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.
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Metabolite, substrate for monoterpene synthase.[1]
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Bottomless glass bottle. Contents are inside inserted fused cone.
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
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
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(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
Old substrates for new enzymes of terpenoid biosynthesis.
Jörg Bohlmann et al.
Proceedings of the National Academy of Sciences of the United States of America, 106(26), 10402-10403 (2009-06-26)
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