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29 Cards in this Set
- Front
- Back
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What are the two metabolic classifications that are used for amino acids?
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Essential and non-essential
Glucogenic and ketogenic |
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List the 9 essential amino acids
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Leucine
Phenylalanine Valine Methionine Isoleucine Lysine Threonine Histidine Tryptophane |
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List the 9 essential amino acids:
Leucine |
1.2 g/day used for fuel in the brain and muscle
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List the 9 essential amino acids:
Phenylalanine |
1.1 g/day used to form tyrosine
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List the 9 essential amino acids:
Valine |
1 g/day used for fuel in the brain and muscle
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List the 9 essential amino acids:
Methionine |
1 g/day that forms cystein and S-adenosylmethionine (SAM)
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List the 9 essential amino acids:
Isoleucine |
950 mg/day used for fuel in brain and muscle
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List the 9 essential amino acids:
Threonine |
500 mg/day used for O-linked glycosylation and for hormone regulated phosphorylation in proteins
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List the 9 essential amino acids:
Lysine |
800 mg/day that is a component of collagen and needed for wound healing
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List the 9 essential amino acids:
Histidine |
350 mg/day used to form histamine and carnosine (treats congestive heart failure)
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List the 9 essential amino acids:
Tryptophane |
250 mg/day used to form niacin, serotonin, and melatonin
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List the 5 nonessential amino acids?
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Alanine
Aspartic Acid Asparagine Glutamic Acid Serine |
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List the 7 conditionally essential amino acids?
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Glutamine
Glycine Proline Arginine Tyrosine Cysteine Taurine |
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What tissue catabolizes most of the amino acids in blood or that come from a recent meal?
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Liver
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How many grams of protein are synthesized each day in a typical person?
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300 grams/day
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why does protein breakdown and then get resynthesized on a regular basis?
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To prevent accumulation of abnormal proteins
To allow rapid changes in protein concentration To have readily available sources of AAs |
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What are the two ways of getting nitrogen out of amino acids?
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Transamination reaction produces aspartate
Oxidative deamination producing ammonium ions |
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Why is glutamate dehydrogenase such an important enzyme in amino acid metabolism?
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It releases ammonia in the liver and traps ammonia in extrahepatic tissues 9for urea cycle)
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What are ALT and AST?
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ALT – alanine amino transferase
AST – aspertate amino transferase |
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how are ALT and AST used to look at liver function?
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ALT and AST indicate hepatocellular activity
Alkaline phosphatase indicates obstructive injury |
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what else besides ALT and AST is used to see how well the liver is working?
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Bilirubin indicates excretory function issue
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what vitamin is required for ALT and AST activity and what happens when this vitamin is deficient?
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Vitamin B6 is necessary for ALT and AST activity
Ammonia production is increase in a B6 deficienty and can cause micrcytic hypochromic anemia |
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List the 4 major keto acids that are used to accept nitrogen in transamination reactions?
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Keto-gluterate to glutamate
Oxaloacetate to aspartate Pyruvate to alanine Glyoxalate to glycine |
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What two enzymes are used to trap ammonia?
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Glutamate dehydrogenase
Glutamine Synthase |
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Go through the process that the liver uses to remove nitrogen from the blood to form urea?
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Glutamate dehydrogenase is used to remove the Nitrogen group from an amino acid using NAD+ and H2O
The ammonia is then trapped and sent to the urea cycle |
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Glucose/Alanine Cycle
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Alanine and α-ketogluterate are reacted by ALT to produce pyruvate and glutamate
Glutamate is the reacted with AST and GDH to produce pyruvate for the TCA |
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how does nitrogen get into the liver from AA?
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Basically, all Nitrogen is shuttled onto glutamate or glutamine and then trapped in the liver
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What is the rate-limiting step in urea synthesis?
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Carbamoyl Phosphate Synthetase I (CPS-I) is the rate limiting enzyme used in the addition of CO2, NH3, and phosphate
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how is Carbornoyl Phosphate Synthetase 1 enzyme regulated?
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Based on the availability of ammonia or aa to liver, the concentration of intermediates, and the protein in the diet
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