EC Number | Cloned (Comment) | Organism |
---|---|---|
1.14.14.126 | gene CYP716A253, semi-quantitative and quantitative RT-PCR enzyme expressison analysis, phylogenetic analysis, recombinant expression in Saccharomyces cerevisiae strain BY4741 | Ocimum basilicum |
EC Number | Protein Variants | Comment | Organism |
---|---|---|---|
1.14.14.126 | additional information | virus-induced gene silencing (VIGS) in Ocimum basilicum, plasmids are individually transformed into Agrobacterium tumefaciens strain GV3101 by the freeze-thaw method | Ocimum basilicum |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.14.14.126 | beta-amyrin + 3 [reduced NADPH-hemoprotein reductase] + 3 O2 | Ocimum basilicum | overall reaction | oleanolate + 3 [oxidized NADPH-hemoprotein reductase] + 4 H2O | - |
? | |
1.14.14.126 | beta-amyrin + [reduced NADPH-hemoprotein reductase] + O2 | Ocimum basilicum | - |
erythrodiol + [oxidized NADPH-hemoprotein reductase] + H2O | - |
? | |
1.14.14.126 | erythrodiol + [reduced NADPH-hemoprotein reductase] + O2 | Ocimum basilicum | - |
oleanolic aldehyde + [oxidized NADPH-hemoprotein reductase] + 2 H2O | - |
? | |
1.14.14.126 | oleanolic aldehyde + [reduced NADPH-hemoprotein reductase] + O2 | Ocimum basilicum | - |
oleanolate + [oxidized NADPH-hemoprotein reductase] + H2O | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
1.14.14.126 | Ocimum basilicum | A0A161ABB0 | - |
- |
EC Number | Source Tissue | Comment | Organism | Textmining |
---|---|---|---|---|
1.14.14.126 | leaf | - |
Ocimum basilicum | - |
1.14.14.126 | additional information | spatiotemporal expression patterns of amyrin synthases and amyrin C-28 oxidases | Ocimum basilicum | - |
1.14.14.126 | seedling | - |
Ocimum basilicum | - |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.14.14.126 | beta-amyrin + 3 [reduced NADPH-hemoprotein reductase] + 3 O2 | overall reaction | Ocimum basilicum | oleanolate + 3 [oxidized NADPH-hemoprotein reductase] + 4 H2O | - |
? | |
1.14.14.126 | beta-amyrin + [reduced NADPH-hemoprotein reductase] + O2 | - |
Ocimum basilicum | erythrodiol + [oxidized NADPH-hemoprotein reductase] + H2O | - |
? | |
1.14.14.126 | erythrodiol + [reduced NADPH-hemoprotein reductase] + O2 | - |
Ocimum basilicum | oleanolic aldehyde + [oxidized NADPH-hemoprotein reductase] + 2 H2O | - |
? | |
1.14.14.126 | additional information | GC-MS metabolite identification | Ocimum basilicum | ? | - |
? | |
1.14.14.126 | oleanolic aldehyde + [reduced NADPH-hemoprotein reductase] + O2 | - |
Ocimum basilicum | oleanolate + [oxidized NADPH-hemoprotein reductase] + H2O | - |
? |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
1.14.14.126 | amyrin C-28 oxidase | - |
Ocimum basilicum |
1.14.14.126 | CYP716A253 | - |
Ocimum basilicum |
EC Number | Cofactor | Comment | Organism | Structure |
---|---|---|---|---|
1.14.14.126 | cytochrome P450 | - |
Ocimum basilicum | |
1.14.14.126 | heme | - |
Ocimum basilicum | |
1.14.14.126 | 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._ | Ocimum basilicum |
EC Number | Organism | Comment | Expression |
---|---|---|---|
1.14.14.126 | Ocimum basilicum | infection with Sclerotinia sclerotiorum and treatement with methyljasmonate and ACC induce the enzyme up to 6.8, 4.3 and 91fold | up |
EC Number | General Information | Comment | Organism |
---|---|---|---|
1.14.14.126 | metabolism | enzymes CYP716A252 and CYP716A253 catalyze sequential three-step oxidation at the C-28 position of alpha-amyrin and beta-amyrin to produce ursolic acid and oleanolic acid, respectively, essential roles for both of these CYP716As in constitutive biosynthesis of ursolic acid and oleanolic acid in sweet basil leaves, similar as well as distinct roles of CYP716A252 and CYP716A253 for the spatio-temporal biosynthesis of pentacyclic triterpenes. The cyclization of 2,3-oxidosqualene into either of two structural isomers, alpha-amyrin or beta-amyrin is the initial diversifying step for ursolic acid and oleanolic acid biosynthesis, pathway overview | Ocimum basilicum |
1.14.14.126 | additional information | enzyme CYP716A253 contains conserved amino acid motifs characteristic of bona fide CYP450s includig the highly conserved heme-binding motif FxxGxRxCxG at the C-terminal end, an EXXR.-.R motif (ERR triad) that maintains protein tertiary structure and positioning of the heme pocket, an A/GGXD/ET motif that participates in oxygen binding and activation, and a proline-rich and a hydrophobic regions at the N-terminal end | Ocimum basilicum |
1.14.14.126 | physiological function | the medicinal plant sweet basil (Ocimum basilicum) accumulates bioactive ursane- and oleanane-type pentacyclic triterpenes (PCTs), ursolic acid and oleanolic acid, respectively, in a spatio-temporal manner. Major role for CYP716A253 and a minor role for CYP716A252 in determining elicitor-induced biosynthesis of ursolic acid and oleanolic acid | Ocimum basilicum |