Secologanin synthase
| Secologanin synthase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 1.14.19.62 | ||||||||
| CAS no. | 258339-71-8 | ||||||||
| Databases | |||||||||
| BRENDA | enzyme data | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | enzyme entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| Rhea | reactions | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
| |||||||||
Secologanin synthase (EC 1.14.19.62, was wrongly classified as EC 1.3.3.9 in the past) is an enzyme that catalyzes the chemical reaction
The three substrates of this enzyme are loganin, reduced nicotinamide adenine dinucleotide phosphate (NADPH), and oxygen. Its products are secologanin, oxidised NADP+, and water.[1][2]
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with oxygen as acceptor. The systematic name of this enzyme class is loganin:oxygen oxidoreductase (ring-cleaving). It is a member of the cytochrome P450 protein superfamily and participates in indole and ipecac alkaloid biosynthesis.[3][4]
References
[edit]- ↑ Enzyme 1.14.19.62 at KEGG Pathway Database.
- ↑ Yamamoto H, Katano N, Ooi Y, Inoue K (1999). "Transformation of loganin and 7-deoxyloganin into secologanin by Lonicera japonica cell suspension cultures". Phytochemistry. 50 (3): 417–422. Bibcode:1999PChem..50..417Y. doi:10.1016/S0031-9422(98)00613-X.
- ↑ Yamamoto H, Katano N, Ooi A, Inoue K (2000). "Secologanin synthase which catalyzes the oxidative cleavage of loganin into secologanin is a cytochrome P450". Phytochemistry. 53 (1): 7–12. Bibcode:2000PChem..53....7Y. doi:10.1016/S0031-9422(99)00471-9. PMID 10656401.
- ↑ Strack D, Matern U, Schroder J (2000). "Indole alkaloid biosynthesis in Catharanthus roseus: new enzyme activities and identification of cytochrome P450 CYP72A1 as secologanin synthase". Plant J. 24 (6): 797–804. doi:10.1046/j.1365-313x.2000.00922.x (inactive 30 July 2025). PMID 11135113.
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