A novel prenyltransferase, farnesylgeranyl diphosphate synthase, from the haloalkaliphilic archaeon, Natronobacterium pharaonis.
A novel prenyltransferase, farnesylgeranyl diphosphate (FGPP) synthase (EC 2.5.1.X), which synthesizes C25-prenyl diphosphate, was found in the haloalkaliphilic archaeon Natronobacterium pharaonis. It was separated from geranylgeranyl diphosphate (GGPP) synthase (EC 2.5.1.29), which synthesizes C20-prenyl diphosphate, a major prenyltransferase in this organism. The highest activity of FGPP synthase was observed when GGPP was used as the allylic substrate. FGPP synthase may synthesize a precursor for the C25 moiety of C20, C25 diether lipids using a longer allylic diphosphate, such as GGPP synthesized by GGPP synthase, rather than dimethylallyl diphosphate, which is the product of isopentenyl diphosphate isomerase.
Tachibana
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Department of Biology, Faculty of Science, Osaka City University, Japan.
D019883:Alkyl and Aryl Transferases; D002852:Chromatography, Ion Exchange; D051231:Farnesyltranstransferase; D006216:Halobacteriaceae / Q000201:enzymology*; D013379:Substrate Specificity; D014166:Transferases / Q000302:isolation & purification / Q000378:metabolism*
D014166:Transferases; D019883:Alkyl and Aryl Transferases; C086466:farnesylgeranyl diphosphate synthase; D051231:Farnesyltranstransferase