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Information on EC 3.1.7.11 - geranyl diphosphate diphosphatase
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EC Tree
3.1.7.11 geranyl diphosphate diphosphataseIUBMB Comments
Isolated from Ocimum basilicum (basil) and Cinnamomum tenuipile (camphor tree). Requires Mg2+ or Mn2+. Geraniol is labelled when formed in the presence of [18O]H2O. Thus mechanism involves a geranyl cation . Neryl diphosphate is hydrolysed more slowly. May be the same as EC 3.1.7.3 monoterpenyl-diphosphatase.
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Word Map
- 3.1.7.11
- synthases
-
sesquiterpene
-
terpenoids
- gpp
- myrcene
-
fragrance
- sabinene
- basilicum
-
scent
-
ocimum
- 1,8-cineole
- pinene
-
oleoresin
- nerol
-
e-beta-ocimene
- beta-pinene
- alpha-pinene
- cineole
-
bornyl
- synthesis
- camphene
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Synonyms
monoterpene synthase, geraniol synthase, ctges, geranyl pyrophosphate pyrophosphatase, 
more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
CtGES
-
-
-
-
geraniol synthase
geranyl pyrophosphate pyrophosphatase
-
-
-
-
GES
geraniol synthase
-
-
-
-
GES
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
geranyl diphosphate + H2O = geraniol + diphosphate
-
-
-
-
geranyl diphosphate + H2O = geraniol + diphosphate
the reaction mechanism of GES is similar to that of other monoterpene synthases and is different from the action of phosphatases
-
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PATHWAY SOURCE
PATHWAYS
BRENDA
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SYSTEMATIC NAME
IUBMB Comments
geranyl-diphosphate diphosphohydrolase
Isolated from Ocimum basilicum (basil) and Cinnamomum tenuipile (camphor tree). Requires Mg2+ or Mn2+. Geraniol is labelled when formed in the presence of [18O]H2O. Thus mechanism involves a geranyl cation [1]. Neryl diphosphate is hydrolysed more slowly. May be the same as EC 3.1.7.3 monoterpenyl-diphosphatase.
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CAS REGISTRY NUMBER
COMMENTARY
139691-86-4
-
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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
additional information
?
-
no substrate: farnesyl diphosphate. Enzyme does no display phosphatase activity
-
-
?
geranyl diphosphate + H2O
geraniol + diphosphate
the monoterpene synthase specifically converts geranyl diphosphate to geraniol, GC-MS analysis
-
-
?
geranyl diphosphate + H2O
geraniol + diphosphate
-
-
-
?
geranyl diphosphate + H2O
geraniol + diphosphate
-
-
-
?
geranyl diphosphate + H2O
geraniol + diphosphate
-
-
-
?
geranyl diphosphate + H2O
geraniol + diphosphate
-
-
-
?
geranyl diphosphate + H2O
geraniol + 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
geranyl diphosphate + H2O
geraniol + diphosphate
-
-
-
?
geranyl diphosphate + H2O
geraniol + diphosphate
-
-
-
?
geranyl diphosphate + H2O
geraniol + diphosphate
-
-
-
?
geranyl diphosphate + H2O
geraniol + diphosphate
-
-
-
?
