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Information on EC 1.14.14.151 - premnaspirodiene oxygenase
for references in articles please use BRENDA:EC1.14.14.151
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EC Tree 1 Oxidoreductases
1.14 Acting on paired donors, with incorporation or reduction of molecular oxygen
1.14.14 With reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen into the other donor
1.14.14.151 premnaspirodiene oxygenase
IUBMB Comments
A cytochrome P-450 (heme-thiolate) protein. The enzyme from the plant Hyoscymus muticus also hydroxylates valencene at C-2 to give the α-hydroxy compound, nootkatol, and this is converted into nootkatone. 5-Epiaristolochene and epieremophilene are hydroxylated at C-2 to give a 2β-hydroxy derivatives that are not oxidized further.
The enzyme appears in viruses and cellular organisms
- 1.14.14.151
-
hyoscyamus
- muticus
-
+-valencene
- aroma
-
environmentally
-
regio
-
sesquiterpenoid
-
pichia
- grapefruit
- nootkatensis
-
+-nootkatone
- pastoris
Reaction Schemes
showSynonyms
premnaspirodiene oxygenase, cyp71d55, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
EC 1.14.13.121
-
-
formerly
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
(-)-vetispiradiene + 2 [reduced NADPH-hemoprotein reductase] + 2 O2 = solavetivone + 2 [oxidized NADPH-hemoprotein reductase] + 3 H2O
overall reaction
-
-
-
(-)-vetispiradiene + [reduced NADPH-hemoprotein reductase] + O2 = solavetivol + [oxidized NADPH-hemoprotein reductase] + H2O
(1a)
-
-
-
solavetivol + [reduced NADPH-hemoprotein reductase] + O2 = solavetivone + [oxidized NADPH-hemoprotein reductase] + 2 H2O
(1b)
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
(Ā)-vetispiradiene,[reduced NADPH-hemoprotein reductase]:oxygen 2alpha-oxidoreductase
A cytochrome P-450 (heme-thiolate) protein. The enzyme from the plant Hyoscymus muticus also hydroxylates valencene at C-2 to give the alpha-hydroxy compound, nootkatol, and this is converted into nootkatone. 5-Epiaristolochene and epieremophilene are hydroxylated at C-2 to give a 2beta-hydroxy derivatives that are not oxidized further.
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(+)-valencene + [reduced NADPH-hemoprotein reductase] + O2
alpha-nootkatol + beta-nootkatol + [oxidized NADPH-hemoprotein reductase] + H2O
Substrates: enzyme HPO-mediated biohydroxylation of (+)-valencene
Products: -
Products: -
?
(-)-vetispiradiene + [reduced NADPH-hemoprotein reductase] + O2
solavetivol + [oxidized NADPH-hemoprotein reductase] + H2O
Substrates: -
Products: solavetivol is also named premnaspirodien-2alpha-ol or (2S,4R,5S,7R)-spirovetiva-1(10),11(12)-dien-2-ol
Products: solavetivol is also named premnaspirodien-2alpha-ol or (2S,4R,5S,7R)-spirovetiva-1(10),11(12)-dien-2-ol
?
4-epi-eremophilene + [reduced NADPH-hemoprotein reductase] + O2
4-epieremophilen-2beta-ol + [oxidized NADPH-hemoprotein reductase] + H2O
Substrates: -
Products: -
Products: -
?
5-epiaristolochene + 3 [reduced NADPH-hemoprotein reductase] + 3 O2
2beta-hydroxy-5-epiaristolochene + 1beta-hydroxy-5-epiaristolochene + 3alpha-hydroxy-5-epiaristolochene + 3 [oxidized NADPH-hemoprotein reductase] + 3 H2O
Substrates: substrate affinity for 5-epiaristolochene is 2-4times lower than that for valencene or (-)-premnaspirodiene, respectively. HPO catalyzes the conversion of 5-epiaristolochene to four mono-hydroxylated products with 2beta-hydroxy-epiaristolochene comprising greater than 80% of the reaction products, 1beta-hydroxy-epiaristolochene about 5%, 3alpha-hydroxy-epiaristolochene less than 2%, and an unknown mono-hydroxylated product of about 20%
Products: -
Products: -
?
cedr-8-ene + [reduced NADPH-hemoprotein reductase] + O2
cedr-8-en-15-ol + [oxidized NADPH-hemoprotein reductase] + H2O
Substrates: -
Products: -
Products: -
?
valencene + 2 [reduced NADPH-hemoprotein reductase] + 2 O2
alpha-nootkatol + beta-nootkatol + 2 [oxidized NADPH-hemoprotein reductase] + 2 H2O
Substrates: -
Products: -
Products: -
?
additional information
?
