Function
The enzyme strictosidine synthase (STR1) (EC 4.3.3.2) from an Indian medicinal plant Rauvolfia serpentina is of primary importance for the biosynthetic pathway of the indole alkaloid ajmaline. STR1 initiates all biosynthetic pathways leading to the entire monoterpenoid indole alkaloid family representing an enormous structural variety of ~2000 compounds in higher plants. The enzyme is involved in the biosynthesis of all these alkaloids by catalyzing the condensation of the two initial building blocks, tryptamine and the monoterpenoid secologanin, leading to the glucoalkaloid strictosidine. The reaction type catalyzed by STR1 is so far an exceptional example in the biosynthesis of natural products. It was hitherto known only from synthetic chemistry (Pictet-Spengler–type reaction), where it is applied in alkaloid synthesis, especially of tetrahydroisoquinolines by condensation of an amine and an aldehyde under acidic conditions[1].
The overall structure of the enzyme contains a six-bladed four-stranded ß-propeller fold. All six blades are radially arranged around a pseudo six-fold symmetry axis. Each blade contains a twisted four-stranded antiparallel ß-sheet.
Structural highlights
The substrate binding pocket of STR1 is located near the pseudo six-fold symmetry axis[2]. Alpha Helices,
Beta Strands ,
Loops ,
Turns. Active site. Water molecule are shown as red sphere.
- ↑ Stockigt J, Barleben L, Panjikar S, Loris EA. 3D-Structure and function of strictosidine synthase--the key enzyme of monoterpenoid indole alkaloid biosynthesis. Plant Physiol Biochem. 2008 Mar;46(3):340-55. doi: 10.1016/j.plaphy.2007.12.011. , Epub 2008 Jan 3. PMID:18280746 doi:https://dx.doi.org/10.1016/j.plaphy.2007.12.011
- ↑ Ma X, Panjikar S, Koepke J, Loris E, Stockigt J. The structure of Rauvolfia serpentina strictosidine synthase is a novel six-bladed beta-propeller fold in plant proteins. Plant Cell. 2006 Apr;18(4):907-20. Epub 2006 Mar 10. PMID:16531499 doi:10.1105/tpc.105.038018
