Information on EC 1.14.13.121 - premnaspirodiene oxygenase

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The expected taxonomic range for this enzyme is: Hyoscyamus muticus

EC NUMBER
COMMENTARY hide
1.14.13.121
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RECOMMENDED NAME
GeneOntology No.
premnaspirodiene oxygenase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
(-)-vetispiradiene + NADPH + H+ + O2 = solavetivol + NADP+ + H2O
show the reaction diagram
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solavetivol + NADPH + H+ + O2 = solavetivone + NADP+ + 2 H2O
show the reaction diagram
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydroxylation
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Biosynthesis of secondary metabolites
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Sesquiterpenoid and triterpenoid biosynthesis
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SYSTEMATIC NAME
IUBMB Comments
(-)-vetispiradiene,NADPH:oxygen 2alpha-oxidoreductase
A heme-thiolate protein (P-450). 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 derivative which is not further oxidized.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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UniProt
Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(-)-vetispiradiene + NADPH + H+ + O2
solavetivol + NADP+ + H2O
show the reaction diagram
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solavetivol is also named premnaspirodien-2alpha-ol or (2S,4R,5S,7R)-spirovetiva-1(10),11(12)-dien-2-ol
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?
5-epiaristolochene + NADPH + H+ + O2
2beta-hydroxy-epiaristolochene + 1beta-hydroxy-epiaristolochene + 3alpha-hydroxy-epiaristolochene + ? + NADP+ + H2O
show the reaction diagram
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%
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?
cedr-8-ene + NADPH + H+ + O2
cedr-8-en-15-ol + NADP+ + H2O
show the reaction diagram
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?
epiaristolochen-2beta-ol + NADPH + H+ + O2
2beta-hydroxy-epiaristolochene + NADP+ + H2O
show the reaction diagram
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?
epieremophilen-2beta-ol + NADPH + H+ + O2
2beta-hydroxy-epieremophilene + NADP+ + H2O
show the reaction diagram
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?
valencene + NADPH + H+ + O2
alpha-nootkatol + beta-nootkatol + NADP+ + H2O
show the reaction diagram
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?
additional information
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
additional information
?
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A6YIH8
HPO also catalyzes the equivalent regio-specific (C-2) hydroxylation of several eremophilane-type (decalin ring system) sesquiterpenes, such as with 5-epi-aristolochene
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0062 - 0.014
(-)-vetispiradiene
0.0025 - 0.0179
5-epiaristolochene
0.0069 - 0.0192
valencene
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2.1 - 20.7
(-)-vetispiradiene
0.2 - 2.8
5-epiaristolochene
1.9 - 15.9
valencene
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
150 - 1590
(-)-vetispiradiene
7905
60 - 650
5-epiaristolochene
2922
260 - 1310
valencene
8911
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in WAT11 yeast strain
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
A484I
the mutation results in a catalytically compromised enzyme
V366S
the mutation dramatically reduces overall enzyme activity
V480I/A484I
mutant with improved catalytic efficiency
V480S
the mutation improves the kcat for the conversion of (-)-vetispiradiene to solavetivol about 2fold
V482I
mutant with improved catalytic efficiency; the mutation improves the kcat for the conversion of (-)-vetispiradiene to solavetivol about 2fold
V482I/A484I
the mutant possesses a 5fold improvement in its catalytic efficiency for nootkatol biosynthesis and a 10fold improvement for 2beta-hydroxy-epiaristolochene biosynthesis