(Redirected from
2-hydroxyisoflavanone synthase)
| Isoflavonoid synthase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 1.14.13.136 | ||||||||
| 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 1.14.13.136, CYT93C, IFS, isoflavonoid synthase) is an enzyme with systematic name liquiritigenin,NADPH:oxygen oxidoreductase (hydroxylating, aryl migration). [1] [2] [3] This enzyme catalyses the following chemical reactions:
- liquiritigenin + O2 + NADPH + H+ 2,4',7-trihydroxyisoflavanone + H2O + NADP+
and
- (2S)- naringenin + O2 + NADPH + H+ 2,4',5,7-tetrahydroxyisoflavanone + H2O + NADP+
Isoflavonoid synthase requires cytochrome P450.
References
- ^ Hashim MF, Hakamatsuka T, Ebizuka Y, Sankawa U (October 1990). "Reaction mechanism of oxidative rearrangement of flavanone in isoflavone biosynthesis". FEBS Letters. 271 (1–2): 219–22. doi: 10.1016/0014-5793(90)80410-k. PMID 2226805.
- ^ Sawada Y, Kinoshita K, Akashi T, Aoki T, Ayabe S (September 2002). "Key amino acid residues required for aryl migration catalysed by the cytochrome P450 2-hydroxyisoflavanone synthase". The Plant Journal. 31 (5): 555–64. doi: 10.1046/j.1365-313x.2002.01378.x. PMID 12207646.
- ^ Sawada Y, Ayabe S (May 2005). "Multiple mutagenesis of P450 isoflavonoid synthase reveals a key active-site residue". Biochemical and Biophysical Research Communications. 330 (3): 907–13. doi: 10.1016/j.bbrc.2005.03.053. PMID 15809082.
External links
- Isoflavonoid+synthase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
(Redirected from
2-hydroxyisoflavanone synthase)
| Isoflavonoid synthase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 1.14.13.136 | ||||||||
| 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 1.14.13.136, CYT93C, IFS, isoflavonoid synthase) is an enzyme with systematic name liquiritigenin,NADPH:oxygen oxidoreductase (hydroxylating, aryl migration). [1] [2] [3] This enzyme catalyses the following chemical reactions:
- liquiritigenin + O2 + NADPH + H+ 2,4',7-trihydroxyisoflavanone + H2O + NADP+
and
- (2S)- naringenin + O2 + NADPH + H+ 2,4',5,7-tetrahydroxyisoflavanone + H2O + NADP+
Isoflavonoid synthase requires cytochrome P450.
References
- ^ Hashim MF, Hakamatsuka T, Ebizuka Y, Sankawa U (October 1990). "Reaction mechanism of oxidative rearrangement of flavanone in isoflavone biosynthesis". FEBS Letters. 271 (1–2): 219–22. doi: 10.1016/0014-5793(90)80410-k. PMID 2226805.
- ^ Sawada Y, Kinoshita K, Akashi T, Aoki T, Ayabe S (September 2002). "Key amino acid residues required for aryl migration catalysed by the cytochrome P450 2-hydroxyisoflavanone synthase". The Plant Journal. 31 (5): 555–64. doi: 10.1046/j.1365-313x.2002.01378.x. PMID 12207646.
- ^ Sawada Y, Ayabe S (May 2005). "Multiple mutagenesis of P450 isoflavonoid synthase reveals a key active-site residue". Biochemical and Biophysical Research Communications. 330 (3): 907–13. doi: 10.1016/j.bbrc.2005.03.053. PMID 15809082.
External links
- Isoflavonoid+synthase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)