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EC Tree
The expected taxonomic range for this enzyme is: Pogostemon cablin
Synonyms
PTS, TPS, TPS177,
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PTS
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TPS177
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-
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(2E,6E)-farnesyl diphosphate + H2O = patchoulol + diphosphate
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-
-
-
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(2E,6E)-farnesyl-diphosphate diphosphate-lyase (patchoulol-forming)
-
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(2E,6E)-farnesyl diphosphate
(-)-patchoulol + diphosphate
-
-
-
-
?
(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
?
-
-
-
?
additional information
?
-
no activity with geranylgeranyl diphosphate
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-
-
(2E,6E)-farnesyl diphosphate + H2O
patchoulol + diphosphate
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-
further products are cyclic olefins alpha- and beta-patchoulene, alpha-bulnesene, and alpha-guiaene
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?
(2E,6E)-farnesyl diphosphate + H2O
patchoulol + diphosphate
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plus at least 13 additional sesquiterpene products
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?
(2E,6E)-farnesyl diphosphate + H2O
patchoulol + diphosphate
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-
main product of recombinant enzyme is germacrene A, additional formation of + alpha-bulnesene
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?
(2E,6E)-farnesyl diphosphate + H2O
patchoulol + diphosphate
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hydride shift mechanism, no indication that germacrene and bulnesene are intermediates
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-
?
(2E,6E)-farnesyl diphosphate + H2O
patchoulol + diphosphate
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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
-
-
?
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(2E,6E)-farnesyl diphosphate
(-)-patchoulol + diphosphate
-
-
-
-
?
(2E,6E)-farnesyl diphosphate
patchoulol + diphosphate
-
-
-
-
?
(2E,6Z)-farnesyl diphosphate
patchoulol + diphosphate
-
-
-
?
(2Z,6E)-farnesyl diphosphate
patchoulol + diphosphate
-
-
-
?
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Mn2+
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may substitute for Mn2+ at 0.1 mM, inhibitory above
Mg2+
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preferred, maximum activity at 1 mM
Mg2+
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required, KM-value 1.7 mM, other divalent metal ions are ineffective
Mg2+
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absolutely required
additional information
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divalent cation required
additional information
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other divalent metal ions than Mg2+ are ineffective
additional information
no activity with Ca2+, Ba2+, Mn2+, Ni2+, Co2+and Cu2+
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Mn2+
-
may substitute for Mn2+ at 0.1 mM, inhibitory above
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0.00445 - 0.0068
(2E,6E)-farnesyl diphosphate
0.008
(2Z,6E)-farnesyl diphosphate
at pH 7.3 and 38°C
0.00445
(2E,6E)-farnesyl diphosphate
-
pH 7.0, 30°C
0.0068
(2E,6E)-farnesyl diphosphate
-
pH 6.5, temperature not specified in the publication
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0.00043
(2E,6E)-farnesyl diphosphate
-
pH 7.0, 30°C
0.072
(2Z,6E)-farnesyl diphosphate
at pH 7.3 and 38°C
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9
(2Z,6E)-farnesyl diphosphate
at pH 7.3 and 38°C
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180
-
pH 6.5, temperature not specified in the publication
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5.7
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half-maximal activity
7
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dramatical reduction in activity below
7.7
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half-maximal activity
8
-
75% of maximum activity
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20
-
30% of maximum activity
30
-
less than 60% of maximum activity
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UniProt
brenda
-
-
-
brenda
Indian Patchouli
UniProt
brenda
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-
-
brenda
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-
brenda
-
-
-
brenda
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TPSPS_POGCB
552
0
64199
Swiss-Prot
W8NXF3_POGCB
552
0
64111
TrEMBL
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40000
-
2 * 40000, SDS-PAGE
55000
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x * 55000, SDS-PAGE
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dimer
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2 * 40000, SDS-PAGE
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additional information
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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; 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
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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
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unstable in crude extracts, losing 80% activity in 6 h at room temperature and 40% activity in 24 h at 0-4°C. Addition of dithiothreitol is essential, and Na2HPO4 markedly stabilizes
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maximum stability in the presence of Mg2+ above 10 mM and 10% (v/v) glycerol
-
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HisTrap column chromatography
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expressed as fusion protein with farnesyl diphosphate synthase in Saccharomyces cerevisiae
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expressed in Chlamydomonas reinhardtii strain UVM4
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expressed in Corynebacterium glutamicum strain ATCC 13032
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expressed in Escherichia coli BL21(DE3) cells
expression in Eschrichia coli
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expression in Saccharomyces cerevisiae
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the expression level of the enzyme is rising drastically with plant aging (5fold increased expression after 10 month of aging)
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synthesis
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construction of several fusion protein variants in which farnesyl diphosphate synthase of yeast has been coupled to patchoulol synthase of plant origin. Expression of the fusion proteins in Saccharomyces cerevisiae increases the production of patchoulol up to 2-fold. The fusion strategy can be used in combination with traditional metabolic engineering to further increase the production of patchoulol; 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
synthesis
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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
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Deguerry, F.; Pastore, L.; Wu, S.; Clark, A.; Chappell, J.; Schalk, M.