geranyl diphosphate + H2O
geraniol + diphosphate
-
-
-
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
Mn2+
additional information
Mg2+
both Mn2+ and Mg2+ are required, optimum concentrations are 1 mM Mg2+ and 0.1 mM Mn2+
Mn2+
both Mn2+ and Mg2+ are required, optimum concentrations are 1 mM Mg2+ and 0.1 mM Mn2+
Mn2+
-
required as a divalent metal cofactor for activity, activating at 0.1-1.0 mM, inhihitory above. Km value of the wild-type enzyme is 0.051 mM at pH 8.5 and 37°C
additional information
-
Mg2+ has no effect on the enzyme activity an cannot substitute for Mn2+
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
not inhibitory: sodium tungstate at 2 mM and sodium fluoride at 1 mM
-
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Hypersensitivity
Overexpression of geraniol synthase induces heat stress susceptibility in Nicotiana tabacum.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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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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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
localization of transcripts in the internal phloem associated parenchyma
brenda
CtGES mRNA is localized in the oil cells of the leaves
brenda
-
highest expression level, about 40fold higher than that found in the roots, leaves, flowers, and fruit pericarp
brenda
expression consistently increases throughout fruit ripening
brenda
CtGES mRNA is localized in the oil cells of the leaves
brenda
-
younger leaves, which have a higher density of epidermis, also have a higher content of monoterpenes than older leaves
brenda
in essential oil within oil cells, the strains vary in the oil composition
brenda
in essential oil within oil cells, the strains vary in the oil composition
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
physiological function
expression of Ocimum basilicum geranyl diposphate synthase in Vitis vinifera, Arabidopsis thaliana, and Nicotiana benthamiana leads to synthesis of geraniol as the main product detected in the leaves, with different minor products citronellol and nerol in Vitis vinifera, linalool and nerol in Nicotiana benthamiana. Engineered Saccharomyces cerevisiae strain A9D expressing Ocimum basilicum geranyl diposphate produces significant quantities of monoterpenes, including 90% geraniol, 5% linalool, 5% citronellol and traces of nerol
physiological function
transgenic expression in Saccharomyces cerevisiae mutated in the farnesyl diphosphate synthase gene leads to secretion of geraniol into the growth medium
physiological function
both transient and stable overexpression of geranyl(geranyl) diphosphate synthase G(G)PPS and coexpression of G(G)PPS plus geraniol synthase GES significantly enhances the accumulation of secologanin, which in turn elevates the levels of monomeric monoterpene indole alkaloids. Transgenic plants exhibit increased levels of root alkaloid ajmalicine. The dimeric alkaloid vinblastine is enhanced only in G(G)PPS but not in G(G)PPS plus GES transgenic lines
physiological function
feeding of leaves with geraniol, but not tryptophan (precursor fortryptamine), increases the accumulation of the monoterpene indole alkaloids catharanthine and vindoline. Gene silencing significantly reduces the monoterpene indole alkaloid content. Overexpression of GES in leaves increased monoterpene indole alkaloids content. GES exhibits correlation with monoterpene indole alkaloids levels in leaves of different Cataranthus roseus cultivars and has significantly lower expression relative to other pathway genes
physiological function
overexpression of GES in Nicotiana tabacum. Growth, morphology and photosynthetic efficiency of GES plants are not significantly different from those of control plants. GES plants' direct defenses against herbivores or pathogens are similar to those of control plants, their indirect defense (i.e. attracting herbivore enemy Nesidiocoris tenuis) is stronger compared to that of control plants. GES transgenic plants are susceptible to cold stress and even more susceptible to extreme heat stress (50°C). GES plants show decreased transcription levels of the WRKY33 transcription factor gene and aquaporin gene PIP2
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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). TPS4_CANOD
586
0
67366
Swiss-Prot
Mitochondrion (Reliability: 3)
BCGS_ORIVU
555
0
64443
Swiss-Prot
other Location (Reliability: 2)
GERS_CINTE
603
0
69081
Swiss-Prot
Chloroplast (Reliability: 3)
GERS_OCIBA
567
0
64933
Swiss-Prot
Mitochondrion (Reliability: 4)
GRNL6_PERFR
603
0
69982
Swiss-Prot
Chloroplast (Reliability: 1)
GRNL7_PERFR
603
0
69805
Swiss-Prot
Chloroplast (Reliability: 2)
GRNLC_PERFH
603
0
70035
Swiss-Prot
Chloroplast (Reliability: 1)
GRNLG_PERFH
603
0
69948
Swiss-Prot
Chloroplast (Reliability: 2)
TPS_MATON
Matsumurasca onukii
303
0
34983
Swiss-Prot
other Location (Reliability: 1)
ATERP_PINBN
626
0
71948
Swiss-Prot
Chloroplast (Reliability: 5)
A0A5B7BIG7_DAVIN
107
0
11820
TrEMBL
other Location (Reliability: 3)
A0A7H9SVV5_DENOF
582
0
68067
TrEMBL
other Location (Reliability: 5)
A0A6C0QEC7_TAICR
607
0
70014
TrEMBL
Chloroplast (Reliability: 3)
