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Enzyme Nomenclature
Information on EC 1.14.13.119 - 5-epiaristolochene 1,3-dihydroxylase
for references in articles please use BRENDA:EC1.14.13.119
Word Map on EC 1.14.13.119
- 1.14.13.119
-
sesquiterpene
- capsidiol
-
bicyclic
- capsicum
-
terpene
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The expected taxonomic range for this enzyme is: Nicotiana tabacum
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EC NUMBER 
COMMENTARY 
1.14.13.119
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RECOMMENDED NAME
GeneOntology No.
5-epiaristolochene 1,3-dihydroxylase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
5-epiaristolochene + 2 NADPH + 2 H+ + 2 O2 = capsidiol + 2 NADP+ + 2 H2O
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-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
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SYSTEMATIC NAME
IUBMB Comments
5-epiaristolochene,NADPH:oxygen oxidoreductase (1- and 3-hydroxylating)
A heme-thiolate protein (P-450). Kinetic studies suggest that 1beta-hydroxyepiaristolochene is mainly formed first followed by hydroxylation at C-3. However the reverse order via 3alpha-hydroxyepiaristolochene does occur.
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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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
1beta-hydroxy-5-epiaristolochene + NADPH + H+ + O2
capsidiol + NADP+ + H2O
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the catalytic efficiency for 1beta-hydroxy-5-epiaristolochene is about 10times greater than that for 3alpha-hydroxy-5-epiaristolochene
-
-
?
3alpha-hydroxy-5-epiaristolochene + NADPH + H+ + O2
capsidiol + NADP+ + H2O
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the catalytic efficiency for 3alpha-hydroxy-5-epiaristolochene is about 10times lower than that for 1beta-hydroxy-5-epiaristolochene
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-
?
5-epiaristolochene + NADPH + H+ + O2
1-deoxycapsidiol + NADP+ + H2O
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-
-
-
?
5-epiaristolochene + NADPH + H+ + O2
1beta-hydroxy-5-epiaristolochene + NADP+ + H2O
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the release of an 1beta-hydroxy-5-epiaristolochene intermediate at high 5-epiaristolochene concentrations and a 10fold catalytic preference for 1beta-hydroxy-5-epiaristolochene versus 3alpha-hydroxy-5-epiaristolochene is indicative of a preferred reaction order of hydroxylation at C-1, followed by that at C-3
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-
?
5-epiaristolochene + 2 NADPH + 2 H+ + 2 O2
3-deoxycapsidiol + 2 NADP+ + 2 H2O
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-
-
-
?
5-epiaristolochene + 2 NADPH + 2 H+ + 2 O2
3-deoxycapsidiol + 2 NADP+ + 2 H2O
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3-deoxycapsidiol is a reaction product when EAH is incubated with high concentrations (above 0.4 mM) of the 5-epiaristolochene substrate
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-
?
5-epiaristolochene + 2 NADPH + 2 H+ + 2 O2
capsidiol + 2 NADP+ + 2 H2O
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-
-
?
5-epiaristolochene + 2 NADPH + 2 H+ + 2 O2
capsidiol + 2 NADP+ + 2 H2O
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-
-
-
?
5-epiaristolochene + 2 NADPH + 2 H+ + 2 O2
capsidiol + 2 NADP+ + 2 H2O
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EAH mediates regio- and stereospecific hydroxylations at the C1 and C3 positions of 5-epi-aristolochene
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-
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
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
5-epiaristolochene + 2 NADPH + 2 H+ + 2 O2
3-deoxycapsidiol + 2 NADP+ + 2 H2O
-
3-deoxycapsidiol is a reaction product when EAH is incubated with high concentrations (above 0.4 mM) of the 5-epiaristolochene substrate
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-
?
5-epiaristolochene + 2 NADPH + 2 H+ + 2 O2
capsidiol + 2 NADP+ + 2 H2O
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-
-
-
?
