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dimethylallyl diphosphate + H2O
dimethylallyl phosphate + phosphate
Substrates: -
Products: -
?
farnesyl diphosphate + H2O
farnesyl phosphate + phosphate
geranyl diphosphate + H2O
geranyl phosphate + phosphate
geranylgeranyl diphosphate + H2O
geranylgeranyl phosphate + phosphate
Substrates: -
Products: -
?
isopentenyl diphosphate + H2O
isopentenyl phosphate + phosphate
Substrates: -
Products: -
?
mevalonate 5-diphosphate + H2O
mevanolate 5-phosphate + phosphate
Substrates: -
Products: -
?
additional information
?
-
farnesyl diphosphate + H2O

farnesyl phosphate + phosphate
Substrates: -
Products: -
?
farnesyl diphosphate + H2O
farnesyl phosphate + phosphate
Substrates: preferred substrate
Products: -
?
farnesyl diphosphate + H2O
farnesyl phosphate + phosphate
Substrates: -
Products: -
?
farnesyl diphosphate + H2O
farnesyl phosphate + phosphate
-
Substrates: -
Products: -
?
farnesyl diphosphate + H2O
farnesyl phosphate + phosphate
-
Substrates: preferred substrate
Products: -
?
farnesyl diphosphate + H2O
farnesyl phosphate + phosphate
Substrates: -
Products: -
?
farnesyl diphosphate + H2O
farnesyl phosphate + phosphate
-
Substrates: -
Products: -
?
farnesyl diphosphate + H2O
farnesyl phosphate + phosphate
-
Substrates: preferred substrate
Products: -
?
farnesyl diphosphate + H2O
farnesyl phosphate + phosphate
Substrates: -
Products: -
?
farnesyl diphosphate + H2O
farnesyl phosphate + phosphate
Substrates: highly preferred substrate
Products: -
?
geranyl diphosphate + H2O

geranyl phosphate + phosphate
-
Substrates: -
Products: -
?
geranyl diphosphate + H2O
geranyl phosphate + phosphate
Substrates: -
Products: -
?
geranyl diphosphate + H2O
geranyl phosphate + phosphate
Substrates: -
Products: -
?
geranyl diphosphate + H2O
geranyl phosphate + phosphate
-
Substrates: -
Products: -
?
geranyl diphosphate + H2O
geranyl phosphate + phosphate
Substrates: -
Products: -
?
geranyl diphosphate + H2O
geranyl phosphate + phosphate
-
Substrates: -
Products: -
?
geranyl diphosphate + H2O
geranyl phosphate + phosphate
Substrates: -
Products: -
?
geranyl diphosphate + H2O
geranyl phosphate + phosphate
-
Substrates: -
Products: -
?
geranyl diphosphate + H2O
geranyl phosphate + phosphate
-
Substrates: -
Products: -
?
geranyl diphosphate + H2O
geranyl phosphate + phosphate
-
Substrates: -
Products: -
?
additional information

?
-
Substrates: substrate specificity, overview. Negligible activity with IPP, dGTP, and 8-oxo-dGTP
Products: -
-
additional information
?
-
-
Substrates: substrate specificity, overview. Negligible activity with IPP, no activity with dGTP and 8-oxo-dGTP
Products: -
-
additional information
?
-
Substrates: very low activity with 8-oxo-dGTP and dGTP, substrates of Arabidospis thaliana Nudx1, EC 3.6.1.
Products: -
?
additional information
?
-
-
Substrates: substrate specificity, overview. Negligible activity with IPP, no activity with dGTP and 8-oxo-dGTP
Products: -
-
additional information
?
-
Substrates: substrate specificity, overview. Negligible activity with IPP, no activity with dGTP and 8-oxo-dGTP
Products: -
-
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farnesyl diphosphate + H2O
farnesyl phosphate + phosphate
geranyl diphosphate + H2O
geranyl phosphate + phosphate
farnesyl diphosphate + H2O

farnesyl phosphate + phosphate
Substrates: -
Products: -
?
farnesyl diphosphate + H2O
farnesyl phosphate + phosphate
-
Substrates: -
Products: -
?
farnesyl diphosphate + H2O
farnesyl phosphate + phosphate
-
Substrates: -
Products: -
?
farnesyl diphosphate + H2O
farnesyl phosphate + phosphate
Substrates: -
Products: -
?
geranyl diphosphate + H2O