A0A7D3V5B7_NEPRA
577
0
66114
TrEMBL
Chloroplast (Reliability: 1)
A0RZI3_MEDTR
567
0
64906
TrEMBL
Mitochondrion (Reliability: 4)
A0A109P1X1_CAMAC
594
0
67726
TrEMBL
Chloroplast (Reliability: 1)
A0A7D3UMC9_NEPCA
577
0
66060
TrEMBL
Chloroplast (Reliability: 1)
A0A2G9GHR4_9LAMI
575
0
66145
TrEMBL
Chloroplast (Reliability: 1)
A0A2G9GUH6_9LAMI
575
0
66154
TrEMBL
Chloroplast (Reliability: 1)
A0A396JEA7_MEDTR
481
0
55157
TrEMBL
other Location (Reliability: 3)
A0A7D3UI70_NEPCA
578
0
66505
TrEMBL
Chloroplast (Reliability: 2)
A0A2G9HTG4_9LAMI
220
0
25105
TrEMBL
other Location (Reliability: 4)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
57700
-
2 * 57700, native enzyme, SDS-PAGE, 2 * 58600, recombinant enzyme, SDS-PAGE
58600
-
2 * 57700, native enzyme, SDS-PAGE, 2 * 58600, recombinant enzyme, SDS-PAGE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
homodimer
-
2 * 57700, native enzyme, SDS-PAGE, 2 * 58600, recombinant enzyme, SDS-PAGE
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
N-terminal truncation at residues S14, L28, S43and S52 all lead to an increase on geraniol production
additional information
-
a truncated mutant which lacks the first 53 amino acids, shows improved production of geraniol
additional information
-
construction of Ser35 and Met44 truncated GES proteins showing reduced activity compared to the wild-type enzyme
additional information
construction of domain swapping mutants between geraniol synthase from Perilla citriodora and linalool synthase from Perilla hirtella. Domains IV-1 and -4 are important for geraniol synthesis, and domains III-b, III-d, and IV-4 for linalool synthesis. The conformation of carbocation intermediates and their electron localization seem different between geraniol and linalool synthases. Five amino acids in domain IV-4 are indispensable for the formation of geraniol and linalool. These residues seem to be responsible for the different spatial arrangement of the amino acid at H524 in the case of geraniol synthase, while N526 is the corresponding residue in linalool synthase
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
45
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
native enzyme 38.3fold from leaves by two differewnt steps of anion exchange chromatography, and by gel filtration
-
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
DNA and amino acid sequence determination and analysis using a GES cDNA, isolated based on analysis of a glandular trichome expressed sequence tag database, sequence comparison, phylogenetic tree, functional expression in Escherichia coli
-
DNA and amino acid sequence determination and analysis, phylogenetic tree, expression of His-tagged enzyme in Escherichia coli strain BL21 (DE3)
DNA and amino acid sequence determination and analysis, sequence comparison, phylogenetic tree
DNA and amino acid sequence determination and analysis, sequence comparisons
DNA and amino acid sequence determination and analysis, sequence comparisons, phylogenetic tree
expression in Escherichia coli
DNA and amino acid sequence determination and analysis, sequence comparison, phylogenetic tree
DNA and amino acid sequence determination and analysis, sequence comparison, phylogenetic tree
DNA and amino acid sequence determination and analysis, sequence comparisons
DNA and amino acid sequence determination and analysis, sequence comparisons
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
expression is induced by methyl jasmonate
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
synthesis
synthesis
coexpression of geranyl diphosphate synthase and geraniol synthase in Escherichia coli. Gene copy number optimization leads to a 1.6fold increase of geraniol production when four copies of geranyl diphosphate synthase and one copy of geraniol synthase are used. The additional fermentation conditions optimization, including removal of organic layers and addition of n-decane, leads to a geraniol production of 74.6 mg/l
synthesis
-
overexpression of a mutant GES with a 5'-untranslated sequence designed for high translational efficiency, along with the additional expression of isopentenyl diphosphate isomerase, and geranyl diphosphate synthase, yields 300 mg/l/12 h geraniol and its derivatives in a shaking flask
synthesis
significant increase in geraniol synthesis is achieved by coexpression of geraniol synthase, mutant S80F of farnesyl diphosphate synthase, and the encoding genes involved in the whole mevalonic acid biosynthetic pathway in Escherichia coli. The additional optimization of medium composition, fermentation time, and addition of metal ions leads to the geraniol production of 48.5 mg/l
synthesis
synthesis of geraniol by expression of GES truncated at residue S43 in Saccharomyces cerevisiae. Coexpression of the reverse fusion of farnesyl diphosphate synthase Erg20 mutant F96W-N127W and truncated GES and another copy of farnesyl diphosphate synthase Erg20 mutant F96W-N127W promotes the geraniol titer to 523.96 mg/l at shakes flask level. A highest reported titer of 1.68 g/l geraniol in eukaryote cells is achieved in 2.0 l fed-batch fermentation under carbon restriction strategy
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Masumoto, N.; Korin, M.; Ito, M.
