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Information on EC 1.14.14.145 - abieta-7,13-dien-18-ol hydroxylase
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EC Tree
1.14.14.145 abieta-7,13-dien-18-ol hydroxylaseIUBMB Comments
A cytochrome P-450 (heme-thiolate) protein. This enzyme catalyses a step in the pathway of abietic acid biosynthesis. The activity has been demonstrated in cell-free stem extracts of Abies grandis (grand fir) and Pinus contorta (lodgepole pine) , and the gene encoding the enzyme has been identified in Pinus taeda (loblolly pine) . The recombinant enzyme catalyses the oxidation of multiple diterpene alcohol and aldehydes, including levopimaradienol, isopimara-7,15-dienol, isopimara-7,15-dienal, dehydroabietadienol and dehydroabietadienal. It is not able to oxidize abietadiene.
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Word Map
- 1.14.14.145
- cyp1a1
-
diterpene
-
pinus
- taeda
-
loblolly
-
picea
-
conifer
-
nadph-cytochrome
-
olefins
- levopimaradiene
- spruce
- abietadiene
-
abietic
-
oleoresin
- sitchensis
The enzyme appears in viruses and cellular organisms
Reaction Schemes
Synonyms
cypa1, cyp720b1, abietadienol/abietadienal oxidase, 
more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
abieta-7,13-dien-18-ol hydroxylase
abietadienol/abietadienal oxidase
CYP720B1
EC 1.14.13.109
-
-
formerly
-
PtAO
CYP720B1
-
-
-
-
PtAO
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
abieta-7,13-dien-18,18-diol = abieta-7,13-dien-18-al + H2O
(1b), spontaneous
-
-
-
abieta-7,13-dien-18-al + [reduced NADPH-hemoprotein reductase] + O2 = abieta-7,13-dien-18-oate + [oxidized NADPH-hemoprotein reductase] + H2O
(1c)
-
-
-
abieta-7,13-dien-18-ol + 2 [reduced NADPH-hemoprotein reductase] + 2 O2 = abieta-7,13-dien-18-oate + 2 [oxidized NADPH-hemoprotein reductase] + 3 H2O
overall reaction
-
-
-
abieta-7,13-dien-18-ol + [reduced NADPH-hemoprotein reductase] + O2 = abieta-7,13-dien-18,18-diol + [oxidized NADPH-hemoprotein reductase] + H2O
(1a)
-
-
-
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PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
abieta-7,13-dien-18-ol,[reduced NADPH-hemoprotein reductase]:oxygen oxidoreductase (18-hydroxylating)
A cytochrome P-450 (heme-thiolate) protein. This enzyme catalyses a step in the pathway of abietic acid biosynthesis. The activity has been demonstrated in cell-free stem extracts of Abies grandis (grand fir) and Pinus contorta (lodgepole pine) [1], and the gene encoding the enzyme has been identified in Pinus taeda (loblolly pine) [3]. The recombinant enzyme catalyses the oxidation of multiple diterpene alcohol and aldehydes, including levopimaradienol, isopimara-7,15-dienol, isopimara-7,15-dienal, dehydroabietadienol and dehydroabietadienal. It is not able to oxidize abietadiene.
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CAS REGISTRY NUMBER
COMMENTARY
160477-93-0
-
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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
(13S)-pimara-7,15-dien-18-al + [reduced NADPH-hemoprotein reductase] + O2
(13S)-pimara-7,15-dien-18-oate + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
abieta-7,13-dien-18-al + [reduced NADPH-hemoprotein reductase] + O2
abieta-7,13-dien-18-oate + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
abieta-7,13-dien-18-ol + 2 [reduced NADPH-hemoprotein reductase] + 2 O2
abieta-7,13-dien-18-oate + 2 [oxidized NADPH-hemoprotein reductase] + 3 H2O
-
-
-
?
abieta-7,13-dien-18-ol + [reduced NADPH-hemoprotein reductase] + O2
abieta-7,13-dien-18-al + [oxidized NADPH-hemoprotein reductase] + H2O
abietadienal + [reduced NADPH-hemoprotein reductase] + O2
abieta-7,13-dien-18-oate + [oxidized NADPH-hemoprotein reductase] + H2O
oxidation at C-18
-
-
?
abietadienol + [reduced NADPH-hemoprotein reductase] + O2
abietadienal + [oxidized NADPH-hemoprotein reductase] + H2O
oxidation at C-18
-
-
?