geranyl phosphate + phosphate
-
Substrates: -
Products: -
?
geranyl diphosphate + H2O
geranyl phosphate + phosphate
Substrates: -
Products: -
?
geranyl diphosphate + H2O
geranyl phosphate + phosphate
-
Substrates: -
Products: -
?
geranyl diphosphate + H2O
geranyl phosphate + phosphate
-
Substrates: -
Products: -
?
geranyl diphosphate + H2O
geranyl phosphate + phosphate
Substrates: -
Products: -
?
geranyl diphosphate + H2O
geranyl phosphate + phosphate
-
Substrates: -
Products: -
?
geranyl diphosphate + H2O
geranyl phosphate + phosphate
-
Substrates: -
Products: -
?
geranyl diphosphate + H2O
geranyl phosphate + phosphate
-
Substrates: -
Products: -
?
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0.0098
dimethylallyl diphosphate
pH 8.0, 22°C
0.00048 - 0.0188
farnesyl diphosphate
0.000138 - 0.00878
geranyl diphosphate
0.0179
geranylgeranyl diphosphate
pH 8.0, 22°C
0.0124
isopentenyl diphosphate
pH 8.0, 22°C
0.0268
mevalonate 5-diphosphate
pH 8.0, 22°C
0.00048
farnesyl diphosphate

pH not specified in the publication, temperature not specified in the publication
0.000484
farnesyl diphosphate
pH 8.8, 30°C, recombinant enzyme
0.000495
farnesyl diphosphate
pH 8.8, 30°C, recombinant enzyme
0.000555
farnesyl diphosphate
-
pH 8.8, 30°C, recombinant enzyme
0.00154
farnesyl diphosphate
-
pH 8.8, 30°C, recombinant enzyme
0.004
farnesyl diphosphate
-
pH 8.8, 30°C, recombinant enzyme
0.0188
farnesyl diphosphate
pH 8.0, 22°C
0.000138
geranyl diphosphate

pH 8.8, 30°C, recombinant enzyme
0.00014
geranyl diphosphate
pH not specified in the publication, temperature not specified in the publication
0.000261
geranyl diphosphate
-
pH 8.8, 30°C, recombinant enzyme
0.00113
geranyl diphosphate
-
pH 8.8, 30°C, recombinant enzyme
0.00196
geranyl diphosphate
-
pH 8.8, 30°C, recombinant enzyme
0.0037
geranyl diphosphate
pH 8.0, 22°C
0.00878
geranyl diphosphate
pH 8.8, 30°C, recombinant enzyme
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0.94
dimethylallyl diphosphate
pH 8.0, 22°C
0.52 - 1.91
farnesyl diphosphate
0.2 - 0.78
geranyl diphosphate
0.15
geranylgeranyl diphosphate
pH 8.0, 22°C
0.87
isopentenyl diphosphate
pH 8.0, 22°C
0.55
mevalonate 5-diphosphate
pH 8.0, 22°C
0.52
farnesyl diphosphate

pH 8.0, 22°C
0.73
farnesyl diphosphate
-
pH 8.8, 30°C, recombinant enzyme
1.21
farnesyl diphosphate
-
pH 8.8, 30°C, recombinant enzyme
1.37
farnesyl diphosphate
-
pH 8.8, 30°C, recombinant enzyme
1.67
farnesyl diphosphate
pH 8.8, 30°C, recombinant enzyme
1.91
farnesyl diphosphate
pH 8.8, 30°C, recombinant enzyme
0.2
geranyl diphosphate

