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J Biol Chem, Vol. 273, Issue 24, 14891-14899, June 12, 1998
From the Institute of Biological Chemistry, and the Department of
Biochemistry and Biophysics, Washington State University,
Pullman, Washington 99164-6340
Common sage (Salvia officinalis)
produces an extremely broad range of cyclic monoterpenes bearing
diverse carbon skeletons, including members of the
p-menthane (1,8-cineole), pinane (
- and 
-pinene),
thujane (isothujone), camphane (camphene), and bornane (camphor)
families. An homology-based polymerase chain reaction cloning strategy
was developed and used to isolate the cDNAs encoding three
multiproduct monoterpene synthases from this species that were
functionally expressed in Escherichia coli. The
heterologously expressed synthases produce (+)-bornyl diphosphate, 1,8-cineole, and (+)-sabinene, respectively, as their major products from geranyl diphosphate. The bornyl diphosphate synthase also produces
significant amounts of (+)--pinene, (+)-camphene, and (±)-limonene.
The 1,8-cineole synthase produces significant amounts of (+)- and
(
)--pinene, (+)- and ()--pinene, myrcene and (+)-sabinene, and the (+)-sabinene synthase produces significant quantities of
-terpinene and terpinolene. All three enzymes appear to be translated as preproteins bearing an amino-terminal plastid targeting sequence, consistent with the plastidial origin of monoterpenes in
plants. Deduced sequence analysis and size exclusion chromatography indicate that the recombinant bornyl diphosphate synthase is a homodimer, whereas the other two recombinant enzymes are monomeric, consistent with the size and subunit architecture of their native enzyme counterparts. The distribution and stereochemistry of the products generated by the recombinant (+)-bornyl diphosphate synthase suggest that this enzyme might represent both (+)-bornyl diphosphate synthase and (+)-pinene synthase which were previously assumed to be
distinct enzymes.
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