Any feedback?
Please rate this page
(enzyme.php)
(0/150)

BRENDA support

BRENDA Home
show all | hide all No of entries

Information on EC 1.14.14.151 - premnaspirodiene oxygenase and Organism(s) Hyoscyamus muticus and UniProt Accession A6YIH8

for references in articles please use BRENDA:EC1.14.14.151
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
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 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.
Specify your search results
Select one or more organisms in this record: ?
This record set is specific for:
Hyoscyamus muticus
UNIPROT: A6YIH8
Show additional data
Do not include text mining results
Include (text mining) results
Include results (AMENDA + additional results, but less precise)
Word Map
hide
The taxonomic range for the selected organisms is: Hyoscyamus muticus
The enzyme appears in selected viruses and cellular organisms
Synonyms
premnaspirodiene oxygenase, cyp71d55, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
CYP71D55
gene name, UniProt
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydroxylation
-
SYSTEMATIC NAME
IUBMB Comments
(–)-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.
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(+)-valencene + [reduced NADPH-hemoprotein reductase] + O2
alpha-nootkatol + beta-nootkatol + [oxidized NADPH-hemoprotein reductase] + H2O
show the reaction diagram
enzyme HPO-mediated biohydroxylation of (+)-valencene
-
-
?
(-)-vetispiradiene + [reduced NADPH-hemoprotein reductase] + O2
solavetivol + [oxidized NADPH-hemoprotein reductase] + H2O
show the reaction diagram
-
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
show the reaction diagram
-
-
-
?
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
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%
-
-
?
cedr-8-ene + [reduced NADPH-hemoprotein reductase] + O2
cedr-8-en-15-ol + [oxidized NADPH-hemoprotein reductase] + H2O
show the reaction diagram
-
-
-
?
valencene + 2 [reduced NADPH-hemoprotein reductase] + 2 O2
alpha-nootkatol + beta-nootkatol + 2 [oxidized NADPH-hemoprotein reductase] + 2 H2O
show the reaction diagram
-
-
-
?
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
(+)-valencene + [reduced NADPH-hemoprotein reductase] + O2
alpha-nootkatol + beta-nootkatol + [oxidized NADPH-hemoprotein reductase] + H2O
show the reaction diagram
enzyme HPO-mediated biohydroxylation of (+)-valencene
-
-
?
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
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._
-
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
60 - 650
5-epiaristolochene
260 - 1310
valencene
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
C7D55_HYOMU
502
0
56788
Swiss-Prot
Secretory Pathway (Reliability: 3)
PROTEIN VARIANTS
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
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
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
expressed in WAT11 yeast strain
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team