Evidence indicating that UDP-N-acetylglucosamine does not appear to stimulate hepatic microsomal UDP-glucuronosyltransferase by interaction with the catalytic unit of the enzyme.
The binding studies in this paper indicate that the catalytic unit(s) of microsomal UDP glucuronosyltransferase(s) is not accessible to N-ethylmaleimide or UDP-N-acetylglucosamine, when the enzyme is in its membrane environment. Thus a separate regulatory factor may exist within the endoplasmic reticulum membrane that mediates the stimulation of UDPglucuronosyltransferase(s) by UDP-N-acetylglucosamine. The possible role and the mode of interaction of the putative regulatory factor with the multiple forms of UDPglucuronosyltransferase are discussed.
D000818:Animals; D004589:Electrophoresis, Disc; D004721:Endoplasmic Reticulum / Q000201:enzymology; D005033:Ethylmaleimide / Q000494:pharmacology; D014453:Glucuronosyltransferase / Q000378:metabolism*; D007425:Intracellular Membranes / Q000201:enzymology; D008862:Microsomes, Liver / Q000201:enzymology*; D051381:Rats; D014537:Uridine Diphosphate N-Acetylglucosamine / Q000494:pharmacology*; D014539:Uridine Diphosphate Sugars / Q000494:pharmacology*
D014539:Uridine Diphosphate Sugars; D014537:Uridine Diphosphate N-Acetylglucosamine; D014453:Glucuronosyltransferase; D005033:Ethylmaleimide