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Biochemistry 2 E3

Biochemistry 2 Palmer Exam 3 protein metabolism

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
Created by: ellerjason12