Strictosidine synthase

strictosidine synthase
Identifiers
EC no.4.3.3.2
CAS no.69669-72-3
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO
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PubMedarticles
NCBIproteins

Strictosidine synthase (EC 4.3.3.2) is an enzyme in alkaloid biosynthesis that catalyses the condensation of tryptamine with secologanin to form strictosidine in a formal Pictet–Spengler reaction:

3-α(S)-strictosidine + H2O = tryptamine + secologanin

Since the condensation of tryptamine and secologanin is the first committed step in alkaloid synthesis, strictosidine synthase plays a fundamental role for the great majority of the indole-alkaloid pathways.

This enzyme belongs to the family of lyases, specifically amine lyases, which cleave carbon-nitrogen bonds. It can be isolated from several alkaloid-producing plants from the family Apocynaceae (e.g. Catharanthus roseus, Voacanga africana). The systematic name of this enzyme class is 3-α(S)-strictosidine tryptamine-lyase (secologanin-forming). Other names in common use include strictosidine synthetase, STR, and 3-α(S)-strictosidine tryptamine-lyase. Originally isolated from the plant Rauvolfia serpentina, a medicinal plant widely used in Indian folk medicine, this enzyme participates in terpenoid biosynthesis and indole and ipecac alkaloid biosynthesis, both of which produce many compounds with significant physiological and medicinal properties.