76532
Geranyl pyrophosphate lithium salt
≥95.0% (TLC)
Synonym(s):
(E)-3,7-Dimethyl-2,6-octadien-1-ol trihydrogen pyrophosphate lithium salt, (E)-3,7-Dimethyl-2,6-octadien-1-yl pyrophosphate lithium salt, GPP-Li
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Biochem/physiol Actions
Metabolite in monoterpenoid biosynthesis, substrate for monoterpene synthases.
Packaging
Bottomless glass bottle. Contents are inside inserted fused cone.
Storage Class Code
11 - Combustible Solids
WGK
WGK 3
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Certificates of Analysis (COA)
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Neuroscience letters, 354(2), 107-110 (2003-12-31)
Statins were recently shown to possess anti-inflammatory activities, which might be responsible for their favourable effects in cardiovascular or CNS disorders independently from the inhibition of hydroxy-methyl-glutaryl CoA reductase. Here we investigated the effects of the statins lovastatin and mevastatin
The Biochemical journal, 386(Pt 1), 169-176 (2004-09-28)
UPPS (undecaprenyl pyrophosphate synthase) catalyses consecutive condensation reactions of FPP (farnesyl pyrophosphate) with eight isopentenyl pyrophosphates to generate C55 UPP, which serves as a lipid carrier for bacterial peptidoglycan biosynthesis. We reported the co-crystal structure of Escherichia coli UPPS in
Assay and drug development technologies, 5(2), 205-214 (2007-05-05)
A mix-and-read FlashPlate (PerkinElmer, Waltham, MA) assay for the enzyme farnesyl pyrophosphate (FPP) synthase (FPPS) was developed to rapidly measure both steps in the synthesis of FPP from dimethylallyl pyrophosphate (DMAPP). The assay used either DMAPP or geranyl pyrophosphate (GPP)
Journal of molecular biology, 404(5), 859-873 (2010-10-23)
Isoprenoids, most of them synthesized by prenyltransferases (PTSs), are a class of important biologically active compounds with diverse functions. The mint geranyl pyrophosphate synthase (GPPS) is a heterotetramer composed of two LSU·SSU (large/small subunit) dimers. In addition to C(10)-GPP, the
Bioorganic & medicinal chemistry letters, 20(19), 5781-5786 (2010-08-31)
A structure-based approach was pursued in designing novel bisphosphonate inhibitors of the human farnesyl pyrophosphate synthase (hFPPS). Preliminary SAR and structural evidence for the simultaneous binding of these inhibitors into the isopentenyl pyrophosphate (IPP) and the geranyl pyrophosphate (GPP) substrate
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