2-hydroxyisoflavanone dehydratase
In enzymology, a 2-hydroxyisoflavanone dehydratase (EC 4.2.1.105) is an enzyme that catalyzes the chemical reaction
- 2,7,4'-trihydroxyisoflavanone daidzein + H2O
| 2-hydroxyisoflavanone dehydratase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 4.2.1.105 | ||||||||
| CAS number | 56022-25-4 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
Hence, this enzyme has one substrate, 2,7,4'-trihydroxyisoflavanone, and two products, daidzein and H2O.
This enzyme belongs to the family of lyases, specifically the hydro-lyases, which cleave carbon-oxygen bonds. The systematic name of this enzyme class is 2,7,4'-trihydroxyisoflavanone hydro-lyase (daidzein-forming). This enzyme is also called 2,7,4'-trihydroxyisoflavanone hydro-lyase. This enzyme participates in isoflavonoid biosynthesis.
References
- Hakamatsuka T, Mori K, Ishida S, Ebizuka Y, Sankawa U (1998). "Purification of 2-hydroxyisoflavanone dehydratase from the cell cultures of Pueraria lobata". Phytochemistry. 49 (2): 497–505. doi:10.1016/S0031-9422(98)00266-0.
This article is issued from Wikipedia. The text is licensed under Creative Commons - Attribution - Sharealike. Additional terms may apply for the media files.