dehydroabietadienal + [reduced NADPH-hemoprotein reductase] + O2
dehydroabietadienoate + [oxidized NADPH-hemoprotein reductase] + H2O
oxidation at C-18
-
-
?
dehydroabietadienol + [reduced NADPH-hemoprotein reductase] + O2
dehydroabietadienal + [oxidized NADPH-hemoprotein reductase] + H2O
isopimara-7,15-dienal + [reduced NADPH-hemoprotein reductase] + O2
isopimara-7,15-dien-18-oate + [oxidized NADPH-hemoprotein reductase] + H2O
oxidation at C-18
-
-
?
isopimara-7,15-dienol + [reduced NADPH-hemoprotein reductase] + O2
isopimara-7,15-dienal + [oxidized NADPH-hemoprotein reductase] + H2O
levopimaradienol + [reduced NADPH-hemoprotein reductase] + O2
levopimaradienal + [oxidized NADPH-hemoprotein reductase] + H2O
abieta-7,13-dien-18-ol + [reduced NADPH-hemoprotein reductase] + O2
abieta-7,13-dien-18-al + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
-
?
abieta-7,13-dien-18-ol + [reduced NADPH-hemoprotein reductase] + O2
abieta-7,13-dien-18-al + [oxidized NADPH-hemoprotein reductase] + H2O
-
activity is induced by wounding of the plant tissue reaching a maximum at 10 days after wounding with about a 60fold increase for the abietadienol hydroxylase
-
-
?
abieta-7,13-dien-18-ol + [reduced NADPH-hemoprotein reductase] + O2
abieta-7,13-dien-18-al + [oxidized NADPH-hemoprotein reductase] + H2O
-
this enzyme catalyzes a step in the pathway of abietic acid biosynthesis. Hydroxylation activity is maximally supported by NADPH, and NADH is less effective as reductant
-
-
?
abieta-7,13-dien-18-ol + [reduced NADPH-hemoprotein reductase] + O2
abieta-7,13-dien-18-al + [oxidized NADPH-hemoprotein reductase] + H2O
-
this enzyme catalyzes a step in the pathway of abietic acid biosynthesis
-
-
?
abieta-7,13-dien-18-ol + [reduced NADPH-hemoprotein reductase] + O2
abieta-7,13-dien-18-al + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
abieta-7,13-dien-18-ol + [reduced NADPH-hemoprotein reductase] + O2
abieta-7,13-dien-18-al + [oxidized NADPH-hemoprotein reductase] + H2O
PtAO catalyzes an array of consecutive oxidation steps with several different diterpenol and diterpenal intermediates in loblolly pine diterpene resin acid biosynthesis
-
-
?
dehydroabietadienol + [reduced NADPH-hemoprotein reductase] + O2
dehydroabietadienal + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
dehydroabietadienol + [reduced NADPH-hemoprotein reductase] + O2
dehydroabietadienal + [oxidized NADPH-hemoprotein reductase] + H2O
oxidation at C-18
-
-
?
isopimara-7,15-dienol + [reduced NADPH-hemoprotein reductase] + O2
isopimara-7,15-dienal + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
isopimara-7,15-dienol + [reduced NADPH-hemoprotein reductase] + O2
isopimara-7,15-dienal + [oxidized NADPH-hemoprotein reductase] + H2O
oxidation at C-18
-
-
?
levopimaradienol + [reduced NADPH-hemoprotein reductase] + O2
levopimaradienal + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
levopimaradienol + [reduced NADPH-hemoprotein reductase] + O2
levopimaradienal + [oxidized NADPH-hemoprotein reductase] + H2O
oxidation at C-18
-
-
?
additional information
?
-
the enzyme is involved in formation of diterpene resin acids, DRAs, in pine, and plays an important role in constitutive and induced oleoresin defense
-
-
?
additional information
?
-
the enzyme is involved in formation of diterpene resin acids, DRAs, in pine, and plays an important role in constitutive and induced oleoresin defense
-
-
?
additional information
?
-
-
the enzyme is involved in formation of diterpene resin acids, DRAs, in pine, and plays an important role in constitutive and induced oleoresin defense
-
-
?
additional information
?
-
the enzyme is involved in formation of diterpene resin acids, DRAs, in pine, and plays an important role in constitutive and induced oleoresin defense
-
-
?
additional information
?