-
pH 8.8, 30°C, recombinant enzyme
0.21
geranyl diphosphate
pH 8.8, 30°C, recombinant enzyme
0.26
geranyl diphosphate
pH 8.8, 30°C, recombinant enzyme
0.29
geranyl diphosphate
-
pH 8.8, 30°C, recombinant enzyme
0.3
geranyl diphosphate
-
pH 8.8, 30°C, recombinant enzyme
0.78
geranyl diphosphate
pH 8.0, 22°C
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99.7
dimethylallyl diphosphate
pH 8.0, 22°C
27.5 - 3950
farnesyl diphosphate
23.92 - 1880
geranyl diphosphate
8.5
geranylgeranyl diphosphate
pH 8.0, 22°C
72.1
isopentenyl diphosphate
pH 8.0, 22°C
20.4
mevalonate 5-diphosphate
pH 8.0, 22°C
27.5
farnesyl diphosphate

pH 8.0, 22°C
182
farnesyl diphosphate
-
pH 8.8, 30°C, recombinant enzyme
786
farnesyl diphosphate
-
pH 8.8, 30°C, recombinant enzyme
2470
farnesyl diphosphate
-
pH 8.8, 30°C, recombinant enzyme
3373.7
farnesyl diphosphate
pH 8.8, 30°C, recombinant enzyme
3950
farnesyl diphosphate
pH 8.8, 30°C, recombinant enzyme
23.92
geranyl diphosphate

pH 8.8, 30°C, recombinant enzyme
102
geranyl diphosphate
-
pH 8.8, 30°C, recombinant enzyme
214.3
geranyl diphosphate
pH 8.0, 22°C
257
geranyl diphosphate
-
pH 8.8, 30°C, recombinant enzyme
1150
geranyl diphosphate
-
pH 8.8, 30°C, recombinant enzyme
1880
geranyl diphosphate
pH 8.8, 30°C, recombinant enzyme
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evolution

-
the phylogenetic tree shows that the species in the genus Rosa began to differentiate about 8.74 million years ago (mya) and completed it within 6.2 mya. Comparative genomics reveal differences in the composition of five groups of genes. The expanded gene families are significantly enriched in monoterpenoid biosynthesis, terpenoid backbone biosynthesis, and sesquiterpenoid and triterpenoid biosynthesis pathways, whole-genome duplication (WGD) analysis, overview
evolution
the enzyme belongs to the Nudix hydrolase gene family
evolution
-
the enzyme belongs to the Nudix hydrolase gene family
evolution
-
the enzyme belongs to the the Nudix hydrolase gene family
evolution
the enzyme belongs to the Nudix hydrolase gene family
evolution
-
the phylogenetic tree shows that the species in the genus Rosa began to differentiate about 8.74 million years ago (mya) and completed it within 6.2 mya. Comparative genomics reveal differences in the composition of five groups of genes. The expanded gene families are significantly enriched in monoterpenoid biosynthesis, terpenoid backbone biosynthesis, and sesquiterpenoid and triterpenoid biosynthesis pathways, whole-genome duplication (WGD) analysis overview
evolution
-
the phylogenetic tree shows that the species in the genus Rosa began to differentiate about 8.74 million years ago (mya) and completed it within 6.2 mya. Comparative genomics reveal differences in the composition of five groups of genes. The expanded gene families are significantly enriched in monoterpenoid biosynthesis, terpenoid backbone biosynthesis, and sesquiterpenoid and triterpenoid biosynthesis pathways, whole-genome duplication (WGD) analysis, overview
-
evolution
-
the phylogenetic tree shows that the species in the genus Rosa began to differentiate about 8.74 million years ago (mya) and completed it within 6.2 mya. Comparative genomics reveal differences in the composition of five groups of genes. The expanded gene families are significantly enriched in monoterpenoid biosynthesis, terpenoid backbone biosynthesis, and sesquiterpenoid and triterpenoid biosynthesis pathways, whole-genome duplication (WGD) analysis, overview
-
metabolism

