Perakine reductase (EC 1.1.1.317) is an enzyme with systematic name raucaffrinoline:NADP+ oxidoreductase.[1][2] This enzyme catalyses the following chemical reaction
| Perakine reductase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 1.1.1.317 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
- raucaffrinoline + NADP+ perakine + NADPH + H+
The biosynthesis of raucaffrinoline from perakine is a side route of the ajmaline biosynthesis pathway.
References
edit- ^ Sun L, Ruppert M, Sheludko Y, Warzecha H, Zhao Y, Stöckigt J (July 2008). "Purification, cloning, functional expression and characterization of perakine reductase: the first example from the AKR enzyme family, extending the alkaloidal network of the plant Rauvolfia". Plant Molecular Biology. 67 (5): 455–67. doi:10.1007/s11103-008-9331-7. PMID 18409028.
- ^ Rosenthal C, Mueller U, Panjikar S, Sun L, Ruppert M, Zhao Y, Stöckigt J (December 2006). "Expression, purification, crystallization and preliminary X-ray analysis of perakine reductase, a new member of the aldo-keto reductase enzyme superfamily from higher plants". Acta Crystallographica Section F. 62 (Pt 12): 1286–9. doi:10.1107/S174430910605041X. PMC 2225361. PMID 17142919.
External links
edit- Perakine+reductase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