-
the enzyme is involved in formation of diterpene resin acids, DRAs, in pine, and plays an important role in constitutive and induced oleoresin defense
-
-
?
additional information
?
-
the enzyme is involved in formation of diterpene resin acids, DRAs, in pine, and plays an important role in constitutive and induced oleoresin defense
-
-
?
additional information
?
-
the enzyme is involved in formation of diterpene resin acids, DRAs, in pine, and plays an important role in constitutive and induced oleoresin defense
-
-
?
additional information
?
-
-
the enzyme is involved in formation of diterpene resin acids, DRAs, in pine, and plays an important role in constitutive and induced oleoresin defense, the enzyme catalyzes an array of consecutive oxidation steps with several different diterpenol and diterpenal intermediates in loblolly pine DRA biosynthesis
-
-
?
additional information
?
-
the enzyme is involved in formation of diterpene resin acids, DRAs, in pine, and plays an important role in constitutive and induced oleoresin defense, the enzyme catalyzes an array of consecutive oxidation steps with several different diterpenol and diterpenal intermediates in loblolly pine DRA biosynthesis
-
-
?
additional information
?
-
the enzyme is involved in formation of diterpene resin acids, DRAs, in pine, and plays an important role in constitutive and induced oleoresin defense, the enzyme catalyzes an array of consecutive oxidation steps with several different diterpenol and diterpenal intermediates in loblolly pine DRA biosynthesis
-
-
?
additional information
?
-
the enzyme is involved in formation of diterpene resin acids, DRAs, in pine, and plays an important role in constitutive and induced oleoresin defense, the enzyme catalyzes an array of consecutive oxidation steps with several different diterpenol and diterpenal intermediates in loblolly pine DRA biosynthesis
-
-
?
additional information
?
-
the enzyme is involved in formation of diterpene resin acids, DRAs, in pine, and plays an important role in constitutive and induced oleoresin defense, the enzyme catalyzes an array of consecutive oxidation steps with several different diterpenol and diterpenal intermediates in loblolly pine DRA biosynthesis
-
-
?
additional information
?
-
-
the enzyme CYP720B1 is a multifunctional, multisubstrate cytochrome P450 monooxygenase
-
-
?
additional information
?
-
the enzyme CYP720B1 is a multifunctional, multisubstrate cytochrome P450 monooxygenase
-
-
?
additional information
?
-
the enzyme CYP720B1 is a multifunctional, multisubstrate cytochrome P450 monooxygenase
-
-
?
additional information
?
-
the enzyme CYP720B1 is a multifunctional, multisubstrate cytochrome P450 monooxygenase
-
-
?
additional information
?
-
the enzyme CYP720B1 is a multifunctional, multisubstrate cytochrome P450 monooxygenase
-
-
?
additional information
?
-
-
the recombinant enzyme catalyzed the oxidation of multiple diterpene alcohol and aldehydes. It is not able to oxidize abietadiene. No activity with neoabietadienol or neoabietadienal
-
-
?
additional information
?
-
the recombinant enzyme catalyzed the oxidation of multiple diterpene alcohol and aldehydes. It is not able to oxidize abietadiene. No activity with neoabietadienol or neoabietadienal
-
-
?
additional information
?
-
the recombinant enzyme catalyzed the oxidation of multiple diterpene alcohol and aldehydes. It is not able to oxidize abietadiene. No activity with neoabietadienol or neoabietadienal
-
-
?
additional information
?
-
the recombinant enzyme catalyzed the oxidation of multiple diterpene alcohol and aldehydes. It is not able to oxidize abietadiene. No activity with neoabietadienol or neoabietadienal
-
-
?
additional information
?
-
the recombinant enzyme catalyzed the oxidation of multiple diterpene alcohol and aldehydes. It is not able to oxidize abietadiene. No activity with neoabietadienol or neoabietadienal
-
-
?