Geraniol and linalool synthases from wild species of perilla
Phytochemistry
71
1068-1075
2010
Perilla frutescens var. hirtella (C0KWV4), Perilla frutescens var. hirtella (C0KWV6), Perilla frutescens var. hirtella (Q4JHG3), Perilla frutescens (Q308N0), Perilla frutescens 79 (Q308N0), Perilla frutescens var. hirtella 5031 (C0KWV4), Perilla frutescens var. hirtella 5073 (C0KWV6), Perilla frutescens var. hirtella 87 (Q4JHG3)
brenda
Yang, T.; Li, J.; Wang, H.X.; Zeng, Y.
A geraniol-synthase gene from Cinnamomum tenuipilum
Phytochemistry
66
285-293
2005
Cinnamomum tenuipile (Q8GUE4), Cinnamomum tenuipile
brenda
Ito, M.; Honda, G.
Geraniol synthases from perilla and their taxonomical significance
Phytochemistry
68
446-453
2007
Perilla frutescens (Q308N0), Perilla frutescens var. hirtella (Q4JHG3)
brenda
Iijima, Y.; Gang, D.R.; Fridman, E.; Lewinsohn, E.; Pichersky, E.
Characterization of geraniol synthase from the peltate glands of sweet basil
Plant Physiol.
134
370-379
2004
Ocimum basilicum
brenda
Fischer, M.J.; Meyer, S.; Claudel, P.; Perrin, M.; Ginglinger, J.F.; Gertz, C.; Masson, J.E.; Werck-Reinhardt, D.; Hugueney, P.; Karst, F.
Specificity of Ocimum basilicum geraniol synthase modified by its expression in different heterologous systems
J. Biotechnol.
163
24-29
2013
Ocimum basilicum (Q6USK1), Ocimum basilicum
brenda
Shishido, H.; Miyamoto, Y.; Ozawa, R.; Taniguchi, S.; Takabayashi, J.; Akimitsu, K.; Gomi, K.
Geraniol synthase whose mRNA is induced by host-selective ACT-toxin in the ACT-toxin-insensitive rough lemon (Citrus jambhiri)
J. Plant Physiol.
169
1401-1407
2012
Citrus jambhiri (I7GSK7), Citrus jambhiri
brenda
Vezzaro, A.; Krause, S.T.; Nonis, A.; Ramina, A.; Degenhardt, J.; Ruperti, B.
Isolation and characterization of terpene synthases potentially involved in flavor development of ripening olive (Olea europaea) fruits
J. Plant Physiol.
169
908-914
2012
Olea europaea (I1VSB0)
brenda
Sato-Masumoto, N.; Ito, M.
A domain swapping approach to elucidate differential regiospecific hydroxylation by geraniol and linalool synthases from perilla
Phytochemistry
102
46-54
2014
Perilla frutescens var. hirtella (Q4JHG3)
brenda
Simkin, A.J.; Miettinen, K.; Claudel, P.; Burlat, V.; Guirimand, G.; Courdavault, V.; Papon, N.; Meyer, S.; Godet, S.; St-Pierre, B.; Giglioli-Guivarch, N.; Fischer, M.J.; Memelink, J.; Clastre, M.
