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Information on EC 4.2.3.70 - patchoulol synthase
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4.2.3.70 patchoulol synthaseSpecify your search results
Word Map
- 4.2.3.70
-
sesquiterpene
-
pogostemon
- cablin
- patchouli
- pt
-
terpene
-
terpenoids
- sesquiterpenoids
- synthases
-
cosmetic
-
perfume
-
perennial
-
biocatalytic
- synthesis
- ergosterol
- squamosa
-
high-value
-
phototrophic
-
protein-like
-
age-regulated
-
elder
- patens
-
moss
- physcomitrella
-
microrna156
- valencene
- germacrene
-
fragrant
The enzyme appears in viruses and cellular organisms
Synonyms
PTS, TPS, TPS177, 
more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
PTS
TPS177
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
(2E,6E)-farnesyl diphosphate + H2O = patchoulol + diphosphate
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
MetaCyc
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SYSTEMATIC NAME
IUBMB Comments
(2E,6E)-farnesyl-diphosphate diphosphate-lyase (patchoulol-forming)
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(2E,6E)-farnesyl diphosphate
patchoulol + diphosphate
-
-
-
?
(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
-
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
-
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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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(2E,6E)-farnesyl diphosphate
patchoulol + diphosphate
-
-
-
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
additional information
Mg2+
-
required, KM-value 1.7 mM, other divalent metal ions are ineffective
additional information
-
other divalent metal ions than Mg2+ are ineffective
additional information
no activity with Ca2+, Ba2+, Mn2+, Ni2+, Co2+and Cu2+
additional information
-
no activity with Ca2+, Ba2+, Mn2+, Ni2+, Co2+and Cu2+
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0068
(2E,6E)-farnesyl diphosphate
-
pH 6.5, temperature not specified in the publication
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). TPSPS_POGCB
552
0
64199
Swiss-Prot
other Location (Reliability: 5)
A0A7L5BCD4_ORYSA
542
0
63039
TrEMBL
other Location (Reliability: 4)
W8NXF3_POGCB
552
0
64111
TrEMBL
other Location (Reliability: 5)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
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
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
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
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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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
maximum stability in the presence of Mg2+ above 10 mM and 10% (v/v) glycerol
-
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed as fusion protein with farnesyl diphosphate synthase in Saccharomyces cerevisiae
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
the expression level of the enzyme is rising drastically with plant aging (5fold increased expression after 10 month of aging)
-
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
synthesis
synthesis
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
synthesis
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
synthesis
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
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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 (Q49SP3), Pogostemon cablin
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 (Q49SP3), Pogostemon cablin
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 (Q49SP3), Pogostemon cablin
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 (Q49SP3), Pogostemon cablin
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 (Q49SP3), Pogostemon cablin
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 (Q49SP3), Pogostemon cablin
brenda
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