Biochemistry 2 Palmer Exam 3 protein metabolism
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| what is a ketoacid | what is left when the amino group is removed from an amino acid
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| alanine goes to what | pyruvate
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| glutamine goes to glutamate which goes to | alpha-ketogluterate
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| asparagine goes to asparatate which goes to | oxaloacetate
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| to make alpha ketoacid knockoff _____ and put on ____ | NH3, O
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| what are the 2 ketogenic amino acids that cannot turn into glucose | leucine and lysine
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| what are the 6 amino acids that can be oxidized by muscle | 1)leucine
2)isoleucine
3)valine
4)glutamate
5)aspartate
6)asparagine
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| what amino acid has the greatest intracellular/extracellular ratio in muscle | glutamate >50 to 1
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| what is anaplerosis | adding to the pathway
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| what is cataplerosis | taking from the pathway
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| what amino acid has the worst intracellular/extracellular ratio in muscle | alanine 6-10 to 1
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| what imports glutamate into the muscle | liver, digestive system, immune system
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| what does the muscle export to the liver, digestive system, immune system | nitrogen
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| what enzyme is used to add nitrogen to glutamate to make it glutamine | glutamine synthetase
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| glutamine goes to cells needing nitrogen like | gut and immune cells
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| what enzyme converts glutamine into glutamate | glutaminase
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| what enzymes are released most from the muscle | glutamine and alanine
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| what happens to the glutamate and alanine concentrations during low intensity exercise | -20% decrease in glutamate concentrations
-no change in alanine concentration
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| what happens to muscle glutamate and alanine concentrations during moderate intensity exercise | -40% decrease in glutamate concentration during 1st minute
-60% increase in alanine concentration
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| what are the plasma trends with exercise | -glutamate CONCENTRATION decrease
-alanine CONCENTRATION increases
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| how does nitrogen remove amino groups | -transamination
-oxidative deamination
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| most amino acids transfer their alpha-amino group to | alpha-ketoglutarate
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| what does transamination result in | glutamate and an alpha-keto acid
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| the main way nitrogen leaves the muscle is as | -glutamine
-alanine
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| what are the entry points to the urea cycle in the liver | 1)glutamate dehydrogenase
2)aspartate amino transferase/glutamate oxaloacetate transaminase
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| what does glutamate dehydrogenase do | deaminates glutamate
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| what does aspartate amino transferase do | transfers amino groups from glutamate to oxaloacetate, forms aspartate
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| what are the unique abilities of the liver | 1)urea cycle
-liver has ability to deal with ammonia
2)gluconeogenesis
-turn alpha-ketoacids into glucose
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| what are the 4 amino acids in the urea cycle | 1)citrulline
2)argininosuccinate
3)arginine
4)ornithine
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| when a branch chain amino acid is oxidized in muscle it must get rid of | the nitrogen
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| alpha ketogluterate takes the nitrogen and | becomes glutamate
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| glutamate gets rid of the nitrogen and gives it to | pyruvate
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| pyruvate becomes | alanine
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| alanine leaves the muscle and | goes to the liver (glucose-alanine cycle)
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| alanine and other excess AA go to | the liver
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| alanine and other excess AA must get rid of | the nitrogen
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| alanine and other amino acids turn into | alpha-ketoacids which turn into: glucose, fat, CO2, and ATP
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| glutamate has what 2 choices as to how it gets rid of the nitrogen | 1)glutamate dehydrogenase
2)aspartate aminotransferase
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| glutamate dehydrogenase makes the NH3 join with CO2 to make what | carbamoyl phosphate
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| carbamoyl phosphate enters what cycle | urea cycle
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| aspartate aminotransferase transfers nitrogen from | glutamate to oxaloacetate
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| oxaloacetate turns into | aspartate
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| aspartate enters the | urea cycle
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| 2 amino acids that are NOT glucogenic | 1)leucine
2)lysine
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| main anaplerotic amino acid to the TCA: | glutamate
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| 3 AA that donate nitrogen for purines and pyrimidines | 1)glutamine
2)aspartate
3)glycine
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| ALT alanine amino transferase | alanine+alpha-ketoglutarate <--> pyruvate+glutamate
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| AST aspartate amino transferase | oxaloacetate+glutamate <--> aspartate+alpha-ketoglutarate
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