Glucosaminephosphate synthase of human liver.
Although human liver contains glucosaminephosphate synthase (glucosaminephosphate isomerase (glutamine-forming), EC 5.3.1.19), its activity is rapidly lost during the course of extraction. The inactivation, however, is largely prevented if the extraction medium contains isopropanol at 1% concentration; using these "stabilized" extracts, the glucosaminephosphate synthase activity of human liver has been shown to be similar to the activity previously reported in rat liver. The enzyme precipitated from these extracts by (NH4)2SO4 is inhibited by UDP-N-acetylglucosamine, the concentration required to produce a half-maximal inhibition being 6 muM. These results seem to be sufficient to postulate that glucosaminephosphate synthase is important for UDP-N-acetylglucosamine synthesis in human liver. In contrast to the rat liver enzyme, the (NH4)2SO4-precipitated human liver enzyme is resistant to trypsin and undergoes no conversion reaction when incubated with glucose 6-phosphate.
D002238:Carbohydrate Epimerases / Q000378:metabolism*; D004355:Drug Stability; D005945:Glutamine-Fructose-6-Phosphate Transaminase (Isomerizing) / Q000302:isolation & purification / Q000378:metabolism*; D006801:Humans; D007700:Kinetics; D008099:Liver / Q000201:enzymology*; D011180:Postmortem Changes; D014357:Trypsin / Q000494:pharmacology; D014537:Uridine Diphosphate N-Acetylglucosamine / Q000494:pharmacology
D014537:Uridine Diphosphate N-Acetylglucosamine; D005945:Glutamine-Fructose-6-Phosphate Transaminase (Isomerizing); D014357:Trypsin; D002238:Carbohydrate Epimerases