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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
abieta-7,13-dien-18-ol + 2 [reduced NADPH-hemoprotein reductase] + 2 O2
abieta-7,13-dien-18-oate + 2 [oxidized NADPH-hemoprotein reductase] + 3 H2O
-
-
-
?
abieta-7,13-dien-18-ol + [reduced NADPH-hemoprotein reductase] + O2
abieta-7,13-dien-18-al + [oxidized NADPH-hemoprotein reductase] + H2O
abieta-7,13-dien-18-ol + [reduced NADPH-hemoprotein reductase] + O2
abieta-7,13-dien-18-al + [oxidized NADPH-hemoprotein reductase] + H2O
-
activity is induced by wounding of the plant tissue reaching a maximum at 10 days after wounding with about a 60fold increase for the abietadienol hydroxylase
-
-
?
abieta-7,13-dien-18-ol + [reduced NADPH-hemoprotein reductase] + O2
abieta-7,13-dien-18-al + [oxidized NADPH-hemoprotein reductase] + H2O
-
this enzyme catalyzes a step in the pathway of abietic acid biosynthesis. Hydroxylation activity is maximally supported by NADPH, and NADH is less effective as reductant
-
-
?
abieta-7,13-dien-18-ol + [reduced NADPH-hemoprotein reductase] + O2
abieta-7,13-dien-18-al + [oxidized NADPH-hemoprotein reductase] + H2O
-
this enzyme catalyzes a step in the pathway of abietic acid biosynthesis
-
-
?
abieta-7,13-dien-18-ol + [reduced NADPH-hemoprotein reductase] + O2
abieta-7,13-dien-18-al + [oxidized NADPH-hemoprotein reductase] + H2O
PtAO catalyzes an array of consecutive oxidation steps with several different diterpenol and diterpenal intermediates in loblolly pine diterpene resin acid biosynthesis
-
-
?
additional information
?
-
the enzyme is involved in formation of diterpene resin acids, DRAs, in pine, and plays an important role in constitutive and induced oleoresin defense
-
-
?
additional information
?
-
the enzyme is involved in formation of diterpene resin acids, DRAs, in pine, and plays an important role in constitutive and induced oleoresin defense
-
-
?
additional information
?
-
-
the enzyme is involved in formation of diterpene resin acids, DRAs, in pine, and plays an important role in constitutive and induced oleoresin defense
-
-
?
additional information
?
-
the enzyme is involved in formation of diterpene resin acids, DRAs, in pine, and plays an important role in constitutive and induced oleoresin defense
-
-
?
additional information
?
-
the enzyme is involved in formation of diterpene resin acids, DRAs, in pine, and plays an important role in constitutive and induced oleoresin defense
-
-
?
additional information
?
-
the enzyme is involved in formation of diterpene resin acids, DRAs, in pine, and plays an important role in constitutive and induced oleoresin defense
-
-
?
additional information
?
-
the enzyme is involved in formation of diterpene resin acids, DRAs, in pine, and plays an important role in constitutive and induced oleoresin defense
-
-
?
additional information
?
-
-
the enzyme is involved in formation of diterpene resin acids, DRAs, in pine, and plays an important role in constitutive and induced oleoresin defense, the enzyme catalyzes an array of consecutive oxidation steps with several different diterpenol and diterpenal intermediates in loblolly pine DRA biosynthesis
-
-
?
additional information
?
-
the enzyme is involved in formation of diterpene resin acids, DRAs, in pine, and plays an important role in constitutive and induced oleoresin defense, the enzyme catalyzes an array of consecutive oxidation steps with several different diterpenol and diterpenal intermediates in loblolly pine DRA biosynthesis
-
-
?
additional information
?
-
the enzyme is involved in formation of diterpene resin acids, DRAs, in pine, and plays an important role in constitutive and induced oleoresin defense, the enzyme catalyzes an array of consecutive oxidation steps with several different diterpenol and diterpenal intermediates in loblolly pine DRA biosynthesis
-
-
?
additional information
?
-
the enzyme is involved in formation of diterpene resin acids, DRAs, in pine, and plays an important role in constitutive and induced oleoresin defense, the enzyme catalyzes an array of consecutive oxidation steps with several different diterpenol and diterpenal intermediates in loblolly pine DRA biosynthesis
-
-
?
additional information
?
