Characterization of flavone synthase I from rice
Author(s) -
Yoon Jung Lee,
Jeong Ho Kim,
Bong Gyu Kim,
Yoongho Lim,
JoongHoon Ahn
Publication year - 2008
Publication title -
bmb reports
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.511
H-Index - 77
eISSN - 1976-670X
pISSN - 1976-6696
DOI - 10.5483/bmbrep.2008.41.1.068
Subject(s) - flavanone , apigenin , flavones , naringenin , chemistry , biochemistry , enzyme , apiaceae , cofactor , atp synthase , biology , stereochemistry , flavonoid , botany , chromatography , antioxidant
Flavones are synthesized from flavanones through the action of flavone synthases (FNSs). There are two FNSs, FNS I and II. FNS I is a soluble dioxygenase present in members of the Apiaceae family and FNS II is a membrane bound cytochrome P450 enzyme that has been identified in numerous plant species. In this study, we cloned OsFNS I-1 from rice by RTPCR, expressed it in E. coli, and purified the recombinant protein. By NMR analysis, we found that OsFNS I-1 converted the flavanone (2S)-naringenin into the flavone, apigenin. Moreover, we found that the cofactors oxoglutarate, FeSO(4), ascorbate and catalase are required for this reaction. OsFNS I-1 encodes a flavone synthase I. This is the first type I FNS I found outside of the Apiaceae family.
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