-
Substrates: HPO also catalyzes the equivalent regio-specific (C-2) hydroxylation of several eremophilane-type (decalin ring system) sesquiterpenes, such as with 5-epi-aristolochene
Products: -
Products: -
?
additional information
?
-
-
Substrates: HPO also catalyzes the equivalent regio-specific (C-2) hydroxylation of several eremophilane-type (decalin ring system) sesquiterpenes, such as with 5-epi-aristolochene
Products: -
Products: -
?
additional information
?
-
Substrates: the enzyme fails to convert nootkatol to nootkatone
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme fails to convert nootkatol to nootkatone
Products: -
Products: -
?
additional information
?
-
Substrates: co-expression of enzyme HPO and cytochrome P450 reductase (CPR) leads to the hydroxylation of externally added (+)-valencene to trans-nootkatol in Pichia pastoris cells
Products: -
Products: -
?
additional information
?
-
-
Substrates: co-expression of enzyme HPO and cytochrome P450 reductase (CPR) leads to the hydroxylation of externally added (+)-valencene to trans-nootkatol in Pichia pastoris cells
Products: -
Products: -
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(+)-valencene + [reduced NADPH-hemoprotein reductase] + O2
alpha-nootkatol + beta-nootkatol + [oxidized NADPH-hemoprotein reductase] + H2O
Substrates: enzyme HPO-mediated biohydroxylation of (+)-valencene
Products: -
Products: -
?
additional information
?
-
Substrates: HPO also catalyzes the equivalent regio-specific (C-2) hydroxylation of several eremophilane-type (decalin ring system) sesquiterpenes, such as with 5-epi-aristolochene
Products: -
Products: -
?
additional information
?
-
-
Substrates: HPO also catalyzes the equivalent regio-specific (C-2) hydroxylation of several eremophilane-type (decalin ring system) sesquiterpenes, such as with 5-epi-aristolochene
Products: -
Products: -
?
additional information
?
-
Substrates: co-expression of enzyme HPO and cytochrome P450 reductase (CPR) leads to the hydroxylation of externally added (+)-valencene to trans-nootkatol in Pichia pastoris cells
Products: -
Products: -
?
additional information
?
-
-
Substrates: co-expression of enzyme HPO and cytochrome P450 reductase (CPR) leads to the hydroxylation of externally added (+)-valencene to trans-nootkatol in Pichia pastoris cells
Products: -
Products: -
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
NADPH-hemoprotein reductase
A flavoprotein containing both FMN and FAD. This enzyme catalyses the transfer of electrons from NADPH, an obligatory two-electron donor, to microsomal P-450 monooxygenases, EC 1.14.14._
-
NADPH-hemoprotein reductase
KY366226
A flavoprotein containing both FMN and FAD. This enzyme catalyses the transfer of electrons from NADPH, an obligatory two-electron donor, to microsomal P-450 monooxygenases, EC 1.14.14._
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0062
(-)-vetispiradiene
mutant enzyme V482I, in 100 mM Tris-HCl, pH 7.5, at 30Ā°C
0.0084
(-)-vetispiradiene
mutant enzyme V480I/A484I, in 100 mM Tris-HCl, pH 7.5, at 30Ā°C
0.013
(-)-vetispiradiene
mutant enzyme V482I/A484I, in 100 mM Tris-HCl, pH 7.5, at 30Ā°C
