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