Psoralen synthase
| Psoralen synthase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 1.14.13.102 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
In enzymology, a psoralen synthase (EC 1.14.13.102) is an enzyme that catalyzes the chemical reaction
- (+)-marmesin + NADPH + H+ + O2 psoralen + NADP+ + acetone + 2 H2O
The 4 substrates of this enzyme are (+)-marmesin, NADPH, H+, and O2, whereas its 4 products are psoralen, NADP+, acetone, and H2O.
This enzyme belongs to the family of oxidoreductases, specifically those acting on paired donors, with O2 as oxidant and incorporation or reduction of oxygen. The oxygen incorporated need not be derived from O2 with NADH or NADPH as one donor, and incorporation of one atom o oxygen into the other donor. The systematic name of this enzyme class is (?). This enzyme is also called CYP71AJ1.
References[edit]
- Larbat R, Kellner S, Specker S, Hehn A, Gontier E, Hans J, Bourgaud F, Matern U (January 2007). "Molecular cloning and functional characterization of psoralen synthase, the first committed monooxygenase of furanocoumarin biosynthesis" (PDF). The Journal of Biological Chemistry. 282 (1): 542–54. doi:10.1074/jbc.M604762200. PMID 17068340.