The diverse sesquiterpene profile of patchouli, Pogostemon cablin, is correlated with a limited number of sesquiterpene synthases
Arch. Biochem. Biophys.
454
123-136
2006
Pogostemon cablin, Pogostemon cablin (Q49SP3)
brenda
Albertsen, L.; Chen, Y.; Bach, L.S.; Rattleff, S.; Maury, J.; Brix, S.; Nielsen, J.; Mortensen, U.H.
Diversion of flux toward sesquiterpene production in Saccharomyces cerevisiae by fusion of host and heterologous enzymes
Appl. Environ. Microbiol.
77
1033-1040
2011
Pogostemon cablin, Pogostemon cablin (Q49SP3)
brenda
Croteau, R.; Munck, S.L.; Akoh, C.C.; Fisk, H.J.; Satterwhite, D.M.
Biosynthesis of the sesquiterpene patchoulol from farnesyl pyrophosphate in leaf extracts of Pogostemon cablin (patchouli): mechanistic considerations
Arch. Biochem. Biophys.
256
56-68
1987
Pogostemon cablin
brenda
Munck, S.L.; Croteau, R.
Purification and characterization of the sesquiterpene cyclase patchoulol synthase from Pogostemon cablin
Arch. Biochem. Biophys.
282
58-64
1990
Pogostemon cablin
brenda
Faraldos, J.A.; Wu, S.; Chappell, J.; Coates, R.M.
Doubly deuterium-labeled patchouli alcohol from cyclization of singly labeled [2-(2)H(1)]farnesyl diphosphate catalyzed by recombinant patchoulol synthase
J. Am. Chem. Soc.
132
2998-3008
2010
Pogostemon cablin
brenda
Hartwig, S.; Frister, T.; Alemdar, S.; Li, Z.; Krings, U.; Berger, R.G.; Scheper, T.; Beutel, S.
Expression, purification and activity assay of a patchoulol synthase cDNA variant fused to thioredoxin in Escherichia coli
Protein Expr. Purif.
97
61-71
2014
Pogostemon cablin, Pogostemon cablin (Q49SP3)
brenda
Frister, T.; Hartwig, S.; Alemdar, S.; Schnatz, K.; Thoens, L.; Scheper, T.; Beutel, S.
Characterisation of a recombinant patchoulol synthase variant for biocatalytic production of terpenes
Appl. Biochem. Biotechnol.
176
2185-2201
2015
Pogostemon cablin, Pogostemon cablin (Q49SP3)
brenda
Henke, N.A.; Wichmann, J.; Baier, T.; Frohwitter, J.; Lauersen, K.J.; Risse, J.M.; Peters-Wendisch, P.; Kruse, O.; Wendisch, V.F.
Patchoulol production with metabolically engineered Corynebacterium glutamicum
Genes (Basel)
9
219
2018
Pogostemon cablin, Pogostemon cablin (Q49SP3)
brenda
Lauersen, K.J.; Baier, T.; Wichmann, J.; Woerdenweber, R.; Mussgnug, J.H.; Huebner, W.; Huser, T.; Kruse, O.
Efficient phototrophic production of a high-value sesquiterpenoid from the eukaryotic microalga Chlamydomonas reinhardtii
Metab. Eng.
38
331-343
2016
Pogostemon cablin, Pogostemon cablin (Q49SP3)
brenda
Yu, Z.X.; Wang, L.J.; Zhao, B.; Shan, C.M.; Zhang, Y.H.; Chen, D.F.; Chen, X.Y.
Progressive regulation of sesquiterpene biosynthesis in Arabidopsis and Patchouli (Pogostemon cablin) by the miR156-targeted SPL transcription factors
Mol. Plant
8
98-110
2015
Pogostemon cablin
brenda
Gruchattka, E.; Kayser, O.
In vivo validation of in silico predicted metabolic engineering strategies in yeast Disruption of alpha-ketoglutarate dehydrogenase and expression of ATP-citrate lyase for terpenoid production
PLoS ONE
10
e0144981
2015
Pogostemon cablin, Pogostemon cablin (Q49SP3)
brenda
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4.2.3.70 patchoulol synthase
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