Strictosidine synthase

strictosidine synthase
Identifiers
EC number	4.3.3.2
CAS number	69669-72-3
Databases
IntEnz	IntEnz view
BRENDA	BRENDA entry
ExPASy	NiceZyme view
KEGG	KEGG entry
MetaCyc	metabolic pathway
PRIAM	profile
PDB structures	RCSB PDB PDBe PDBsum
Gene Ontology	AmiGO / EGO
Search PMC articles PubMed articles

Strictosidine synthase (EC 4.3.3.2) a key enzyme in alkaloid biosynthesis. It catalyses the condensation of tryptamine with secologanin to form strictosidine:

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 2FP8, 2FP9, 2FPB, and 2FPC.

References

• Treimer JF, Zenk MH (1979). "Purification and properties of strictosidine synthase, the key enzyme in indole alkaloid formation". Eur. J. Biochem. 101 (1): 225–233. doi:10.1111/j.1432-1033.1979.tb04235.x. PMID 510306. 
• Kutchan TM (1993). "Strictosidine: from alkaloid to enzyme to gene". Phytochemistry. 32 (3): 493–506. doi:10.1016/S0031-9422(00)95128-8. PMID 7763429. 
• de Waal A, Meijer AH, Verpoorte R (Pt 2). "Strictosidine synthase from Catharanthus roseus: purification and characterization of multiple forms". Biochem. J. 306: 571–80. PMC 1136556. PMID 7887913. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1136556. 
• Ruppert M, Woll J, Giritch A, Genady E, Ma X, Stockigt J (2005). "Functional expression of an ajmaline pathway-specific esterase from Rauvolfia in a novel plant-virus expression system". Planta. 222 (5): 888–898. doi:10.1007/s00425-005-0031-0. PMID 16133216. 
• McCoy E, Galan MC, O'Connor SE (2006). "Substrate specificity of strictosidine synthase". Bioorg. Med. Chem. Lett. 16 (9): 2475–2478. doi:10.1016/j.bmcl.2006.01.098. PMID 16481164. 
• Ma X, Panjikar S, Koepke J, Loris E, Stockigt J (2006). "The structure of Rauvolfia serpentina strictosidine synthase is a novel six-bladed beta-propeller fold in plant proteins". Plant. Cell. 18 (4): 907–920. doi:10.1105/tpc.105.038018. PMC 1425862. PMID 16531499. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1425862.