-
in most plant species, geraniol is produced in a one-step, TPS-dependent manner, but in Rosa hybrida, geraniol production involves dephosphorylation of GPP to geranyl phosphate (GP) by NUDX1-1a, followed by further dephosphorylation of GP by unknown phosphatases. The function of NUDX1-1a in geraniol production results from the specialization of NUDX1 during natural evolution in roses. Geraniol, citronellol, and their derivatives are major components of the floral scent
metabolism
-
in most plant species, geraniol is produced in a one-step, TPS-dependent manner, but in Rosa hybrida, geraniol production involves dephosphorylation of GPP to geranyl phosphate (GP) by RhNUDX1-1a, followed by further dephosphorylation of GP by unknown phosphatases. The function of NUDX1-1a in geraniol production results from the specialization of NUDX1 during natural evolution in roses
metabolism
functional diversification in the Nudix hydrolase gene family drives sesquiterpene biosynthesis in Rosa x wichurana
metabolism
-
Rosa chinensis has a unique NUDX1 (Nudix hydrolase 1)-dependent monoterpene geraniol biosynthesis pathway, the rose has two cultivar varieties, Old Blush and Old Blus-like, with contrasting aromas, profiling of the volatile metabolome of both materials reveals that geraniol is the main component that distinguishes the aroma of these two varieties, analysis of transcriptional regulation, overview. RcNUDX1 is a key factor affecting geraniol content, as well as 17 transcription factor genes coexpressed with RcNUDX1
metabolism
-
in most plant species, geraniol is produced in a one-step, TPS-dependent manner, but in Rosa hybrida, geraniol production involves dephosphorylation of GPP to geranyl phosphate (GP) by NUDX1-1a, followed by further dephosphorylation of GP by unknown phosphatases. The function of NUDX1-1a in geraniol production results from the specialization of NUDX1 during natural evolution in roses. Geraniol, citronellol, and their derivatives are major components of the floral scent
metabolism
-
in most plant species, geraniol is produced in a one-step, TPS-dependent manner, but in Rosa hybrida, geraniol production involves dephosphorylation of GPP to geranyl phosphate (GP) by NUDX1-1a, followed by further dephosphorylation of GP by unknown phosphatases. The function of NUDX1-1a in geraniol production results from the specialization of NUDX1 during natural evolution in roses. Geraniol, citronellol, and their derivatives are major components of the floral scent
-
metabolism
-
in most plant species, geraniol is produced in a one-step, TPS-dependent manner, but in Rosa hybrida, geraniol production involves dephosphorylation of GPP to geranyl phosphate (GP) by NUDX1-1a, followed by further dephosphorylation of GP by unknown phosphatases. The function of NUDX1-1a in geraniol production results from the specialization of NUDX1 during natural evolution in roses. Geraniol, citronellol, and their derivatives are major components of the floral scent
-
physiological function

compared with control, petals expressing a isoformNUDX1 RNAi construct have fewer monoterpenes. Amounts of other volatiles are unaffected. Transient expression in Nicotiana benthamiana leads to enzyme accumulation in leaves and accumulation of geraniol and geraniol glycosides
physiological function
-
geraniol is the main component that distinguishes the aroma of different rose varieties, analysis of transcriptional regulation, overview. RcNUDX1 is a key factor affecting geraniol content, as well as 17 transcription factor genes coexpressed with RcNUDX1. Transcription factor RcWRKY70 binds to four W-box motifs in the promoter of RcNUDX1, repressing RcNUDX1 expression. Terpenes account for 54.8% of the 31 compounds that are more abundant in Old Blush petals. Terpenes also represented the highest proportion of detected compounds in Old Blush petals. By contrast, compounds derived from the shikimic acid pathway are more abundant in Old Blush-like petals (36.2%), followed by volatiles derived from fatty acids (33.3%), with terpenes only representing 28.5% of all volatiles detected in these samples
additional information

