Products of S cerevisiae cis-prenyltransferase activity in vitro.
Products of cis-prenyltransferase activity, the first committed enzyme of the dolichol biosynthetic pathway, have been characterized in Saccharomyces cerevisiae. The evidence based on the results of ion exchange, HPTLC chromatography and acid phosphatase digestion has been presented indicating that the final product of the enzyme action in vitro is free polyprenol and not polyprenol mono- or diphosphate. On the other hand, the results of HPLC analysis confirmed that in vivo yeast accumulate alpha-saturated polyprenols (dolichols). Phosphorylation of endogenous dolichols by cytidine triphosphate (CTP)-dependent kinase is demonstrated. The hypothesis is put forth that in S cerevisiae free polyprenol is the substrate for the alpha-reductase responsible for its conversion to dolichol which in turn is phosphorylated into its active form: dolichyl phosphate.
Szkopińska
A
A
Institute of Biochemistry and Biophysics PAS, Warsaw, Poland.
Karst
F
F
Palamarczyk
G
G
D002848:Chromatography, DEAE-Cellulose; D002851:Chromatography, High Pressure Liquid; D004122:Dimethylallyltranstransferase / Q000378:metabolism*; D066298:In Vitro Techniques; D007536:Isomerism; D012441:Saccharomyces cerevisiae / Q000201:enzymology*
D004122:Dimethylallyltranstransferase