EC Number   |
General Information |
Reference |
|---|
   1.14.19.62 | malfunction |
mutant DELTAthSLS fusion protein forms punctuated aggregates in the cytosol in close vicinity with plastids |
724967 |
| 1.14.19.62 | metabolism |
the enzyme catalyzes the last step of the monoterpene secoiridoid pathway |
724967 |
| 1.14.19.62 | metabolism |
the enzyme is important in the monoterpenoid indole alkaloid (MIA) biosynthesis in Catharanthus roseus, subcellular organization of the central steps of the pathway, overview. The ring-opening reaction of loganin in the biosynthesis of secologanin is catalyzed by the fourth P450 of this pathway, secologanin synthase (SLS, CYP72A1). Both isozymes SLS1 and SLS2 not only catalyze the oxidative ring cleavage of loganin to produce secologanin but also perform the oxidation of secologanin into secoxyloganin. SLS1 and SLS2 constitute the third type of P450 from the seco-iridoid pathway performing more than one catalytic reaction. Additional enzymes might convert secoxyloganin back to secologanin, the subcellular compartmentation of secologanin biosynthesis may also limit secoxyloganin formation in planta. Secoxyloganin is an acidic compound derived from secologanin that is no longer able to be condensed with tryptamine by STR in the vacuole, due to the absence of the aldehyde function. If secoxyloganin formation occurs in vivo, the resulting depletion of the secologanin pool is deleterious for the subsequent synthesis of MIAs |
744599 |
| 1.14.19.62 | more |
consensus transcriptome analysis of Catharanthus roseus, detailed overview |
744599 |
| 1.14.19.62 | more |
the enzyme is anchored to the endoplasmic reticulum via a N-teminal helix, thus allowing the production of secologanin on the cytosolic side of the endoplasmic reticulum membrane |
724967 |
| 1.14.19.62 | physiological function |
secologanin synthases (SLS) are P450 enzymes that catalyze an unusual ring-opening reaction of loganin in the biosynthesis of the monoterpenoid indole alkaloids (MIA) precursor secologanin |
744599 |