0.014
(-)-vetispiradiene
wild type enzyme, in 100 mM Tris-HCl, pH 7.5, at 30Ā°C
0.0025
5-epiaristolochene
mutant enzyme V480I/A484I, product is 2beta-hydroxy-epiaristolochene, in 100 mM Tris-HCl, pH 7.5, at 30Ā°C
0.0033
5-epiaristolochene
wild type enzyme, product is 2beta-hydroxy-epiaristolochene, in 100 mM Tris-HCl, pH 7.5, at 30Ā°C
0.0043
5-epiaristolochene
mutant enzyme V482I/A484I, product is 2beta-hydroxy-epiaristolochene, in 100 mM Tris-HCl, pH 7.5, at 30Ā°C
0.0179
5-epiaristolochene
mutant enzyme V482I, product is 2beta-hydroxy-epiaristolochene, in 100 mM Tris-HCl, pH 7.5, at 30Ā°C
0.0069
valencene
mutant enzyme V482I, product is beta-nootkatol, in 100 mM Tris-HCl, pH 7.5, at 30Ā°C
0.0074
valencene
wild type enzyme, product is beta-nootkatol, in 100 mM Tris-HCl, pH 7.5, at 30Ā°C
0.0121
valencene
mutant enzyme V482I/A484I, product is beta-nootkatol, in 100 mM Tris-HCl, pH 7.5, at 30Ā°C
0.0192
valencene
mutant enzyme V480I/A484I, product is beta-nootkatol, in 100 mM Tris-HCl, pH 7.5, at 30Ā°C
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2.1
(-)-vetispiradiene
wild type enzyme, in 100 mM Tris-HCl, pH 7.5, at 30Ā°C
3.8
(-)-vetispiradiene
mutant enzyme V482I, in 100 mM Tris-HCl, pH 7.5, at 30Ā°C
12.7
(-)-vetispiradiene
mutant enzyme V480I/A484I, in 100 mM Tris-HCl, pH 7.5, at 30Ā°C
20.7
(-)-vetispiradiene
mutant enzyme V482I/A484I, in 100 mM Tris-HCl, pH 7.5, at 30Ā°C
0.2
5-epiaristolochene
wild type enzyme, product is 2beta-hydroxy-epiaristolochene, in 100 mM Tris-HCl, pH 7.5, at 30Ā°C
0.7
5-epiaristolochene
mutant enzyme V480I/A484I, product is 2beta-hydroxy-epiaristolochene, in 100 mM Tris-HCl, pH 7.5, at 30Ā°C
1.4
5-epiaristolochene
mutant enzyme V482I, product is 2beta-hydroxy-epiaristolochene, in 100 mM Tris-HCl, pH 7.5, at 30Ā°C
2.8
5-epiaristolochene
mutant enzyme V482I/A484I, product is 2beta-hydroxy-epiaristolochene, in 100 mM Tris-HCl, pH 7.5, at 30Ā°C
1.9
valencene
wild type enzyme, product is beta-nootkatol, in 100 mM Tris-HCl, pH 7.5, at 30Ā°C
5.1
valencene
mutant enzyme V482I, product is beta-nootkatol, in 100 mM Tris-HCl, pH 7.5, at 30Ā°C
5.7
valencene
mutant enzyme V480I/A484I, product is beta-nootkatol, in 100 mM Tris-HCl, pH 7.5, at 30Ā°C
15.9
valencene
mutant enzyme V482I/A484I, product is beta-nootkatol, in 100 mM Tris-HCl, pH 7.5, at 30Ā°C
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
150
(-)-vetispiradiene
wild type enzyme, in 100 mM Tris-HCl, pH 7.5, at 30Ā°C
610
(-)-vetispiradiene
mutant enzyme V482I, in 100 mM Tris-HCl, pH 7.5, at 30Ā°C
1510
(-)-vetispiradiene
mutant enzyme V480I/A484I, in 100 mM Tris-HCl, pH 7.5, at 30Ā°C
1590
(-)-vetispiradiene
mutant enzyme V482I/A484I, in 100 mM Tris-HCl, pH 7.5, at 30Ā°C
60
5-epiaristolochene
wild type enzyme, product is 2beta-hydroxy-epiaristolochene, in 100 mM Tris-HCl, pH 7.5, at 30Ā°C
80
5-epiaristolochene
mutant enzyme V482I, product is 2beta-hydroxy-epiaristolochene, in 100 mM Tris-HCl, pH 7.5, at 30Ā°C
280
5-epiaristolochene
mutant enzyme V480I/A484I, product is 2beta-hydroxy-epiaristolochene, in 100 mM Tris-HCl, pH 7.5, at 30Ā°C
650
5-epiaristolochene
mutant enzyme V482I/A484I, product is 2beta-hydroxy-epiaristolochene, in 100 mM Tris-HCl, pH 7.5, at 30Ā°C
