1.14.14.83: geraniol 8-hydroxylase
This is an abbreviated version!
For detailed information about geraniol 8-hydroxylase, go to the full flat file.
Word Map on EC 1.14.14.83
-
1.14.14.83
-
roseus
-
catharanthus
-
indole
-
monoterpenoids
-
iridoids
-
strictosidine
-
ajmalicine
-
nadph-cytochrome
-
vinblastine
-
terpenoid
-
co-overexpression
-
periwinkle
-
vincristine
-
croton
-
acuminata
-
synthesis
-
methyljasmonate
-
vinca
-
camptotheca
-
drug development
-
pharmacology
- 1.14.14.83
- roseus
-
catharanthus
- indole
-
monoterpenoids
-
iridoids
- strictosidine
- ajmalicine
-
nadph-cytochrome
- vinblastine
-
terpenoid
-
co-overexpression
- periwinkle
- vincristine
-
croton
- acuminata
- synthesis
-
methyljasmonate
- vinca
-
camptotheca
- drug development
- pharmacology
Reaction
Synonyms
10-hydroxygeraniol oxidoreductase, CPR I, Cr10HGO, CYP76B10, CYP76B6, CYP76B6 protein, CYP76F45, EC 1.14.13.152, G10H, G8H, geraniol 10-hydroxylase, geraniol-10-hydroxylase, monoterpene hydroxylase, PgCYP76C9, PgG10H
ECTree
Advanced search results
General Information
General Information on EC 1.14.14.83 - geraniol 8-hydroxylase
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
evolution
metabolism
physiological function
additional information
-
the enzyme belongs to the cytochrome-P450 monooxygenase family
evolution
the enzyme belongs to the cytochrome-P450 monooxygenase family
evolution
-
the enzyme is a cyt P450 monoterpene hydroxylase and belongs to the cytochrome-P450 monooxygenase family
evolution
-
the enzyme is a cyt P450 monoterpene hydroxylase and belongs to the cytochrome-P450 monooxygenase family
evolution
enzyme CsCPR I belongs to Class I of dicotyledonous CPRs
evolution
enzyme CYP76F45 belongs to the CYP76 family of dicotyledonous CPR class I
evolution
-
enzyme CYP76F45 belongs to the CYP76 family of dicotyledonous CPR class I
-
-
G10H catalyses an early step of the biosynthesis of the monoterpene precursor of monoterpene indole alkaloids
metabolism
G10H catalyzes the first committed step of the biosynthetic pathway of strictosidine and other terpenoid indole alkaloids, overview
metabolism
G10H plays a role in the iridoid monoterpene and indole alkaloid biosynthesis
metabolism
-
the enzyme is involved in the monoterpene indole alkaloids, regulation of the enzyme activity involves two distinct calmodulin isoforms, CAM1 and CAM2, overview
metabolism
-
the enzyme is one of the key enzymes of the biosynthesis of monoterpene indole alkaloids that originate from the coupling of the indole and the iridoid pathways. Overview of metabolic pathways leading to the biosynthesis of monoterpene indole alkaloids and their metabolic regulation
metabolism
the enzyme plays an important role in the iridoid monoterpenoid and the indole alkaloid biosynthesis, overview
metabolism
the enzyme is catalyzing the first commited step to iridoid monoterpene biosynthesis and is involved in monoterpene indole alkaloid biosynthesis in specialized cells of the laticifer-idioblast system, overview
metabolism
-
the enzyme is involved in the 2-C-methyl-D-erythritol-4-phosphate/terpenoid metabolic pathway part of the iridoid pathway, overview. Induction of G10H is a requirement, but not the only, necessary to produce other terpenoid indole alkaloids than strictosidine
metabolism
-
the enzyme is involved in the biosynthesis of iridiod monoterpenoids
metabolism
-
the enzyme is involved in the biosynthesis of iridiod monoterpenoids
metabolism
the enzyme is involved in the biosynthesis of secologanin from geraniol, overview
metabolism
the enzyme is involved in biosynthesis of terpenoid indole alkaloids
metabolism
the enzyme is involved in terpenoid indole alkaloid (TIA) biosynthetic pathway
metabolism
the enzyme catalyzes the first committed step in the camptothecin biosynthetic pathway and a key regulation point of the campothecin biosynthetic pathway
metabolism
-
the enzyme is involved in the secoiridoid pathway and the biosynthesis of terpenoid indole alkaloid via strictosidine
physiological function
G10H hydroxylates geraniol and is involved in biosynthesis of swertiamarin via the iridoid pathway and of strictosidine via the indole pathway, overview, induced by methyljasmonate
physiological function
-
geraniol 10-hydroxylase is a cytochrome P450 monooxygenase involved in the biosynthesis of iridoid monoterpenoids and several classes of monoterpenoid alkaloids found in a diverse range of plant species. G10H plays a key regulatory role in terpenoid indole alkaloid biosynthesis
physiological function
-