Characterization of the plastidial geraniol synthase from Madagascar periwinkle which initiates the monoterpenoid branch of the alkaloid pathway in internal phloem associated parenchyma
Phytochemistry
85
36-43
2013
Catharanthus roseus (J9PZR5), Catharanthus roseus
brenda
Kumar, S.; Shilpashree, H.; Nagegowda, D.
Terpene moiety enhancement by overexpression of geranyl(geranyl) diphosphate synthase and geraniol synthase elevates monomeric and dimeric monoterpene indole alkaloids in transgenic Catharanthus roseus
Front. Plant Sci.
9
942
2018
Catharanthus roseus (J9PZR5), Catharanthus roseus
brenda
Ye, P.; Liang, S.; Wang, X.; Duan, L.; Jiang-Yan, F.; Yang, J.; Zhan, R.; Ma, D.
Transcriptome analysis and targeted metabolic profiling for pathway elucidation and identification of a geraniol synthase involved in iridoid biosynthesis from Gardenia jasminoides
Ind. Crops Prod.
132
48-58
2019
Gardenia jasminoides
-
brenda
Yahyaa, M.; Ibdah, M.; Marzouk, S.; Ibdah, M.
Profiling of the terpene metabolome in carrot fruits of wild (Daucus carota L. ssp. carota) accessions and characterization of a geraniol synthase
J. Agric. Food Chem.
66
2378-2386
2018
Daucus carota subsp. carota
brenda
Tashiro, M.; Fujii, A.; Kawai-Noma, S.; Saito, K.; Umeno, D.
Directed evolution and expression tuning of geraniol synthase for efficient geraniol production in Escherichia coli
J. Gen. Appl. Microbiol.
63
287-295
2017
Escherichia coli
brenda
Chen, F.; Li, W.; Jiang, L.; Pu, X.; Yang, Y.; Zhang, G.; Luo, Y.
Functional characterization of a geraniol synthase-encoding gene from Camptotheca acuminata and its application in production of geraniol in Escherichia coli
J. Ind. Microbiol. Biotechnol.
43
1281-1292
2016
Camptotheca acuminata (A0A109P1X1), Camptotheca acuminata
brenda
Yang, L.; Jiang, L.; Li, W.; Yang, Y.; Zhang, G.; Luo, Y.
A homomeric geranyl diphosphate synthase-encoding gene from Camptotheca acuminata and its combinatorial optimization for production of geraniol in Escherichia coli
J. Ind. Microbiol. Biotechnol.
44
1431-1441
2017
Camptotheca acuminata (A0A109P1X1)
brenda
Jiang, G.Z.; Yao, M.D.; Wang, Y.; Zhou, L.; Song, T.Q.; Liu, H.; Xiao, W.H.; Yuan, Y.J.
Manipulation of GES and ERG20 for geraniol overproduction in Saccharomyces cerevisiae
Metab. Eng.
41
57-66
2017
Catharanthus roseus (J9PZR5)
brenda
Kumar, K.; Kumar, S.R.; Dwivedi, V.; Rai, A.; Shukla, A.K.; Shanker, K.; Nagegowda, D.A.
Precursor feeding studies and molecular characterization of geraniol synthase establish the limiting role of geraniol in monoterpene indole alkaloid biosynthesis in Catharanthus roseus leaves
Plant Sci.
239
56-66
2015
Catharanthus roseus (J9PZR5), Catharanthus roseus
brenda
Hamachi, A.; Nisihara, M.; Saito, S.; Rim, H.; Takahashi, H.; Islam, M.; Uemura, T.; Ohnishi, T.; Ozawa, R.; Maffei, M.E.; Arimura, G.I.
Overexpression of geraniol synthase induces heat stress susceptibility in Nicotiana tabacum
Planta
249
235-249
2019
Ocimum basilicum (Q6USK1)
brenda
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