260
valencene
wild type enzyme, product is beta-nootkatol, in 100 mM Tris-HCl, pH 7.5, at 30Ā°C
300
valencene
mutant enzyme V480I/A484I, product is beta-nootkatol, in 100 mM Tris-HCl, pH 7.5, at 30Ā°C
740
valencene
mutant enzyme V482I, product is beta-nootkatol, in 100 mM Tris-HCl, pH 7.5, at 30Ā°C
1310
valencene
mutant enzyme V482I/A484I, product is beta-nootkatol, in 100 mM Tris-HCl, pH 7.5, at 30Ā°C
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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
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
KY366226
overexpression of rice premnaspirodiene oxygenase reduces the infection rate of Xanthomonas oryzae pv. oryzae. Gene OsCYP71 does not contain a signal peptide
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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). C7D55_HYOMU
502
0
56788
Swiss-Prot
Secretory Pathway (Reliability: 3)
G7K4E8_MEDTR
502
1
57962
TrEMBL
Secretory Pathway (Reliability: 1)
A0A072U9U4_MEDTR
500
1
56968
TrEMBL
Secretory Pathway (Reliability: 1)
G7K4L2_MEDTR
503
1
57326
TrEMBL
Secretory Pathway (Reliability: 1)
A0A2P6S6G7_ROSCH
520
0
58607
TrEMBL
Secretory Pathway (Reliability: 3)
A0A2G9HYB0_9LAMI
509
1
57927
TrEMBL
Secretory Pathway (Reliability: 2)
A0A2P6SB24_ROSCH
520
0
58364
TrEMBL
other Location (Reliability: 5)
A0A396HZL9_MEDTR
207
0
23424
TrEMBL
Secretory Pathway (Reliability: 5)
A0A396HCI4_MEDTR
204
0
23319
TrEMBL
other Location (Reliability: 5)
A0A396I4X9_MEDTR
543
1
62609
TrEMBL
other Location (Reliability: 4)
G7JZP7_MEDTR
502
1
57557
TrEMBL
Secretory Pathway (Reliability: 1)
G7K4E4_MEDTR
533
2
61253
TrEMBL
Secretory Pathway (Reliability: 2)
A0A2P6P5G3_ROSCH
385
1
43725
TrEMBL
Secretory Pathway (Reliability: 2)
A0A072UJ32_MEDTR
502
1
57567
TrEMBL
Secretory Pathway (Reliability: 1)
G7J474_MEDTR
509
1
57831
TrEMBL
Secretory Pathway (Reliability: 1)
A0A2P6S6F2_ROSCH
231
0
26147
TrEMBL
other Location (Reliability: 2)
A0A2P6P5G9_ROSCH
510
1
58178
TrEMBL
Secretory Pathway (Reliability: 3)
A0A396I2M3_MEDTR
555
1
63987
TrEMBL
Mitochondrion (Reliability: 4)
A0A2P6R511_ROSCH
519
0
58860
TrEMBL
Secretory Pathway (Reliability: 5)
A0A2P6P5G6_ROSCH
536
1
61100
TrEMBL
other Location (Reliability: 5)
A0A396HZ00_MEDTR
320
0
36671
TrEMBL
Mitochondrion (Reliability: 3)
A0A2G9I2Z1_9LAMI
509
1
57880
TrEMBL
Secretory Pathway (Reliability: 2)
A0A396HEG0_MEDTR
329
1
38034
TrEMBL
Secretory Pathway (Reliability: 3)
A0A2P6R510_ROSCH
219
1
24755
TrEMBL
Secretory Pathway (Reliability: 2)
A0A2P6QD81_ROSCH
518
0
58707
TrEMBL
Secretory Pathway (Reliability: 1)
A0A2P6QDF6_ROSCH
115
0
13619
TrEMBL
other Location (Reliability: 3)
A0A2P6SCN2_ROSCH
420
0
47465
TrEMBL
Secretory Pathway (Reliability: 3)
G7JMV4_MEDTR
503
1
57197
TrEMBL
Secretory Pathway (Reliability: 1)
A0A2P6QDB8_ROSCH
355
0
40519
TrEMBL
other Location (Reliability: 5)
A0A396HX15_MEDTR
246
0
28913
TrEMBL
other Location (Reliability: 2)
G7IFC5_MEDTR
500
2
57095
TrEMBL
Secretory Pathway (Reliability: 4)
A0A2P6QG57_ROSCH
86
0
10031
TrEMBL
Secretory Pathway (Reliability: 5)
A0A2P6S6H6_ROSCH
513
1
57569
TrEMBL
Mitochondrion (Reliability: 5)
