| Title : Structural basis and enzymatic mechanism of the biosynthesis of C9- from C10-monoterpenoid indole alkaloids - Yang_2009_Angew.Chem.Int.Ed.Engl_48_5211 |
| Author(s) : Yang L , Hill M , Wang M , Panjikar S , Stockigt J |
| Ref : Angew Chem Int Ed Engl , 48 :5211 , 2009 |
|
Abstract :
Cutting carbons: The three-dimensional structure of polyneuridine aldehyde esterase (PNAE) gives insight into the enzymatic mechanism of the biosynthesis of C(9)- from C(10)-monoterpenoid indole alkaloids (see scheme). PNAE is a very substrate-specific serine esterase. It harbors the catalytic triad S87-D216-H244, and is a new member of the alpha/beta-fold hydrolase superfamily. Its novel function leads to the diversification of alkaloid structures. |
| PubMedSearch : Yang_2009_Angew.Chem.Int.Ed.Engl_48_5211 |
| PubMedID: 19496101 |
| Gene_locus related to this paper: rause-pnae |
| Inhibitor | 16-epi-Vellosimine |
| Substrate | Polyneuridine-aldehyde |
| Gene_locus | rause-pnae |
| Structure | 3GZJ 2WFL 2WFM |
Yang L, Hill M, Wang M, Panjikar S, Stockigt J (2009)
Structural basis and enzymatic mechanism of the biosynthesis of C9- from C10-monoterpenoid indole alkaloids
Angew Chem Int Ed Engl
48 :5211
Yang L, Hill M, Wang M, Panjikar S, Stockigt J (2009)
Angew Chem Int Ed Engl
48 :5211