5-epiaristolochene + NADPH + H+ + O2
1-deoxycapsidiol + NADP+ + H2O
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-
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Ancymidol
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dose-dependent inhibition with more than 80% by 0.075 mM ancymidol
dimethyl sulfoxide
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conversion of 5-epiaristolochene to capsidiol activity is inhibited at concentrations above 10% (v/v) dimethyl sulfoxide
ketoconazole
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dose-dependent inhibition with 95% inhibition at 0.1 mM ketoconazole
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
dimethyl sulfoxide
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maximum conversion of 5-epiaristolochene to capsidiol activity is observed at final concentrations of 2-5% (v/v) dimethyl sulfoxide
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00174
1beta-hydroxy-5-epiaristolochene
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wild type enzyme, the reaction product is capsidiol, in 100 mM Tris-HCl (pH 7.5), at 30°C
0.0062
1beta-hydroxy-5-epiaristolochene
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mutant enzyme S368A, the reaction product is capsidiol, in 100 mM Tris-HCl (pH 7.5), at 30°C
0.00997
1beta-hydroxy-5-epiaristolochene
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mutant enzyme S368T, the reaction product is capsidiol, in 100 mM Tris-HCl (pH 7.5), at 30°C
0.02124
1beta-hydroxy-5-epiaristolochene
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mutant enzyme I486A, the reaction product is capsidiol, in 100 mM Tris-HCl (pH 7.5), at 30°C
0.01518
5-epiaristolochene
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mutant enzyme S368T, the reaction product is capsidiol, in 100 mM Tris-HCl (pH 7.5), at 30°C
0.01672
5-epiaristolochene
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mutant enzyme S386V, the reaction product is 1beta-hydroxy-5-epiaristolochene, in 100 mM Tris-HCl (pH 7.5), at 30°C
0.01918
5-epiaristolochene
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wild type enzyme, the reaction product is capsidiol, in 100 mM Tris-HCl (pH 7.5), at 30°C
0.02267
5-epiaristolochene
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mutant enzyme S368A, the reaction product is capsidiol, in 100 mM Tris-HCl (pH 7.5), at 30°C
0.03863
5-epiaristolochene
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mutant enzyme S386C, the reaction product is 1beta-hydroxy-5-epiaristolochene, in 100 mM Tris-HCl (pH 7.5), at 30°C
0.0688
5-epiaristolochene
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mutant enzyme I486A, the reaction product is 1beta-hydroxy-5-epiaristolochene, in 100 mM Tris-HCl (pH 7.5), at 30°C
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.132
1beta-hydroxy-5-epiaristolochene
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mutant enzyme I486A, the reaction product is capsidiol, in 100 mM Tris-HCl (pH 7.5), at 30°C
0.482
1beta-hydroxy-5-epiaristolochene
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mutant enzyme S368T, the reaction product is capsidiol, in 100 mM Tris-HCl (pH 7.5), at 30°C
0.581
1beta-hydroxy-5-epiaristolochene
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mutant enzyme S368A, the reaction product is capsidiol, in 100 mM Tris-HCl (pH 7.5), at 30°C
0.582
1beta-hydroxy-5-epiaristolochene
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wild type enzyme, the reaction product is capsidiol, in 100 mM Tris-HCl (pH 7.5), at 30°C
0.037
5-epiaristolochene
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mutant enzyme S368T, the reaction product is capsidiol, in 100 mM Tris-HCl (pH 7.5), at 30°C
0.154
5-epiaristolochene
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mutant enzyme S368A, the reaction product is capsidiol, in 100 mM Tris-HCl (pH 7.5), at 30°C
0.278
5-epiaristolochene
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mutant enzyme S386C, the reaction product is 1beta-hydroxy-5-epiaristolochene, in 100 mM Tris-HCl (pH 7.5), at 30°C
0.293
5-epiaristolochene
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mutant enzyme I486A, the reaction product is 1beta-hydroxy-5-epiaristolochene, in 100 mM Tris-HCl (pH 7.5), at 30°C
0.493
5-epiaristolochene
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wild type enzyme, the reaction product is capsidiol, in 100 mM Tris-HCl (pH 7.5), at 30°C
