Journal
BIOTECHNOLOGY LETTERS
Volume 32, Issue 4, Pages 579-584Publisher
SPRINGER
DOI: 10.1007/s10529-009-0188-x
Keywords
Flavonol synthase; Kaempferol; 3-O-methylkaempferol; Naringenin; O-methyltransferase
Categories
Funding
- Biogreen 21 Program, Rural Development Administration, Republic of Korea
- Agenda program (NIAS) [11-30-68]
- Ministry of Education, Science and Technology [2009-0093824]
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Biosynthesis of flavonoid derivatives requires enzyme(s) having high reactivity as well as regioselectivity. We have synthesized 3-O-kaempferol from naringenin using two enzymes. The first reaction, in which naringenin is converted to kaempferol, is mediated by flavonol synthase (FLS). An FLS (PFLS) with strong catalytic activity was cloned and characterized from the genome sequence of the poplar (Populus deltoides). PFLS consists of a 1,008 bp ORF encoding a 38 kDa protein. PFLS was expressed in Escherichia coli with a glutathione-S-transferase (GST) tagging. The purified recombinant PFLS was characterized. Catalytically, it was more efficient than the previously characterized FLSs. A mixture of two E. coli transformants harboring either PFLS or ROMT9 (a kaempferol 3-O-methyltransferase) converted naringenin into 3-O-methylkaempferol.
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