacids in liver?   show
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What is produced and secreted by the serous cells of the stomach? Its role?   show
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show It hydrolyzes large, denatured proteins to medium and small oligopeptides  
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Once proteins reach the intestine what chemical storm occurs? What initiates the storm?   show
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show trypsinogen converts to active form, trypsin. Trypsin cleaves to activate all the other zymogens.  
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show amino acids absorbed by the intestinal mucosal cells and released into portal system  
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show Extracellular low, Intracellular high  
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show ATP-dependent transport systems  
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show steatorrhea (lipid in the feces) and undigested protein in feces  
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show malabsorption resulting from immune-mediated damage to small intestine in response to ingestion of gluten  
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show cystinuria  
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How does cystinuria clinically present itself? What is the etiology?   show
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What amino acids appear in the urine with cystinuria?   show
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How does 90% of the nitrogen that enters the body via diet, exit the body?   show
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What fills the amino acid pool?   show
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show PEST are Pro-Glu-Ser-Thr, or proline, glutamin, serine and threonine. Proteins with these series have a very short half-live  
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show intracellular Extracellular such as collagen last from months to years  
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show synthesis proteins to replace rapidly turning over plasma proteins  
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show purines, pyrimidines, heme groups (porphyrins), neurotransmitters  
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show metabolized into product to enter various pathways such as glycolysis and TCA for energy production/ATP synthesis  
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show muscle proteins are broken down via proteolysis  
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show Glucose-Alanine cycle: transamination to alpha-ketoacid. Nitrogen transfered to pyruvate which becomes alanine. Alanine goes to liver and switches back to pyruvate while the nitrogen group goes to alpha ketoglutate which become glutamate=glyconeogen..  
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What must happen in order to use an amino acid for fuel?   show
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show Most is disposed as urea, a little remains as ammonia  
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What four things does the Nitrogen atom play a crucial role in building and regulation?   show
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When alpha-keto acids enter the TCA cycle what are the final products?   show
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Liver enzymes convert nitrogen groups to urea from what compounds?   show
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What is the most common inborn error of amino acid metabolism that causes mental retardation?   show
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How might a person with PKU look different?   show
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What rare disease involves homogentisic acid oxidase deficiency? Why? Symptoms?   show
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show Maple Syrup Urine D. due to inability to decarboxylate leucine, isoleucine and valine It can be lethal!  
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What will a B12 deficiency cause? Why?   show
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If you are low on B12, B6 and folate what pathway is in jeopardy? What condition will occur? treatmen?   show
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show Hyperammonemia  
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What are the two enzymes that must be known for hyperammonemia?   show
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Alcoholics and folks with hepatisis aquire a deficiency in which enzyme that brings on hyperammonemia?   show
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show X-linked recessive, and the most common of all the urea disorders  
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show 1. glutamine synthetase; 2. glutaminase; 3. transaminases: ALT & AST; 4. Glutamate Dehydrogenase  
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show amination: glutamate + ammonium NH4 + ATP = glutamine + ADP + Pi catalyzed by glutamine synthase!!!  
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show glutaminase catalzyes glutamine + H2O = glutamate + NH4+  
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show ALT: alanine aminotransferase AST: aspartate aminotransferase  
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show Named based on the starting amino acid, alanine or aspartate because the end product of both reactions is alpha-ketoglutarate  
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show They are intracellular enzymes. physical trauma or disease cause cells to lyse releasing them.  
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show Liver disease:viral hepatitis, toxic injury (alcoholism), prolonged circulatory collapse Non-liver: MI, muscle disorders  
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show glutamate dehydrogenase can catalyze reversible deamination from glutamate to alpha-ketoglutarate which release NH4 ions  
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show 1. glutamine synthetase 2. glucose-alanine pathway  
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show glutamine synthetase combines ammonia + glutamate = glutamine: nontoxic, travels in blood to liver. In liver it can be cleaved by glutaminase to release the NH$  
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show transamination: NH3 from glutamate put on pyruvate = alanine. alanine travels in blood to liver. switched back to pyruvate by ALT. ALT also puts the NH3 on alpha-ketoglutarate. Glutamate dehydrogenase then takes it off to send it for urea formation.  
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show glutamine synthetase binds NH3 to glutamate to make non-toxi glutamine  
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show glutaminase  
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If glutamine goes to the intestine, what enzyme kicks free the NH for export (via the portal vein) for trip liver and urea synthesis?   show
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