Isoflavonoid synthase
Isoflavonoid synthase | |||||||||
---|---|---|---|---|---|---|---|---|---|
Identifiers | |||||||||
EC number | 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, M.F.; Hakamatsuka, T.; Ebizuka, Y.; Sankawa, U. (1990). "Reaction mechanism of oxidative rearrangement of flavanone in isoflavone biosynthesis". FEBS Lett. 271 (1-2): 219–222. doi:10.1016/0014-5793(90)80410-k. PMID 2226805.
- ↑ Sawada, Y.; Kinoshita, K.; Akashi, T.; Aoki, T.; Ayabe, S. (2002). "Key amino acid residues required for aryl migration catalysed by the cytochrome P450 2-hydroxyisoflavanone synthase". Plant J. 31 (5): 555–564. doi:10.1046/j.1365-313x.2002.01378.x. PMID 12207646.
- ↑ Sawada, Y.; Ayabe, S. (2005). "Multiple mutagenesis of P450 isoflavonoid synthase reveals a key active-site residue". Biochem. Biophys. Res. Commun. 330 (3): 907–913. doi:10.1016/j.bbrc.2005.03.053. PMID 15809082.
External links
- Isoflavonoid synthase at the US National Library of Medicine Medical Subject Headings (MeSH)
This article is issued from Wikipedia - version of the 5/21/2016. The text is available under the Creative Commons Attribution/Share Alike but additional terms may apply for the media files.