Biology:Isoflavonoid synthase
| Isoflavonoid synthase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 1.14.14.87 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
2-hydroxyisoflavanone synthase (EC 1.14.14.87, CYT93C, IFS, isoflavonoid synthase) is an enzyme with systematic name liquiritigenin,NADPH:oxygen oxidoreductase (hydroxylating, aryl migration).[1][2] It catalyses a rearrangement reaction which converts flavonoids into isoflavones, for example:
The product 2,4',7-trihydroxyisoflavanone is unstable and loses water, either spontaneously or by the action of 2-hydroxyisoflavanone dehydratase, giving daidzein.[3]
The enzyme can also act on naringenin, leading to the isoflavone genistein.{[4]
Isoflavonoid synthase is a cytochrome P450 protein containing heme. It requires a partner cytochrome P450 reductase for functional expression. This uses nicotinamide adenine dinucleotide phosphate (NADPH).[5]
References
- ↑ "Reaction mechanism of oxidative rearrangement of flavanone in isoflavone biosynthesis". FEBS Letters 271 (1–2): 219–22. October 1990. doi:10.1016/0014-5793(90)80410-k. PMID 2226805. Bibcode: 1990FEBSL.271..219H.
- ↑ "Multiple mutagenesis of P450 isoflavonoid synthase reveals a key active-site residue". Biochemical and Biophysical Research Communications 330 (3): 907–13. May 2005. doi:10.1016/j.bbrc.2005.03.053. PMID 15809082. Bibcode: 2005BBRC..330..907S.
- ↑ Hakamatsuka, Takashi; Mori, Kazumi; Ishida, Shinichi; Ebizuka, Yutaka; Sankawa, Ushio (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.
- ↑ Enzyme 1.14.14.87 at KEGG Pathway Database.
- ↑ "Key amino acid residues required for aryl migration catalysed by the cytochrome P450 2-hydroxyisoflavanone synthase". The Plant Journal 31 (5): 555–64. September 2002. doi:10.1046/j.1365-313x.2002.01378.x. PMID 12207646.
External links
- Isoflavonoid+synthase at the US National Library of Medicine Medical Subject Headings (MeSH)
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