12436
Neryl pyrophosphate lithium salt
≥95.0% (TLC)
Synonym(s):
(Z)-3,7-Dimethyl-2,6-octadien-1-yl pyrophosphate lithium salt, Neryl diphosphate lithium salt
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About This Item
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assay
≥95.0% (TLC)
storage temp.
−20°C
Application
Neryl pyrophosphate, the cis isomer of geranyl pyrophosphate, may be used to characterize and study the kinetics of enzymes such as 1,8-cineole synthase, farnesyl pyrophosphate synthase, pinene cyclase and geranyl pyrophosphate:sabinene hydrate cyclase.
Biochem/physiol Actions
Metabolite, substrate for monoterpene synthase.
Packaging
Bottomless glass bottle. Contents are inside inserted fused cone.
signalword
Warning
hcodes
Hazard Classifications
Eye Irrit. 2 - Skin Irrit. 2 - STOT SE 3
target_organs
Respiratory system
Storage Class
11 - Combustible Solids
wgk_germany
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
Certificates of Analysis (COA)
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Archives of biochemistry and biophysics, 309(1), 184-192 (1994-02-15)
Geranyl pyrophosphate: 1,8-cineole cyclase (cineole synthase) catalyzes the conversion of geranyl pyrophosphate to the symmetrical monoterpene ether 1,8-cineole (1,3,3-trimethyl-2-oxabicyclo[2.2.2]octane) by a process thought to involve the initial isomerization of the substrate to the tertiary allylic isomer, linalyl pyrophosphate, and cyclization
The Journal of biological chemistry, 264(26), 15309-15315 (1989-09-15)
(+)-Pinene cyclase from sage (Salvia officinalis) catalyzes the isomerization and cyclization of geranyl pyrophosphate to (+)-alpha-pinene and (+)-camphene, and to lesser amounts of (+)-limonene, myrcene, and terpinolene, whereas (-)-pinene cyclase from this tissue catalyzes the conversion of the acyclic precursor
The Journal of biological chemistry, 264(31), 18598-18607 (1989-11-05)
A prenyltransferase purified from the commercial rubber tree, Hevea brasiliensis, that elongates existing cis-polyisoprene rubber molecules also catalyzes the formation of all trans-farnesyl pyrophosphate (t,t-FPP) from dimethylallyl pyrophosphate (DMAPP) and isopentenyl pyrophosphate (IPP). In assays of the latter activity trans-geranyl
Archives of biochemistry and biophysics, 264(2), 618-631 (1988-08-01)
A soluble enzyme preparation from the leaves of sweet marjoram (Majorana hortensis Moench) catalyzes the divalent cation-dependent cyclization of [1-3H]geranyl pyrophosphate to the bicyclic monoterpene alcohols (+)-[6-3H]cis- and (+)-[6-3H]-transsabinene hydrate, providing labeling patterns consistent with current mechanistic considerations. No free
Old substrates for new enzymes of terpenoid biosynthesis.
Proceedings of the National Academy of Sciences of the United States of America, 106(26), 10402-10403 (2009-06-26)
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