Evidence map›Paper›PMID 34514540›Full record

ArticleBiotechnology letters2021

Screening and heterologous expression of flavone synthase and flavonol synthase to catalyze hesperetin to diosmetin.

Zhen Wang, Xu Huang, Juan Liu, Feiyao Xiao, Miaomiao Tian, Shenghua Ding, Yang Shan

Abstract read
PubMed Publisher
In one paragraph

Article in Biotechnology letters, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
0.4field-weighted citation impact, top 47% 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

3 citing papers in PubMed, 3 citations in OpenAlex.

  1. Review
  2. Review
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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

7 authors at 1 institution in 1 country.

Zhen WangLongping Branch Graduate School of Hunan University, Changsha, 410125, People's Republic of China.
Xu HuangLongping Branch Graduate School of Hunan University, Changsha, 410125, People's Republic of China.
Juan LiuLongping Branch Graduate School of Hunan University, Changsha, 410125, People's Republic of China.
Feiyao XiaoLongping Branch Graduate School of Hunan University, Changsha, 410125, People's Republic of China.
Miaomiao TianLongping Branch Graduate School of Hunan University, Changsha, 410125, People's Republic of China.
Shenghua DingLongping Branch Graduate School of Hunan University, Changsha, 410125, People's Republic of China. shhding@hotmail.com.ORCID http://orcid.org/0000-0003-2383-0843
Yang ShanLongping Branch Graduate School of Hunan University, Changsha, 410125, People's Republic of China. sy6302@sohu.com.
Hunan University · CN

Funding

Agricultural Science and Technology Innovation Fund of Hunan 2020CX47Agricultural Science and Technology Innovation Project of Hunan Province 2021CX05Science and Technology Innovation Platform and Talent Plan of Hunan 2018TP1030Special Project for Construction of Innovative Hunan Province 2019NK2041Training Program for Excellent Young Innovators of Changsha KQ1905025
6 · The paper itself

Abstract

objectivesIn this study, 44 flavone synthases (FNS) and flavonol synthases (FLS) from different origins were collected. The instability index and conserved domain of the enzymes were analyzed through bioinformatics analysis, the results of which allowed us to screen suitable enzymes for constructing recombinant Escherichia coli. Defective enzymes were selected as controls.

resultsNative- and sodium dodecyl sulfate-polyacrylamide gel electrophoresis were conducted to isolate the heterologously expressed proteins. Liquid chromatography-mass spectrometry,

conclusionsThe catalytic capacity of FNS/FLS from different origins exhibited the expected results, indicating that bioinformatics analysis is useful for screening enzymes. In addition, the catalytic properties of AnFNS and CaFLS (from Camellia sinensis) differed significantly, although these enzymes are structurally similar. Based on this difference, C-2 was predicted as the key site for FNS/FLS catalytic synthesis of diosmetin rather than C-3.

Indexed as

Mixed Function OxygenasesOxidoreductasesPlant ProteinsAngelica archangelicaCamelliaFlavonoidsHesperidinSynthetic Biologydiosmetinflavone synthase IFlavonoidsflavonol synthasehesperetinHesperidinMixed Function OxygenasesOxidoreductasesPlant ProteinsDiosmetinFlavone synthaseFlavonol synthetaseSynthetic biology

Identifiers

PMID34514540
OpenAlexW3199987950

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.