AminotransferaseTransaminationTransaminasePyridoxal phosphateOxidative deaminationL-glutamate dehydrogenaseGlutamate synthetaseGlucose-alanine cycleAmmonotelicUreotelicUricotelicUrea cycleUreaCreatine kinaseEssential ===[[amino acidsKetogenicGlucogenicTetrahydrofolateS-adenosylmethioninePhenylketonuriaMixed-function oxidaseAlkaptonuriaMaple syrup urine diseaseMost essential amino acids in biology glutamine glutamate aspartate and alanine gastrin pepsinogensecretincholecystokinincarboxypeptidaseaminopepsidasePLPPLP is bond to the Lys residue and forms an internal aldiminewhen substrate binds, it becomes external aldimine form three different fates for acid oxidation]]===deaminationracemizationdecarboxylation L-glutarate dehydrogenase serves as the only enzyme to utilize two molecules, both NAD+ or NADP+ as substrateglutamate dehydrogenaseL-glutamine the carrier of amino groupglutamate dehydrogenase and glutaminase glucose alanine transportcarbamoyl phosphate synthetase 1 mitochondria urea cyclecarbamoyl phsophate synthetase 2 mitochondria, pyrimidine synthesiscarbamoyl phosphate and ornithine citrulline citruyl AMP argininosuccinate fumarate and arginine ornithineornithine transcarbamoylaseornithine from glutamatefive enzyme in urea cycleTwo ATP included in the formation of carbamoyl phosphatebicarbonate and ATP anhydride replacement ATP ===[[oxidative phosphorylationcrbomylphosphate synthetase ornithine trancarbamoylaseargininosuccinate synthetase argininosuccinasearginasemalate aspartate shuttleaspartate argininosuccinate shuntmalate alpha-ketoglutarate glutamate aspartate malate and aspartate 4 carbonglutamate and alpha-ketoglutarate 5 carbonaspartate aminotransferaseaspartate aminotransferaseglutamate oxaloacetate aminotransferaseAAT and GOTcreatine kinasecarbamoyl phosphate synthetase 1 arginine surplus and N-acetylglutamate activate N-acetylglutamate synthasehyperammonemia]]===