Journal
FEBS LETTERS
Volume 588, Issue 14, Pages 2307-2314Publisher
WILEY
DOI: 10.1016/j.febslet.2014.05.023
Keywords
Liverworts; Flavone synthase; Flavonol synthase; 2-Hydroxyflavanone; Site-directed mutagenesis
Funding
- National Natural Science Foundation of China [31170280, 31370330]
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FNS I is a 2-oxoglutarate dependent dioxygenase (2-ODD) found mainly in species of the Apiaceae family. Here, an FNS I cDNA sequence was isolated from the liverwort Plagiochasma appendiculatum (Aytoniaceae) and characterized. The recombinant protein exhibited high FNS I activity catalyzing the conversion of naringenin to apigenin and 2-hydroxynaringenin. The critical residue for flavanone-2-hydroxylation activity was Tyr240, as identified from homology modeling and site-directed mutagenesis. The recombinant protein also showed some flavonol synthase activity, as it can convert dihydrokaempferol to kaempferol. When the Leu311 residue was mutated to Phe, the enzyme's capacity to convert dihydrokaempferol to kaempferol was substantially increased. PaFNS I represents a 2-ODD in which a hydrophobic pi-stacking interaction between the key residue and the naringenin A-ring determines 2-hydroxyflavanone formation. (C) 2014 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
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