amino acid metabolism stack 1
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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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Created by:
El Diablo
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