-
the enzyme is involved in formation of diterpene resin acids, DRAs, in pine, and plays an important role in constitutive and induced oleoresin defense, the enzyme catalyzes an array of consecutive oxidation steps with several different diterpenol and diterpenal intermediates in loblolly pine DRA biosynthesis
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
FAD
-
omission of flavins results in measurable reduction in both hydroxylation activities
FMN
-
omission of flavins results in measurable reduction in both hydroxylation activities
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
the enzyme expression is induced upon simulated insect attack using methyl jasmonate treatment of loblolly pine
-
additional information
the enzyme expression is induced upon simulated insect attack using methyl jasmonate treatment of loblolly pine
-
additional information
the enzyme expression is induced upon simulated insect attack using methyl jasmonate treatment of loblolly pine
-
additional information
the enzyme expression is induced upon simulated insect attack using methyl jasmonate treatment of loblolly pine
-
additional information
the enzyme expression is induced upon simulated insect attack using methyl jasmonate treatment of loblolly pine
-
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Coinfection
Co-expression of human cytochrome P4501A1 (CYP1A1) variants and human NADPH-cytochrome P450 reductase in the baculovirus/insect cell system.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0015
isopimaradienol
pH 7.6, 30°C, recombinant enzyme
0.0005
abietadienal
pH 7.6, 30°C, recombinant enzyme
0.0008
abietadienol
pH 7.6, 30°C, recombinant enzyme
0.0006
dehydroabietadienal
pH 7.6, 30°C, recombinant enzyme
0.0053
dehydroabietadienol
pH 7.6, 30°C, recombinant enzyme
0.0006
isopimaradienal
pH 7.6, 30°C, recombinant enzyme
0.0019
levopimaradienol
pH 7.6, 30°C, recombinant enzyme
additional information
additional information
-
MichaelisMenten kinetics, recombinant enzyme
-
additional information
additional information
MichaelisMenten kinetics, recombinant enzyme
-
additional information
additional information
MichaelisMenten kinetics, recombinant enzyme
-
additional information
additional information
MichaelisMenten kinetics, recombinant enzyme
-
additional information
additional information
MichaelisMenten kinetics, recombinant enzyme
-
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
Abies grandis
-
no inhibition detected by ancymidol at 0.2 mM
-
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.5 - 7.6
7.6
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7 - 8
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
32
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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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). C72B1_PINTA
481
1
55702
Swiss-Prot
Secretory Pathway (Reliability: 2)
A0A2P6RUC7_ROSCH
499
1
57435
TrEMBL
Secretory Pathway (Reliability: 2)
A0A2P6SMN2_ROSCH
500
0
57488
TrEMBL
Secretory Pathway (Reliability: 3)
A0A2P6SG79_ROSCH
393
0
45563
TrEMBL
other Location (Reliability: 5)
A0A2P6SMQ2_ROSCH
506
2
57869
TrEMBL
Secretory Pathway (Reliability: 4)
A0A2P6SII9_ROSCH
287
0
33258
TrEMBL
other Location (Reliability: 3)
G7LDJ8_MEDTR
512
2
58852
TrEMBL
Secretory Pathway (Reliability: 1)
A0A396GJD6_MEDTR
204
1
23581
TrEMBL
Secretory Pathway (Reliability: 1)
G7ZXN1_MEDTR
515
1
59593
TrEMBL
Secretory Pathway (Reliability: 1)
A0A2P6QKU8_ROSCH
102
0
12063
TrEMBL
other Location (Reliability: 5)
G7LDK1_MEDTR
511
1
58844
TrEMBL
