IUBMB Enzyme Nomenclature

EC 3.5.99.13

Accepted name: strictosidine synthase

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

For diagram of reaction click here

Other name(s): strictosidine synthetase; STR; 3-α(S)-strictosidine tryptamine-lyase; 3-α(S)-strictosidine tryptamine-lyase (secologanin-forming)

Systematic name: 3-α(S)-strictosidine tryptamine-hydrolase (secologanin-forming)

Comments: Catalyses a Pictet-Spengler reaction between the aldehyde group of secologanin and the amino group of tryptamine [4,5]. Involved in the biosynthesis of the monoterpenoid indole alkaloids.

Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:

References:

1. Treimer, J.K. and Zenk, M.H. Purification and properties of strictosidine synthase, the key enzyme in indole alkaloid formation. Eur. J. Biochem. 101 (1979) 225-233. [PMID: 510306]

2. Kutchan, T.M. Strictosidine: from alkaloid to enzyme to gene. Phytochemistry 32 (1993) 493-506. [PMID: 7763429]

3. de Waal, A., Meijer, A.H. and Verpoorte, R. Strictosidine synthase from Catharanthus roseus: purification and characterization of multiple forms. Biochem. J. 306 (1995) 571-580. [PMID: 7887913]

4. Ruppert, M., Woll, J., Giritch, A., Genady, E., Ma, X. and Stöckigt, J. Functional expression of an ajmaline pathway-specific esterase from Rauvolfia in a novel plant-virus expression system. Planta 222 (2005) 888-898. [PMID: 16133216]

5. McCoy, E., Galan, M.C. and O'Connor, S.E. Substrate specificity of strictosidine synthase. Bioorg. Med. Chem. Lett. 16 (2006) 2475-2478. [PMID: 16481164]

6. Ma, X., Panjikar, S., Koepke, J., Loris, E. and Stöckigt, J. The structure of Rauvolfia serpentina strictosidine synthase is a novel six-bladed β-propeller fold in plant proteins. Plant Cell 18 (2006) 907-920. [PMID: 16531499]

[EC 3.5.99.13 created 1990 as EC 4.3.3.2, transferred 2024 to EC 3.5.99.13]


Return to EC 3.5.99 home page
Return to EC 3.5 home page
Return to EC 3 home page
Return to Enzymes home page
Return to IUBMB Biochemical Nomenclature home page