Information on EC 1.14.13.183 - dammarenediol 12-hydroxylase

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The expected taxonomic range for this enzyme is: Panax

EC NUMBER
COMMENTARY hide
1.14.13.183
transferred to EC 1.14.14.120
RECOMMENDED NAME
GeneOntology No.
dammarenediol 12-hydroxylase
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
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UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
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the enzyme is part of the biosynthetic pathway for ginsenoside production in Panax ginseng, overview
physiological function
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protopanaxadiol (PPD) is an aglycone of dammarene-type ginsenoside and has a wide range of pharmacological activities and high medicinal values. It is synthesized via the hydroxylation of dammarenediol-II (DD) by CYP716A47 enzyme
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
dammarenediol-II + NADPH + H+ + O2
protopanaxadiol + NADP+ + H2O
show the reaction diagram
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
dammarenediol-II + NADPH + H+ + O2
protopanaxadiol + NADP+ + H2O
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
cytochrome P450
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NADPH
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.4
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assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30
-
assay at
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
the enzyme contains a transmembrane domain
Manually annotated by BRENDA team
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
gene CYP716A47, recombinant expression under control of 35S CaMV promoter in leaves of tobacco via Agrobacterium tumefaciens GV3101 transformation method, RT-PCR expression analysis
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gene PqD12H, expression of PqD12H in Saccharmoyces cerevisiae strain WAT21 from plasmid pAUR123-PqD12H, RT-PCR enzyme expression analysis, recombinant coexpression with dammarenediol synthase DS leads to increased accumulation of ginsenosides, i.e. protopanaxatriol protopanaxadiol. compared to control, both PqDS and PqD12H have higher accumulation of mRNA in the transgenic hairy roots and the increase ratio decreased slightly over culture time. Yeast with single recombinant vector pAUR123-PqD12H is unable to express protopanaxadiol without exogenous dammarenediol-II
recombinant expression of wild-type and mutant fusion proteins in Saccharomyces cerevisiae strain W303-1a. coexpression of wild-type enzyme with dammarenediol-II synthase from Panax ginseng and a Arabidopsis thaliana NADPH-cytochrome P450 reductase (ATR1). The low metabolic flux through PPDS results in a low productivity of protopanaxadiol, but is increased with the fusion enzymes
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
auxin treatment, particularly 2,4-dichlorophenoxyacetic acid, strongly enhances the transcription of the HMG-Co reductase (HMGR) and squalene epoxidase genes and thus the production of dammarenediol-II and protopanaxadiol (PPD)
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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to increase the low metabolic flux through PPDS and increase the productivity of protopanaxadiol production, enzyme PPDS is modified through transmembrane domain truncation and construction of self-sufficient PPDS-ATR1 fusion proteins. The fusion enzymes exhibit approximately 4.5fold increase in catalytic activity and 71.1% increase in protopanaxadiol production compared with PPDS and ATR1 co-expression. The engineered yeast carrying fusion protein effectively converts 96.8% of dammarenediol-II into protopanaxadiol, bioreactor in fed-batch fermentation. Construction of four fusion proteins named as PPDS-linker1-46tATR1, PPDSlinker2-46tATR1, PPDS-linker3-46tATR1, and PPDS-nolinker-46tATR1, respectively. In addition, 31tPPDS heme domain and 46tATR1 reductase domain are linked by polypeptide GSTSSGSG. Method optimization, overview. Evaluation of the oxidative stress in yeast cells induced by co-expression of PPDS and ATR1