the cytochrome P450 enzyme geraniol 10-hydroxylase plays an important role in the biosynthesis of pharmaceutically important alkaloids in Catharanthus roseus
physiological function
the enzyme is catalyzing the first commited step to iridoid monoterpene biosynthesis and is involved in monoterpene indole alkaloid biosynthesis in specialized cells of the laticifer-idioblast system, overview
physiological function
-
the enzyme is involved in the biosynthesis of iridiod monoterpenoids, which are important in plant defense systems against herbivores
physiological function
-
the enzyme is involved in the biosynthesis of iridiod monoterpenoids, which are important in plant defense systems against herbivores
physiological function
enzymes CYP97C27 and CPR I function as the enzyme geraniol-8-hydroxylase (G8H), which is likely to be involved in the biosynthesis of the indole alkaloid 19-E-vallesamine in Croton stellatopilosus
physiological function
overexpression of G10H alone or coexpression G10H with octadecanoid-derivative responsive Catharanthus AP2-domain gene ORCA3 in transgenic Catharanthus roseus plants. G10H transcripts show a significant increase under G10H and ORCA3 cooverexpression. ORCA3 and G10H overexpression significantly increase the accumulation of strictosidine, vindoline, catharanthine and ajmalicine but have limited effects on anhydrovinblastine and vinblastine levels
physiological function
the enzyme plays an important role in stimulating campothecin accumulation, capothecin has anti-tumor activity
physiological function
transient expression in Nicotiana benthamiana leaf leads to formation of 8-hydroxygeraniol and 8-oxogeraniol
physiological function
-
downregulation of CYP76B6 results in reduction of mRNA transcript levels as well as camptothecin content in comparison to control. Overexpression of CYP76B6 in leaf leads to significantly higher content of camptothecin
physiological function
-
enzymes CYP97C27 and CPR I function as the enzyme geraniol-8-hydroxylase (G8H), which is likely to be involved in the biosynthesis of the indole alkaloid 19-E-vallesamine in Croton stellatopilosus
-
-
geraniol 10-hydroxylase is a cytochrome P450 monooxygenase
additional information
-
geraniol 10-hydroxylase is a cytochrome P450 monooxygenase
additional information
geraniol 10-hydroxylase is a cytochrome P450 monooxygenase
additional information
-
geraniol 10-hydroxylase is a cytochrome P450 monooxygenase
additional information
-
geraniol 10-hydroxylase is a cytochrome P450 monooxygenase. It consists of a reductase and a monooxygenase. The cytochrome P450 reductase, EC 1.6.2.4, is a membrane-bound flavoprotein, which transfers electrons from NADPH to the cytochrome P450 monooxygenase, CPR requires the cofactors FMN, FAD and NADPH
additional information
-
the calmodulins CAM1 and CAM2 are required for monoterpene indole alkaloid biosynthesis in Catharanthus roseus cells by acting on regulation of expression of genes encoding enzymes that catalyse early steps of monoterpene indole alkaloid biosynthesis, such as 1-deoxy-D-xylulose 5-phosphate reductoisomerase and geraniol 10-hydroxylase, overview. CAM regulation by Ca2+, overview
additional information
-
the individual overexpression of the terpenoid genes 1-deoxy-D-xylulose synthase, DXS, and G10H resulted in mixed results in regards to the accumulation of terpenoid indole alkaloid metabolite pools
additional information
-
the transcription level of gene g10h is altered by treatment with Agrobacterium tumefaciens for induction of hariry root growth in second metabolite production, expression analysis, overview
additional information
-
molecular docking is used for accurate prediction of protein-ligand interaction geometries at molecular level, molecular interaction studies, overview. Geraniol interacts with G10H residues Ala303 and Thr307 from the central helix I
additional information
the enzyme contains specific oxygen- and heme-binding sites
additional information
the enzyme contains specific oxygen- and heme-binding sites
additional information
-
the enzyme contains specific oxygen- and heme-binding sites
additional information
the enzyme contains two FMN-, FAD-, and NADPH-binding sites and one P450-binding site
additional information
the enzyme contains two FMN-, FAD-, and NADPH-binding sites and one P450-binding site
additional information
-
the enzyme contains two FMN-, FAD-, and NADPH-binding sites and one P450-binding site
additional information
-
the enzyme contains specific oxygen- and heme-binding sites
-