-
expression profiles of HMGR and TPS genes, overview
additional information
enzyme structure homology modeling using, in order to remove bias from a single template, several structures as templates: the crystal structure of AtNUDX1 in complex with IPP (PDB ID 6DBZ), 8-oxo-dGTP (PDB ID 6FL4), and GPP (PDB ID 5GP0), MutT and MTH1 in complex with 8-oxo-GMP (PDB IDs 3A6T and 3ZR0, respectively), and RhNUDX1 in complex with GPP (PDB ID 6YPF). Substrate binding pocket structure, structure comparisons, overview
additional information
-
enzyme structure homology modeling using, in order to remove bias from a single template, several structures as templates: the crystal structure of AtNUDX1 in complex with IPP (PDB ID 6DBZ), 8-oxo-dGTP (PDB ID 6FL4), and GPP (PDB ID 5GP0), MutT and MTH1 in complex with 8-oxo-GMP (PDB IDs 3A6T and 3ZR0, respectively), and RhNUDX1 in complex with GPP (PDB ID 6YPF), structure comparisons, overview
additional information
-
substrate binding pocket structure, structure comparisons, overview
additional information
substrate binding pocket structure, structure comparisons, overview
additional information
-
expression profiles of HMGR and TPS genes, overview
additional information
-
expression profiles of HMGR and TPS genes, overview
-
additional information
-
expression profiles of HMGR and TPS genes, overview
-
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hanging drop vapor diffusion method, using
-
purified recombinant detagged enzyme AtNUDX1, with and without substrate GPP, X-ray diffraction structure determination and analysis, model building, analysis of crystal structures of AtNUDX1 in complex with IPP (PDB ID 6DBZ), 8-oxo-dGTP (PDB ID 6FL4), and GPP (PDB ID 5GP0), overview
purified recombinant detagged enzyme RhNUDX1, with and without substrate GPP, from 200 mM ammonium sulfate, 100 mM sodium acetate, pH 4.6, and 25% PEG 400, for the complx crystals, soaking the crystals 1 sec in 5 mM GPP without divalent cations before flash-freezing in liquid nitrogen, X-ray diffraction structure determination and analysis at 1.7 A and 1.45 A resolution, respectively, model building (RhNUDX1 in complex with GPP, PDB ID 6YPF) and structure modeling
-
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F127N
-
the mutant shows reduced activity compared to the wild type enzyme
F127N/P129N
-
the mutant shows reduced activity compared to the wild type enzyme
F78N
-
the mutant shows reduced activity compared to the wild type enzyme
F85N
-
the mutation decreases the enzyme activity by nearly half or more
H42A
-
the mutant shows strongly reduced activity compared to the wild type enzyme
H49A
-
the mutation exhibits little effect on the catalytic reaction
L38N
-
the mutant shows reduced activity compared to the wild type enzyme
L45N
-
the mutation leads to severely compromised hydrolase activity toward geranyl diphosphate
P129N
-
the mutant shows reduced activity compared to the wild type enzyme
R27A
-
the mutant shows strongly reduced activity compared to the wild type enzyme
R34A
-
the mutation leads to severely compromised hydrolase activity toward geranyl diphosphate
V10K
-
the mutation leads to the dissociation of the enzyme dimer
V13N
-
the mutant shows reduced activity compared to the wild type enzyme
V20N
-
the mutation decreases the enzyme activity by nearly half or more
Y87A
-
the mutant shows strongly reduced activity compared to the wild type enzyme
Y94A
-
the mutation leads to severely compromised hydrolase activity toward geranyl diphosphate
F134N

-
the mutation leads to severely compromised hydrolase activity toward geranyl diphosphate
F134N
-
the mutation decreases the enzyme activity by nearly half or more
P136N

-
the mutation leads to severely compromised hydrolase activity toward geranyl diphosphate
P136N
-
the mutation exhibits little effect on the catalytic reaction
additional information

-
a three-step pathway in the citronellol synthesis is identified and successfully installed in Nicotiana benthamiana. The copy number of NUDX1-1a is a crucial factor in determining the variation of citronellol content in roses
additional information
-
a three-step pathway in the citronellol synthesis is identified and successfully installed in Nicotiana benthamiana. The copy number of NUDX1-1a is a crucial factor in determining the variation of citronellol content in roses
additional information
-
a three-step pathway in the citronellol synthesis is identified and successfully installed in Nicotiana benthamiana. The copy number of NUDX1-1a is a crucial factor in determining the variation of citronellol content in roses
additional information
-
a three-step pathway in the citronellol synthesis is identified and successfully installed in Nicotiana benthamiana. The copy number of NUDX1-1a is a crucial factor in determining the variation of citronellol content in roses
-
additional information
-
a three-step pathway in the citronellol synthesis is identified and successfully installed in Nicotiana benthamiana. The copy number of NUDX1-1a is a crucial factor in determining the variation of citronellol content in roses
-
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expression in Escherichia coli
four NUDX1-1a genes on chromosome 4, recombinant epression in Nicotiana benthamiana, coexpression with HMGR and TPS genes, whose expression leads to the enrichment of terpenes in roses
-
gene NUDX1-1a recombinant epression in Nicotiana benthamiana, coexpression with HMGR and TPS genes, whose expression leads to the enrichment of terpenes in roses
-
gene RcNUDX1, expression analysis. Three of the RcNUDX1 genes are expressed in the green-module, expression of transcription factor RcWRKY70 represses RcNUDX1 transcription
-
recombinant expression of C-terminally His6-tagged enzyme in Escherichia coli strain Rosetta 2 (DE3)
-
recombinant expression of His6-tagged enzyme in Escherichia coli strain Rosetta 2 (DE3)
recombinant expression of His6-tagged enzyme in Escherichia coli strain Rosetta 2 (DE3), transient recombinant expression in Nicotiana benthamiana leaves via transfection by Agrobacterium tumefaciens strain C58 (pMP90)
six NUDX1-1a genes on chromosome 4, recombinant epression in Nicotiana benthamiana, coexpression with HMGR and TPS genes, whose expression leads to the enrichment of terpenes in roses. The level of coverage of the NUDX1-1a genomic region is highly correlated with geraniol and citronellol content
-
recombinant expression of His6-tagged enzyme in Escherichia coli strain Rosetta 2 (DE3)

