Isoflavonoid synthase | |||||||||
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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 | ||||||||
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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). 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)
Oxidoreductases: dioxygenases, including steroid hydroxylases (EC 1.14) | |
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1.14.11: 2-oxoglutarate | |
1.14.13: NADH or NADPH | |
1.14.14: reduced flavin or flavoprotein | |
1.14.15: reduced iron–sulfur protein | |
1.14.16: reduced pteridine (BH4 dependent) | |
1.14.17: reduced ascorbate | |
1.14.18-19: other | |
1.14.99 - miscellaneous |
Enzymes | |
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