Secretory Pathway (Reliability: 1)
A0A2P6SMI4_ROSCH
138
1
15913
TrEMBL
Secretory Pathway (Reliability: 4)
A0A2P6SML6_ROSCH
525
1
59851
TrEMBL
Secretory Pathway (Reliability: 4)
A0A2P6P821_ROSCH
514
1
59006
TrEMBL
Secretory Pathway (Reliability: 1)
A0A2P6RXU5_ROSCH
193
0
22714
TrEMBL
Mitochondrion (Reliability: 3)
A0A396GM56_MEDTR
140
0
16111
TrEMBL
other Location (Reliability: 2)
A0A396HLN7_MEDTR
497
1
57269
TrEMBL
other Location (Reliability: 3)
G7ID37_MEDTR
508
1
58547
TrEMBL
Secretory Pathway (Reliability: 1)
A0A2P6SMI9_ROSCH
524
1
60328
TrEMBL
other Location (Reliability: 5)
A0A2P6P1E8_ROSCH
489
1
56000
TrEMBL
Secretory Pathway (Reliability: 2)
A0A2P6SG86_ROSCH
517
1
59695
TrEMBL
Secretory Pathway (Reliability: 1)
A0A2P6SG73_ROSCH
67
0
7770
TrEMBL
other Location (Reliability: 4)
A0A2P6SIJ4_ROSCH
187
1
21029
TrEMBL
Secretory Pathway (Reliability: 5)
A0A7C9CEN8_OPUST
121
1
14170
TrEMBL
Secretory Pathway (Reliability: 2)
A0A7C9CTZ0_OPUST
400
1
45831
TrEMBL
Secretory Pathway (Reliability: 2)
A0A2P6SG89_ROSCH
517
1
60033
TrEMBL
Secretory Pathway (Reliability: 1)
G7ZXN7_MEDTR
510
1
58575
TrEMBL
Secretory Pathway (Reliability: 1)
A0A2P6SMN3_ROSCH
208
1
24555
TrEMBL
Secretory Pathway (Reliability: 2)
A0A396K819_MEDTR
299
0
34645
TrEMBL
other Location (Reliability: 4)
A0A7C8YTC9_OPUST
305
0
34943
TrEMBL
Secretory Pathway (Reliability: 4)
G7LCS2_MEDTR
513
1
59048
TrEMBL
Secretory Pathway (Reliability: 1)
A0A2G9IA64_9LAMI
499
1
57225
TrEMBL
Secretory Pathway (Reliability: 2)
A0A2P6RY09_ROSCH
541
1
62936
TrEMBL
Secretory Pathway (Reliability: 4)
A0A2G9GJK6_9LAMI
439
0
50243
TrEMBL
other Location (Reliability: 1)
G7LDK2_MEDTR
510
1
58597
TrEMBL
Secretory Pathway (Reliability: 1)
A0A2P6SMR2_ROSCH
502
0
57355
TrEMBL
Secretory Pathway (Reliability: 4)
A0A2P6QGZ8_ROSCH
57
0
6297
TrEMBL
other Location (Reliability: 3)
A0A2P6SMJ7_ROSCH
500
1
57380
TrEMBL
Secretory Pathway (Reliability: 4)
A0A2P6RAU6_ROSCH
178
2
20205
TrEMBL
Secretory Pathway (Reliability: 4)
A0A2P6QC69_ROSCH
532
1
61163
TrEMBL
Mitochondrion (Reliability: 4)
A0A2G9H402_9LAMI
498
0
56503
TrEMBL
Secretory Pathway (Reliability: 5)
A0A2P6SMS2_ROSCH
479
0
54720
TrEMBL
Secretory Pathway (Reliability: 2)
A0A2G9GVV1_9LAMI
491
1
56647
TrEMBL
other Location (Reliability: 5)
A0A7C9CFU1_OPUST
140
2
16354
TrEMBL
Secretory Pathway (Reliability: 2)
G7K3H1_MEDTR
474
1
53583
TrEMBL
Mitochondrion (Reliability: 5)
A0A2P6RRP5_ROSCH
104
0
12265
TrEMBL
Mitochondrion (Reliability: 3)
A0A396JUC7_MEDTR
104
1
12134
TrEMBL
Secretory Pathway (Reliability: 1)
A0A072UD95_MEDTR
508
1
58415
TrEMBL
Secretory Pathway (Reliability: 1)
A0A396GGF5_MEDTR
46
0
5350
TrEMBL
other Location (Reliability: 2)
A0A2P6SMP8_ROSCH
567
1
64887
TrEMBL
other Location (Reliability: 3)
A0A2P6SML8_ROSCH
501
1
57582
TrEMBL
Secretory Pathway (Reliability: 4)
A0A2P6SMQ3_ROSCH
514
1
59960
TrEMBL
Secretory Pathway (Reliability: 2)
A0A2G9H4H9_9LAMI
476
0
54443
TrEMBL
Mitochondrion (Reliability: 4)
A0A2P6SG72_ROSCH
299
0
35025
TrEMBL
other Location (Reliability: 4)
A0A2P6SIJ7_ROSCH
508
1
58103
TrEMBL
Secretory Pathway (Reliability: 5)
A0A2P6SML0_ROSCH
137
0
15715
TrEMBL
other Location (Reliability: 2)
A0A2P6SMM8_ROSCH
215
0
24529
TrEMBL
other Location (Reliability: 3)
A0A2P6SG76_ROSCH
285
0
32817
TrEMBL
other Location (Reliability: 1)
A0A2P6SG67_ROSCH
245
0
28444
TrEMBL
Mitochondrion (Reliability: 4)
A0A2P6SMM1_ROSCH
500
1
57092
TrEMBL
Secretory Pathway (Reliability: 2)
A0A2P6SML1_ROSCH
500
1
57349
TrEMBL
Secretory Pathway (Reliability: 5)
A0A2P6RRB3_ROSCH
500
2
57057
TrEMBL
Secretory Pathway (Reliability: 5)
A0A2P6SG77_ROSCH
513
1
59525
TrEMBL
