Information on EC 1.14.13.121 - premnaspirodiene oxygenase

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The enzyme appears in viruses and cellular organisms

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EC NUMBER
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1.14.13.121
transferred to EC 1.14.14.151
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RECOMMENDED NAME
GeneOntology No.
premnaspirodiene oxygenase
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Sesquiterpenoid and triterpenoid biosynthesis
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Biosynthesis of secondary metabolites
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ORGANISM
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LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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UniProt
Manually annotated by BRENDA team
cv. Jinbaek
KY366226
GenBank
Manually annotated by BRENDA team
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
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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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(+)-valencene + NADPH + H+ + O2
alpha-nootkatol + beta-nootkatol + NADP+ + H2O
show the reaction diagram
additional information
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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
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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
(+)-valencene + NADPH + H+ + O2
alpha-nootkatol + beta-nootkatol + NADP+ + H2O
show the reaction diagram
A6YIH8
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additional information
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A6YIH8
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
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COFACTOR
ORGANISM
UNIPROT
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LITERATURE
IMAGE
cytochrome P450
KY366226
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SOURCE TISSUE
ORGANISM
UNIPROT
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LITERATURE
SOURCE
KY366226
young leaves
Manually annotated by BRENDA team
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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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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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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LINKS TO OTHER DATABASES (specific for EC-Number 1.14.13.121)
ExplorEnz
ExPASy
KEGG
MetaCyc
SABIO-RK
NCBI: PubMed, Protein, Nucleotide, Structure, Genome, OMIM
IUBMB Enzyme Nomenclature
PROSITE Database of protein families and domains
InterPro (database of protein families, domains and functional sites)