recombinant expression of His6-tagged enzyme in Escherichia coli strain Rosetta 2 (DE3)
-
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Magnard, J.; Roccia, A.; Caissard, J.; Vergne, P.; Sun, P.; Hecquet, R.; Dubois, A.; Oyant, L.; Jullien, F.; Nicole, F.; Raymond, O.; Huguet, S.; Baltenweck, R.; Meyer, S.; Claudel, P.; Jeauffre, J.; Rohmer, M.; Foucher, F.; Hugueney, P.; Bendahmane, M.
PLANT VOLATILES. Biosynthesis of monoterpene scent compounds in roses
Science
349
81-83
2015
Rosa hybrid cultivar (M4I1C6)
brenda
Liu, J.; Guan, Z.; Liu, H.; Qi, L.; Zhang, D.; Zou, T.; Yin, P.
Structural insights into the substrate recognition mechanism of Arabidopsis GPP-bound NUDX1 for noncanonical monoterpene biosynthesis
Mol. Plant
11
218-221
2018
Arabidopsis thaliana
brenda
Scaletti, E.R.; Unterlass, J.E.; Almloef, I.; Koolmeister, T.; Vallin, K.S.; Kapsitidou, D.; Tsuber, V.; Helleday, T.; Stenmark, P.; Jemth, A.S.
Kinetic and structural characterization of NUDT15 and NUDT18 as catalysts of isoprene pyrophosphate hydrolysis
FEBS J.
291
4301-4322
2024
Homo sapiens (Q6ZVK8)
brenda
Shang, J.; Feng, D.; Liu, H.; Niu, L.; Li, R.; Li, Y.; Chen, M.; Li, A.; Liu, Z.; He, Y.; Gao, X.; Jian, H.; Wang, C.; Tang, K.; Bao, M.; Wang, J.; Yang, S.; Yan, H.; Ning, G.
Evolution of the biosynthetic pathways of terpene scent compounds in roses
Curr. Biol.
34
3550-3563.e8
2024
Rosa rugosa, Rosa hybrid cultivar, Rosa chinensis, no activity in Rosa multiflora, no activity in Rosa wichuraiana, Rosa rugosa Wild, Rosa rugosa Zizhi
brenda
Yu, J.; Liu, X.; Peng, Y.; Li, Q.; Han, Y.
Identification and characterization of transcription factors involved in geraniol biosynthesis in Rosa chinensis
Int. J. Mol. Sci.
23
14684
2022
Rosa chinensis
brenda
Sun, P.; Degut, C.; Rety, S.; Caissard, J.C.; Hibrand-Saint Oyant, L.; Bony, A.; Paramita, S.N.; Conart, C.; Magnard, J.L.; Jeauffre, J.; Abd-El-Haliem, A.M.; Marie-Magdelaine, J.; Thouroude, T.; Baltenweck, R.; Tisne, C.; Foucher, F.; Haring, M.; Hugueney, P.; Schuurink, R.C.; Baudino, S.
Functional diversification in the Nudix hydrolase gene family drives sesquiterpene biosynthesis in Rosa x wichurana
Plant J.
104
185-199
2020
Rosa lucieae (M4I1C6), Arabidopsis thaliana (Q9CA40), Rosa chinensis, Rosa hybrid cultivar
brenda