Identity of GD1C, GT1a and GQ1b synthase in Golgi vesicles from rat liver.
Competition experiments using GM1b, GD1a and GT1b as substrates, and as mutual inhibitors for ganglioside sialyltransferase activity in preparations of Golgi vesicles derived from rat liver, suggested that sialyl transfer to these three respective compounds, leading to gangliosides GD1C, GT1a and GQ1b, respectively, is catalyzed by one enzyme. These results are incorporated into a model for ganglioside biosynthesis and its regulation.
Iber
H
H
Institut für Organische Chemie und Biochemie der Universität Bonn, FRG.
Sandhoff
K
K
D000818:Animals; D001665:Binding Sites; D001667:Binding, Competitive; D002384:Catalysis; D005732:Gangliosides / Q000096:biosynthesis*; D006056:Golgi Apparatus / Q000201:enzymology* / Q000378:metabolism; D007700:Kinetics; D008099:Liver / Q000201:enzymology* / Q000378:metabolism; D008956:Models, Chemical; D019158:N-Acetylneuraminic Acid; D051381:Rats; D012794:Sialic Acids / Q000378:metabolism; D012799:Sialyltransferases / Q000037:antagonists & inhibitors / Q000378:metabolism*
D005732:Gangliosides; D012794:Sialic Acids; D012799:Sialyltransferases; D019158:N-Acetylneuraminic Acid