4.2.1.125: dammarenediol II synthase
This is an abbreviated version!
For detailed information about dammarenediol II synthase, go to the full flat file.
Word Map on EC 4.2.1.125
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4.2.1.125
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panax
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ginsenosides
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ginseng
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saponin
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epoxidase
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protopanaxadiol
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triterpene
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jasmonate
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triterpenoid
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2,3-oxidosqualene
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adventitious
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tetracyclic
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aglycone
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dammarane-type
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notoginseng
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oxidosqualene
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elicitors
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nadph-cytochrome
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quinquefolius
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meyer
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beta-amyrin
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sapogenins
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lanosterol
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udp-glycosyltransferase
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cycloartenol
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chromatography-atmospheric
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synthesis
- 4.2.1.125
- panax
- ginsenosides
- ginseng
- saponin
-
epoxidase
- protopanaxadiol
-
triterpene
- jasmonate
-
triterpenoid
- 2,3-oxidosqualene
-
adventitious
-
tetracyclic
-
aglycone
-
dammarane-type
- notoginseng
- oxidosqualene
- elicitors
-
nadph-cytochrome
- quinquefolius
-
meyer
- beta-amyrin
-
sapogenins
- lanosterol
- udp-glycosyltransferase
- cycloartenol
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chromatography-atmospheric
- synthesis
Reaction
Synonyms
dammarenediol synthase, dammarenediol-II synthase, DDS, PgDDS, PgDDS1, PNA
ECTree
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General Information
General Information on EC 4.2.1.125 - dammarenediol II synthase
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metabolism
physiological function
additional information
the enzyme catalyzes the first step in biosynthetic pathway of ginsenosides, overview
metabolism
the enzyme catalyzes the first step in the biosynthetic pathway for ginsenosides in Panax ginseng, overview
metabolism
the enzyme catalyzes the first step in the synthesis of dammarane-type ginsenoside, the cyclization of 2,3-oxidosqualene to dammarenediol-II, overview
metabolism
the enzyme is involved in the ginsenoside biosynthetic pathway catalyzing the first committed step, the cyclization of 2,3-oxidosqualene to dammarenediol
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Centella asiatica hairy roots overexpressing ginseng farnesyl diphosphate synthase show higher levels of dammarenediol synthase and cycloartenol synthase mRNA when compared with the controls. No differences are detected in expression of the squalene synthase gene. The upregulation of dammarenediol synthase transcripts suggests that FPS may result in alterations in triterpene biosynthesis capacity. Squalene contents in the T17, T24, and T27 lines increase to 1.1-, 1.3- and 1.5fold those in the controls, respectively. The total sterol contents in the T24 line are approximately three times higher than those of the controls
physiological function
dammarenediol-II synthase catalyzes the cyclization of 2,3-oxidosqualene to dammarenediol-II, which is the basic triterpene skeleton in dammarene-type saponin (ginsenosides) in Panax ginseng. Dammarenediol-II is present in the roots of Panax ginseng in trace amounts because it is an intermediate product in triterpene biosynthesis
physiological function
dammarenediol synthase is a key enzyme in the biosynthetic process of ginsenosides
physiological function
dammarenediol-II synthase gene (PgDDS) from Panax ginseng is responsible for the cyclization of 2,3-oxidosqualene to dammarenediol-II, the nucleus of dammarane-type ginsenosides, which are a group of active triterpenoids exhibiting various pharmacological activities
close correlation of dammarenediol synthetase and saponin production in vitro
additional information
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close correlation of dammarenediol synthetase and saponin production in vitro
additional information
determination of ginsenosides, i.e. Rg1, Re, F11, Rf, S-Rh1, Rg2, Rb1, R-Rh1, Rc, F1, R0, Rb2, Rb3, Rd, F2, S-Rg3, R1, and R-Rg3, in Panax ginseng cv. DAMAYA. The ginsenoside contents, of such as Rf, Rg1 and F1, change with the gene mutation
additional information
three-dimensional structure and catalytic active sites structures of dammarenediol-II synthase by homology modeling using human oxidosqualene cyclase 3D models (PDB IDs 1W6K and 1W6J) as templates and by molecular docking simulation between enzyme model and product dammarenediol-II, overview. Residues C568 and C264 play significant roles in the catalytic process of the enzyme. Active site residues are identified: Asp488 initiates the ring forming reaction by protonating the 2,3-oxirane ring, and is activated by strong polar amino acid Cys489 and Cys568. Aromatic residues Trp421, Phe477, Trp538, Tyr263 and Tyr732 may stabilize the intermediate conformation during the cyclization. Cys264, Tyr268 and Ile559 may have relation with a substrate channel that guides 2,3-oxidosqualene into the active site cavity