Evidence map›Paper›PMID 38041062›Full record

ArticleBMC plant biology2023

Functional and kinetics of two efficient phenylalanine ammonia lyase from Pyrus bretschneideri.

Guohui Li, Cheng Song, Muhammad Aamir Manzoor, Daoyuan Li, Yunpeng Cao, Yongping Cai

Open access · goldAbstract read
In one paragraph

Article in BMC plant biology, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
3.1field-weighted citation impact, top 8% 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

11 citing papers in PubMed, 20 citations in OpenAlex.

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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

6 authors at 4 institutions in 1 country.

Guohui Li *Anhui Engineering Research Center for Eco-Agriculture of Traditional Chinese Medicine, Anhui Provincial Key Laboratory for Quality Evaluation and Improvement of Traditional Chinese Medicine, College of Biological and Pharmaceutical Engineering, West Anhui University, Lu'an, 237012, China.
Cheng Song *Anhui Engineering Research Center for Eco-Agriculture of Traditional Chinese Medicine, Anhui Provincial Key Laboratory for Quality Evaluation and Improvement of Traditional Chinese Medicine, College of Biological and Pharmaceutical Engineering, West Anhui University, Lu'an, 237012, China.
Muhammad Aamir ManzoorDepartment of Plant Science, School of Agriculture and Biology, Shanghai Jiao Tong University, Shanghai, China.
Daoyuan LiAnhui Engineering Research Center for Eco-Agriculture of Traditional Chinese Medicine, Anhui Provincial Key Laboratory for Quality Evaluation and Improvement of Traditional Chinese Medicine, College of Biological and Pharmaceutical Engineering, West Anhui University, Lu'an, 237012, China.
Yunpeng CaoCAS Key Laboratory of Plant Germplasm Enhancement and Specialty Agriculture, Wuhan Botanical Garden, Chinese Academy of Sciences, Wuhan, 430074, China. caoyunpeng@wbgcas.cn.
Yongping CaiAnhui Agricultural University, Hefei, 230036, China. ypcaiah@163.com.
West Anhui University · CNAnhui Agricultural University · CNChinese Academy of Sciences · CNShanghai Jiao Tong University · CN

Funding

National Natural Science Foundation of China 32202442Startup fund for high-level talents of West Anhui University WGKQ2021079
6 · The paper itself

Abstract

backgroundThe enzyme phenylalanine ammonia lyase (PAL) controls the transition from primary to secondary metabolism by converting L-phenylalanine (L-Phe) to cinnamic acid. However, the function of PAL in pear plants (Pyrus bretschneideri) has not yet been fully elucidated.

resultsWe identified three PAL genes (PbPAL1, PbPAL2 and PbPAL3) from the pear genome by exploring pear genome databases. The evolutionary tree revealed that three PbPALs were classified into one group. We expressed PbPAL1 and PbPAL2 recombinant proteins, and the purified PbPAL1 and PbPAL2 proteins showed strict substrate specificity for L-Phe, no activity toward L-Tyr in vitro, and modest changes in kinetics and enzyme characteristics. Furthermore, overexpression of PbAL1 and PbPAL1-RNAi, respectively, and resulted in significant changes in stone cell and lignin contents in pear fruits. The results of yeast one-hybrid (Y1H) assays that PbWLIM1 could bind to the conserved PAL box in the PbPAL promoter and regulate the transcription level of PbPAL2.

conclusionsOur findings not only showed PbPAL's potential role in lignin biosynthesis but also laid the foundation for future studies on the regulation of lignin synthesis and stone cell development in pear fruit utilizing molecular biology approaches.

Indexed as

PyrusGene Expression Regulation, PlantLigninPhenylalanine Ammonia-LyasePhylogenyPlant ProteinsLigninPhenylalanine Ammonia-LyasePlant ProteinsKineticsLigninPhenylalanine ammonia lyase (PAL)Pyrus bretschneideri

Identifiers

PMID38041062
PMCPMC10693048
OpenAlexW4389257881

What OpenQuestion holds

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LicenceCC BY
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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.