Evidence map›Paper›PMID 26754912›Full record

ArticleScientific reports2016

Flavone synthases from Lonicera japonica and L. macranthoides reveal differential flavone accumulation.

Jie Wu, Xiao-Chen Wang, Yang Liu, Hui Du, Qing-Yan Shu, Shang Su, Li-Jin Wang, Shan-Shan Li, Liang-Sheng Wang

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.

0numbers the graph read from it
0cells of the map it votes in
32citing papers in PubMed
2.6field-weighted citation impact, top 11% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

32 citing papers in PubMed, 54 citations in OpenAlex.

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  14. Expanding flavone and flavonol production capabilities inFrontiers in bioengineering and biotechnology · 2023
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  17. The Flavonoid Biosynthesis Network in Plants.International journal of molecular sciences · 2021
    Review
  18. Article
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

9 authors at 4 institutions in 1 country.

Jie WuKey Laboratory of Plant Resources/Beijing Botanical Garden, Institute of Botany, Chinese Academy of Sciences, Beijing 100093, China.
Xiao-Chen WangUniversity of Chinese Academy of Sciences, Beijing 100049, China.
Yang LiuKey Laboratory of Plant Resources/Beijing Botanical Garden, Institute of Botany, Chinese Academy of Sciences, Beijing 100093, China.
Hui DuKey Laboratory of Plant Resources/Beijing Botanical Garden, Institute of Botany, Chinese Academy of Sciences, Beijing 100093, China.
Qing-Yan ShuKey Laboratory of Plant Resources/Beijing Botanical Garden, Institute of Botany, Chinese Academy of Sciences, Beijing 100093, China.
Shang SuKey Laboratory of Plant Resources/Beijing Botanical Garden, Institute of Botany, Chinese Academy of Sciences, Beijing 100093, China.
Li-Jin WangKey Laboratory of Plant Resources/Beijing Botanical Garden, Institute of Botany, Chinese Academy of Sciences, Beijing 100093, China.
Shan-Shan LiKey Laboratory of Plant Resources/Beijing Botanical Garden, Institute of Botany, Chinese Academy of Sciences, Beijing 100093, China.
Liang-Sheng WangKey Laboratory of Plant Resources/Beijing Botanical Garden, Institute of Botany, Chinese Academy of Sciences, Beijing 100093, China.
University of Chinese Academy of Sciences · CNBeijing Botanical Garden · CNChinese Academy of Sciences · CNInstitute of Botany · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Flavones are important secondary metabolites found in many plants. In Lonicera species, flavones contribute both physiological and pharmaceutical properties. However, flavone synthase (FNS), the key enzyme responsible for flavone biosynthesis, has not yet been characterized in Lonicera species. In this study, FNSII genes were identified from Lonicera japonica Thunb. and L. macranthoides Hand.-Mazz. In the presence of NADPH, the recombinant cytochrome P450 proteins encoded by LjFNSII-1.1, LjFNSII-2.1, and LmFNSII-1.1 converted eriodictyol, naringenin, and liquiritigenin to the corresponding flavones directly. The different catalytic properties between LjFNSII-2.1 and LjFNSII-1.1 were caused by a single amino acid substitution at position 242 (glutamic acid to lysine). A methionine at position 206 and a leucine at position 381 contributed considerably to the high catalytic activity of LjFNSII-1.1. In addition, LjFNSII-1.1&2.1 and LmFNSII-1.1 also biosynthesize flavones that were further modified by O-glycosylation in transgenic tobacco. The expression levels of the FNSII genes were consistent with flavone accumulation patterns in flower buds. Our findings suggested that the weak catalytic activity of LmFNSII-1.1 and the relatively low expression of LmFNSII-1.1 in flowers might be responsible for the low levels of flavone accumulation in flower buds of L. macranthoides.

Indexed as

Amino Acid SequenceBiosynthetic PathwaysCatalysisEnzyme ActivationFlavonesGene ExpressionLoniceraMixed Function OxygenasesModels, MolecularMolecular Sequence DataMutationPhylogenyProtein ConformationProtein TransportRecombinant ProteinsFlavonesMixed Function OxygenasesRecombinant Proteins

Identifiers

PMID26754912
PMCPMC4709722
OpenAlexW2233264049

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