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Information on EC 4.2.3.70 - patchoulol synthase and Organism(s) Pogostemon cablin and UniProt Accession Q49SP3

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EC Tree
     4 Lyases
         4.2 Carbon-oxygen lyases
             4.2.3 Acting on phosphates
                4.2.3.70 patchoulol synthase
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Select one or more organisms in this record: ?
This record set is specific for:
Pogostemon cablin
UNIPROT: Q49SP3 not found.
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The taxonomic range for the selected organisms is: Pogostemon cablin
The enzyme appears in selected viruses and cellular organisms
Synonyms
patchoulol synthase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
PATHWAY SOURCE
PATHWAYS
-
-
SYSTEMATIC NAME
IUBMB Comments
(2E,6E)-farnesyl-diphosphate diphosphate-lyase (patchoulol-forming)
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(2E,6E)-farnesyl diphosphate
patchoulol + diphosphate
show the reaction diagram
(2E,6E)-farnesyl diphosphate + H2O
patchoulol + diphosphate
show the reaction diagram
(2E,6Z)-farnesyl diphosphate
patchoulol + diphosphate
show the reaction diagram
-
-
-
?
(2Z,6E)-farnesyl diphosphate
patchoulol + diphosphate
show the reaction diagram
-
-
-
?
Geranyl diphosphate
?
show the reaction diagram
-
-
-
?
neryl diphosphate
?
show the reaction diagram
-
-
-
?
(2E,6E)-farnesyl diphosphate
(-)-patchoulol + diphosphate
show the reaction diagram
-
-
-
-
?
(2E,6E)-farnesyl diphosphate + H2O
patchoulol + diphosphate
show the reaction diagram
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
(2E,6E)-farnesyl diphosphate
patchoulol + diphosphate
show the reaction diagram
(2E,6Z)-farnesyl diphosphate
patchoulol + diphosphate
show the reaction diagram
-
-
-
?
(2Z,6E)-farnesyl diphosphate
patchoulol + diphosphate
show the reaction diagram
-
-
-
?
(2E,6E)-farnesyl diphosphate
(-)-patchoulol + diphosphate
show the reaction diagram
-
-
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mn2+
may substitute for Mn2+ at 0.1 mM, inhibitory above
Mg2+
-
required, KM-value 1.7 mM, other divalent metal ions are ineffective
additional information
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Mn2+
may substitute for Mn2+ at 0.1 mM, inhibitory above
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00445
(2E,6E)-farnesyl diphosphate
pH 7.0, 30°C
0.008
(2Z,6E)-farnesyl diphosphate
at pH 7.3 and 38°C
0.0068
(2E,6E)-farnesyl diphosphate
-
pH 6.5, temperature not specified in the publication
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00043
(2E,6E)-farnesyl diphosphate
pH 7.0, 30°C
0.072
(2Z,6E)-farnesyl diphosphate
at pH 7.3 and 38°C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
9
(2Z,6E)-farnesyl diphosphate
at pH 7.3 and 38°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
180
-
pH 6.5, temperature not specified in the publication
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7
dramatical reduction in activity below
8
75% of maximum activity
5.7
-
half-maximal activity
7.7
-
half-maximal activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
20
30% of maximum activity
30
less than 60% of maximum activity
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5
-
isoelectric focusing
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
TPSPS_POGCB
552
0
64199
Swiss-Prot
other Location (Reliability: 5)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
55000
x * 55000, SDS-PAGE
40000
-
2 * 40000, SDS-PAGE
80000
-
gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 55000, SDS-PAGE
dimer
-
2 * 40000, SDS-PAGE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
maximum stability in the presence of Mg2+ above 10 mM and 10% (v/v) glycerol
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
HisTrap column chromatography
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed as fusion protein with farnesyl diphosphate synthase in Saccharomyces cerevisiae
expressed in Chlamydomonas reinhardtii strain UVM4
expressed in Corynebacterium glutamicum strain ATCC 13032
expressed in Escherichia coli BL21(DE3) cells
expression in Eschrichia coli
expression in Saccharomyces cerevisiae
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
the expression level of the enzyme is rising drastically with plant aging (5fold increased expression after 10 month of aging)
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
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
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
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team