Strictosidine synthase

In enzymology, a strictosidine synthase is an enzyme that catalyzes the chemical reaction


 * 3-alpha(S)-strictosidine + H2O $$\rightleftharpoons$$ tryptamine + secologanin

Thus, the two substrates of this enzyme are 3-alpha(S)-strictosidine and H2O, whereas its two products are tryptamine and secologanin.

This enzyme belongs to the family of lyases, specifically amine lyases, which cleave carbon-nitrogen bonds. The systematic name of this enzyme class is 3-alpha(S)-strictosidine tryptamine-lyase (secologanin-forming). Other names in common use include strictosidine synthetase, STR, and 3-alpha(S)-strictosidine tryptamine-lyase. This enzyme participates in terpenoid biosynthesis and indole and ipecac alkaloid biosynthesis.

Structural studies
As of late 2007, 4 structures have been solved for this class of enzymes, with PDB accession codes, , , and.