A0A2G9HGN9_9LAMI
454
0
51889
TrEMBL
Mitochondrion (Reliability: 2)
A0A396HZH9_MEDTR
216
0
25268
TrEMBL
other Location (Reliability: 3)
A0A2P6S6G0_ROSCH
277
0
31605
TrEMBL
other Location (Reliability: 2)
A0A396HZP9_MEDTR
315
0
35790
TrEMBL
other Location (Reliability: 2)
A0A396I4W9_MEDTR
85
0
9838
TrEMBL
other Location (Reliability: 3)
A0A2P6QG75_ROSCH
148
0
16837
TrEMBL
other Location (Reliability: 5)
A0A072U7W3_MEDTR
503
1
56942
TrEMBL
Secretory Pathway (Reliability: 1)
A0A2P6SCB5_ROSCH
80
1
8868
TrEMBL
Secretory Pathway (Reliability: 4)
A0A396IJQ4_MEDTR
170
0
19922
TrEMBL
other Location (Reliability: 3)
G7K4F8_MEDTR
501
1
57548
TrEMBL
Secretory Pathway (Reliability: 1)
G7KAS9_MEDTR
506
2
57954
TrEMBL
Secretory Pathway (Reliability: 2)
G7K4E9_MEDTR
502
1
57449
TrEMBL
Secretory Pathway (Reliability: 1)
G7IUY3_MEDTR
240
0
27748
TrEMBL
other Location (Reliability: 4)
A0A2P6QD94_ROSCH
222
1
25688
TrEMBL
other Location (Reliability: 2)
G7K4L5_MEDTR
502
1
57022
TrEMBL
Secretory Pathway (Reliability: 2)
G7KAS8_MEDTR
507
2
57346
TrEMBL
Secretory Pathway (Reliability: 2)
A0A2G9H5V6_9LAMI
251
1
28972
TrEMBL
Secretory Pathway (Reliability: 5)
G7KAT1_MEDTR
505
2
57745
TrEMBL
Secretory Pathway (Reliability: 2)
G7JZQ3_MEDTR
503
1
57514
TrEMBL
Secretory Pathway (Reliability: 1)
A0A2P6PXD7_ROSCH
537
1
60683
TrEMBL
Secretory Pathway (Reliability: 1)
A0A2P6PXD7_ROSCH
537
1
60683
TrEMBL
Secretory Pathway (Reliability: 1)
A0A2P6SCQ4_ROSCH
378
1
42151
TrEMBL
Secretory Pathway (Reliability: 2)
A0A396JHD6_MEDTR
59
0
6405
TrEMBL
Secretory Pathway (Reliability: 3)
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
V480S
the mutation improves the kcat for the conversion of (-)-vetispiradiene to solavetivol about 2fold
V482I
V482I/A484I
the mutant possesses a 5fold improvement in its catalytic efficiency for nootkatol biosynthesis and a 10fold improvement for 2beta-hydroxy-epiaristolochene biosynthesis
additional information
V482I
the mutation improves the kcat for the conversion of (-)-vetispiradiene to solavetivol about 2fold
additional information
production of the sesquiterpenoid (+)-nootkatone by metabolic engineering of Pichia pastoris by generation of a strain co-expressing the premnaspirodiene oxygenase of Hyoscyamus muticus (HPO) and the Arabidopsis thaliana cytochrome P450 reductase (CPR) that hydroxylates extracellularly added (+)-valencene. Intracellular production of (+)-valencene by co-expression of valencene synthase from Callitropsis nootkatensis resolves the phase-transfer issues of (+)-valencene. Bi-phasic cultivations of Pichia pastoris result in the production of trans-nootkatol, which is oxidized to (+)-nootkatone by an intrinsic Pichia pastoris activity. Additional overexpression of a Pichia pastoris alcohol dehydrogenase and truncated hydroxy-methylglutaryl-CoA reductase (tHmg1p) significantly enhances the (+)-nootkatone yield to 208 mg/l cell culture in bioreactor cultivations. After 12 h of biotransformation about 50% of added (+)-valencene is converted to (+)-nootkatone without residual trans-nootkatol or ot herby-products, but with a moderate overall yield of 48% due to high substrate loss overtime. HPO,CPR and ADH-C3 protein levels are only marginally decreased by co-overexpression of tHMG1