0.553
5-epiaristolochene
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mutant enzyme S386V, the reaction product is 1beta-hydroxy-5-epiaristolochene, in 100 mM Tris-HCl (pH 7.5), at 30°C
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
6.2
1beta-hydroxy-5-epiaristolochene
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mutant enzyme I486A, the reaction product is capsidiol, in 100 mM Tris-HCl (pH 7.5), at 30°C
48.3
1beta-hydroxy-5-epiaristolochene
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mutant enzyme S368T, the reaction product is capsidiol, in 100 mM Tris-HCl (pH 7.5), at 30°C
93.7
1beta-hydroxy-5-epiaristolochene
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mutant enzyme S368A, the reaction product is capsidiol, in 100 mM Tris-HCl (pH 7.5), at 30°C
334.4
1beta-hydroxy-5-epiaristolochene
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wild type enzyme, the reaction product is capsidiol, in 100 mM Tris-HCl (pH 7.5), at 30°C
2.4
5-epiaristolochene
-
mutant enzyme S368T, the reaction product is capsidiol, in 100 mM Tris-HCl (pH 7.5), at 30°C
4.3
5-epiaristolochene
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mutant enzyme I486A, the reaction product is 1beta-hydroxy-5-epiaristolochene, in 100 mM Tris-HCl (pH 7.5), at 30°C
6.8
5-epiaristolochene
-
mutant enzyme S368A, the reaction product is capsidiol, in 100 mM Tris-HCl (pH 7.5), at 30°C
7.2
5-epiaristolochene
-
mutant enzyme S386C, the reaction product is 1beta-hydroxy-5-epiaristolochene, in 100 mM Tris-HCl (pH 7.5), at 30°C
25.7
5-epiaristolochene
-
wild type enzyme, the reaction product is capsidiol, in 100 mM Tris-HCl (pH 7.5), at 30°C
33.1
5-epiaristolochene
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mutant enzyme S386V, the reaction product is 1beta-hydroxy-5-epiaristolochene, in 100 mM Tris-HCl (pH 7.5), at 30°C
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
after an apparent lag phase of 8 h, a rapid induction of hydroxylase activity is observed 10 to 15 h after elicitor addition (cellulase or paraciticein) to the cell cultures, reaching a maximum by 18 h followed by a rather gradual decline of 10 to 20% over the next 8 h
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
I468A
-
the mutant produces significant amounts 1beta-hydroxy-5-epiaristolochene, but negligible amounts of capsidiol from 5-epiaristolochene
S368A
-
the mutant retains its ability to fully convert 5-epiaristolochene to capsidiol, but the turnover rates for capsidiol formation is 3-13times lower compared with that of the wild type enzyme and is also able to convert 1beta-hydroxy-5-epiaristolochene to capsidiol with kcat values comparable with that of wild type enzyme, but with Km values for 1beta-hydroxy-5-epiaristolochene 4-6times greater compared with that of wild type
S368C
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the mutant exhibits wild type catalytic efficiency for 1beta-hydroxy-5-epiaristolochene biosynthesis, but is devoid of the successive hydroxylation activity for capsidiol biosynthesis
S368F
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devoid of any hydroxylase activity for 5-epiaristolochene or 1beta-hydroxy-5-epiaristolochene
S368I
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devoid of any hydroxylase activity for 5-epiaristolochene or 1beta-hydroxy-5-epiaristolochene
S368T
-
the mutant retains its ability to fully convert 5-epiaristolochene to capsidiol, but the turnover rates for capsidiol formation is 3-13times lower compared with that of the wild type enzyme and is also able to convert 1beta-hydroxy-5-epiaristolochene to capsidiol with kcat values comparable with that of wild type enzyme, but with Km values for 1beta-hydroxy-5-epiaristolochene 4-6times greater compared with that of wild type
S368V
-
the mutant exhibits wild type catalytic efficiency for 1beta-hydroxy-5-epiaristolochene biosynthesis, but is devoid of the successive hydroxylation activity for capsidiol biosynthesis, the mutant catalyzes the relative equal biosynthesis of 1beta-hydroxy-5-epiaristolochene, 2beta-hydroxy-5-epiaristolochene, and 3beta-hydroxy-5-epiaristolochene from 5-epiaristolochene with wild type efficiency and converts about 1.5% of these monohydroxylated products to their respective ketone forms
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