Secretory Pathway (Reliability: 1)
A0A2P6QC63_ROSCH
472
0
54072
TrEMBL
Mitochondrion (Reliability: 5)
A0A2P6SMJ5_ROSCH
78
0
9143
TrEMBL
other Location (Reliability: 3)
A0A7C9D076_OPUST
124
0
14789
TrEMBL
other Location (Reliability: 4)
A0A2P6SG75_ROSCH
510
1
59300
TrEMBL
Secretory Pathway (Reliability: 1)
A0A2P6SMK0_ROSCH
184
1
21544
TrEMBL
Secretory Pathway (Reliability: 4)
A0A2P6SG82_ROSCH
513
1
59244
TrEMBL
Secretory Pathway (Reliability: 1)
A0A2P6SGC5_ROSCH
211
0
24541
TrEMBL
other Location (Reliability: 2)
A0A2P6SGA3_ROSCH
485
1
56160
TrEMBL
Secretory Pathway (Reliability: 1)
A0A2G9G833_9LAMI
392
1
45330
TrEMBL
Secretory Pathway (Reliability: 1)
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
CYP720B1, functional cDNA screening and expression as FLAG-tagged protein in Saccharomyces cerevisiae, de novo diterpenoid formation in metabolically engineered yeast, overview
CYP720B1, functional cDNA screening and expression as FLAG-tagged protein in Saccharomyces cerevisiae, DNA and amino acid sequence determination and analysis
CYPA, functional cDNA screening and expression as FLAG-tagged protein in Saccharomyces cerevisiae, DNA and amino acid sequence determination and analysis
CYPA1, functional cDNA screening and expression as FLAG-tagged protein in Saccharomyces cerevisiae, DNA and amino acid sequence determination and analysis
CYPA2, functional cDNA screening and expression as FLAG-tagged protein in Saccharomyces cerevisiae, DNA and amino acid sequence determination and analysis
CYPB, functional cDNA screening and expression as FLAG-tagged protein in Saccharomyces cerevisiae, DNA and amino acid sequence determination and analysis
CYPC, functional cDNA screening and expression as FLAG-tagged protein in Saccharomyces cerevisiae, DNA and amino acid sequence determination and analysis
expression of GFP-fusion protein in transiently transformed tobacco cells. The first 48 amino of PtAO are fused to the N-terminus of green fluorescent protein (GFP) and expressed in tobacco under control of Cauliflower Mosaic Virus 35S promoter
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Ro, D.K.; Bohlmann, J.
Diterpene resin acid biosynthesis in loblolly pine (Pinus taeda): Functional characterization of abietadiene/levopimaradiene synthase (PtTPS-LAS) cDNA and subcellular targeting of PtTPS-LAS and abietadienol/abietadienal oxidase (PtAO, CYP720B1)
Phytochemistry
67
1572-1578
2006
Pinus taeda (Q50EK6), Pinus taeda
brenda
Ro, D.K.; Arimura, G.; Lau, S.Y.; Piers, E.; Bohlmann, J.
Loblolly pine abietadienol/abietadienal oxidase PtAO (CYP720B1) is a multifunctional, multisubstrate cytochrome P450 monooxygenase
Proc. Natl. Acad. Sci. USA
102
8060-8065
2005
Pinus taeda, Pinus taeda (Q50EK3), Pinus taeda (Q50EK4), Pinus taeda (Q50EK5), Pinus taeda (Q50EK6), Picea sitchensis (Q50EK0), Picea sitchensis (Q50EK1)
brenda
Funk, C.; Croteau, R.
Diterpenoid resin acid biosynthesis in conifers: characterization of two cytochrome P450-dependent monooxygenases and an aldehyde dehydrogenase involved in abietic acid biosynthesis
Arch. Biochem. Biophys.
308
258-266
1994
Abies grandis, Pinus contorta
brenda
Funk, C.; Lewinsohn, E.; Vogel, B.; Steele, C.; Croteau, R.
Regulation of oleoresinosis in grand fir (Abies grandis). Coordinate induction of monoterpene and diterpene cyclases and two cytochrome P450-dependent diterpenoid hydroxylases by stem wounding
Plant Physiol.
106
999-1005
1994
Abies grandis
brenda
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Release 2023.1 (January 2023)
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