additional information
-
production of the sesquiterpenoid (+)-nootkatone by metabolic engineering of Pichia pastoris by generation of a strain co-expressing the premnaspirodiene oxygenase of Hyoscyamus muticus (HPO) and the Arabidopsis thaliana cytochrome P450 reductase (CPR) that hydroxylates extracellularly added (+)-valencene. Intracellular production of (+)-valencene by co-expression of valencene synthase from Callitropsis nootkatensis resolves the phase-transfer issues of (+)-valencene. Bi-phasic cultivations of Pichia pastoris result in the production of trans-nootkatol, which is oxidized to (+)-nootkatone by an intrinsic Pichia pastoris activity. Additional overexpression of a Pichia pastoris alcohol dehydrogenase and truncated hydroxy-methylglutaryl-CoA reductase (tHmg1p) significantly enhances the (+)-nootkatone yield to 208 mg/l cell culture in bioreactor cultivations. After 12 h of biotransformation about 50% of added (+)-valencene is converted to (+)-nootkatone without residual trans-nootkatol or ot herby-products, but with a moderate overall yield of 48% due to high substrate loss overtime. HPO,CPR and ADH-C3 protein levels are only marginally decreased by co-overexpression of tHMG1
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
co-expression of C-terminally FLAG-tagged premnaspirodiene oxygenase of Hyoscyamus muticus (HPO) and the Arabidopsis thaliana cytochrome P450 reductase (CPR) in Pichia pastoris strains ADH-C1 and -C3
gene OsCYP71, DNA and amino acid seuence determination and analysis, sequence comparisons and phylogenetic analysis. Overexpression of full-length cDNA of premnaspirodiene oxygenase from Oryza sativa subsp. japonica in the wild-type, Dongjin, which is susceptible to bacterial blight Korean strain K2, transformed via Agrobacterium tumefaciens strain EHA105 reduces the infection rate of Xanthomonas oryzae pv. oryzae
KY366226
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Takahashi, S.; Yeo, Y.S.; Zhao, Y.; O'Maille, P.E.; Greenhagen, B.T.; Noel, J.P.; Coates, R.M.; Chappell, J.
Functional characterization of premnaspirodiene oxygenase, a cytochrome P450 catalyzing regio- and stereo-specific hydroxylations of diverse sesquiterpene substrates
J. Biol. Chem.
282
31744-31754
2007
Hyoscyamus muticus (A6YIH8), Hyoscyamus muticus
brenda
Nino, M.; Song, J.; Nogoy, F.; Kim, M.; Jung, Y.; Kang, K.; Nou, I.; Cho, Y.
Overexpression of rice premnaspirodiene oxygenase reduces the infection rate of Xanthomonas oryzae pv. oryzae
J. Plant Biotechnol.
43
422-431
2016
Oryza sativa Japonica Group (KY366226)
-
brenda
Wriessnegger, T.; Augustin, P.; Engleder, M.; Leitner, E.; Mueller, M.; Kaluzna, I.; Schuermann, M.; Mink, D.; Zellnig, G.; Schwab, H.; Pichler, H.
Production of the sesquiterpenoid (+)-nootkatone by metabolic engineering of Pichia pastoris
Metab. Eng.
24
18-29
2014
Hyoscyamus muticus (A6YIH8), Hyoscyamus muticus
brenda
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Release 2023.1 (January 2023)
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