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(2E,6E)-farnesyl diphosphate
patchoulol + diphosphate
(2E,6E)-farnesyl diphosphate + H2O
patchoulol + diphosphate
(2E,6Z)-farnesyl diphosphate
patchoulol + diphosphate
-
-
-
?
(2Z,6E)-farnesyl diphosphate
patchoulol + diphosphate
-
-
-
?
Geranyl diphosphate
?
-
-
-
?
neryl diphosphate
?
-
-
-
?
(2E,6E)-farnesyl diphosphate
(-)-patchoulol + diphosphate
-
-
-
-
?
(2E,6E)-farnesyl diphosphate + H2O
patchoulol + diphosphate
additional information
?
-
(2E,6E)-farnesyl diphosphate
patchoulol + diphosphate
-
-
-
?
(2E,6E)-farnesyl diphosphate
patchoulol + diphosphate
-
-
-
-
?
(2E,6E)-farnesyl diphosphate
patchoulol + diphosphate
-
-
-
?
(2E,6E)-farnesyl diphosphate + H2O
patchoulol + diphosphate
-
plus at least 13 additional sesquiterpene products
-
?
(2E,6E)-farnesyl diphosphate + H2O
patchoulol + diphosphate
-
main product of recombinant enzyme is germacrene A, additional formation of + alpha-bulnesene
-
?
(2E,6E)-farnesyl diphosphate + H2O
patchoulol + diphosphate
-
-
further products are cyclic olefins alpha- and beta-patchoulene, alpha-bulnesene, and alpha-guiaene
-
?
(2E,6E)-farnesyl diphosphate + H2O
patchoulol + diphosphate
-
hydride shift mechanism, no indication that germacrene and bulnesene are intermediates
-
-
?
(2E,6E)-farnesyl diphosphate + H2O
patchoulol + diphosphate
-
reaction proceeds via an exocyclic [7,10:1,5]patchoul-4(12)-ene intermediate. Occurrence of a 1,3-hydride shift across the 5-membered ring
-
-
?
additional information
?
-
no activity with geranylgeranyl diphosphate
-
-
?
additional information
?
-
-
no activity with geranylgeranyl diphosphate
-
-
?
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additional information
fusion to thioredoxin and careful codon optimization of the eukaryotic sequence improves solubl expression on average by 42% in comparison to an unoptimized, His-tagged construct
additional information
-
fusion to thioredoxin and careful codon optimization of the eukaryotic sequence improves solubl expression on average by 42% in comparison to an unoptimized, His-tagged construct
additional information
-
use of a bifunctional enzymatic chimera composed as a fusion between farnesyl diphosphate synthase from yeast and patchoulol synthase from patchouli improves patchoulol production compared to that with the use of free enzymes up to 2fold. The effect is additive to improvements obtained by traditional metabolic engineering
additional information
use of a bifunctional enzymatic chimera composed as a fusion between farnesyl diphosphate synthase from yeast and patchoulol synthase from patchouli improves patchoulol production compared to that with the use of free enzymes up to 2fold. The effect is additive to improvements obtained by traditional metabolic engineering
additional information
-
construction of several fusion protein variants in which farnesyl diphosphate synthase of yeast has been coupled to patchoulol synthase of plant origin. patchoulol synthase can be extended N- and C-terminally with farnesyl diphosphate synthase and retain activity in vivo. Expression of the fusion proteins in Saccharomyces cerevisiae increases the production of patchoulol up to 2-fold
additional information
construction of several fusion protein variants in which farnesyl diphosphate synthase of yeast has been coupled to patchoulol synthase of plant origin. patchoulol synthase can be extended N- and C-terminally with farnesyl diphosphate synthase and retain activity in vivo. Expression of the fusion proteins in Saccharomyces cerevisiae increases the production of patchoulol up to 2-fold
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97
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Characterisation of a recombinant patchoulol synthase variant for biocatalytic production of terpenes
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176
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Patchoulol production with metabolically engineered Corynebacterium glutamicum
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9
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8
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Pogostemon cablin
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brenda