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Information on EC 4.2.3.70 - patchoulol synthase
for references in articles please use BRENDA:EC4.2.3.70
Word Map on EC 4.2.3.70
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The expected taxonomic range for this enzyme is: Pogostemon cablin
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EC NUMBER 
COMMENTARY 
4.2.3.70
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RECOMMENDED NAME
GeneOntology No.
patchoulol synthase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
(2E,6E)-farnesyl diphosphate + H2O = patchoulol + diphosphate
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-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
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SYSTEMATIC NAME
IUBMB Comments
(2E,6E)-farnesyl-diphosphate diphosphate-lyase (patchoulol-forming)
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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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 + 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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?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
additional information
Mg2+
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required, KM-value 1.7 mM, other divalent metal ions are ineffective
additional information
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other divalent metal ions than Mg2+ are ineffective
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0068
(2E,6E)-farnesyl diphosphate
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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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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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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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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
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
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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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
synthesis
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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LINKS TO OTHER DATABASES (specific for EC-Number 4.2.3.70)
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