Evidence map›Paper›PMID 27580618›Full record

ArticlePlanta2017

Characterization of the cinnamoyl-CoA reductase (CCR) gene family in Populus tomentosa reveals the enzymatic active sites and evolution of CCR.

Nan Chao, Ning Li, Qi Qi, Shuang Li, Tong Lv, Xiang-Ning Jiang, Ying Gai

Abstract read
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In one paragraph

Article in Planta, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
–field-weighted citation impact
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

24 citing papers in PubMed.

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  9. Characterization, Expression Profiling, and Biochemical Analyses of theInternational journal of molecular sciences · 2022
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  10. Comparative Genomic Analysis ofInternational journal of molecular sciences · 2022
    Article
  11. Genome-wide identification and characterization ofFrontiers in plant science · 2022
    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

7 authors.

Nan ChaoCollege of Biological Sciences and Biotechnology, Beijing Forestry University, Beijing, 100083, China.
Ning LiCollege of Biological Sciences and Biotechnology, Beijing Forestry University, Beijing, 100083, China.
Qi QiCollege of Biological Sciences and Biotechnology, Beijing Forestry University, Beijing, 100083, China.
Shuang LiCollege of Biological Sciences and Biotechnology, Beijing Forestry University, Beijing, 100083, China.
Tong LvCollege of Biological Sciences and Biotechnology, Beijing Forestry University, Beijing, 100083, China.
Xiang-Ning JiangCollege of Biological Sciences and Biotechnology, Beijing Forestry University, Beijing, 100083, China.
Ying GaiCollege of Biological Sciences and Biotechnology, Beijing Forestry University, Beijing, 100083, China. gaiying@bjfu.edu.cn.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

MAIN

conclusionTwo distinct cinnamoyl-coenzyme A reductases (CCRs) from Populus tomentosa were cloned and studied and active sites in CCRs were further identified based on sequence divergence, molecular simulation, and site-directed mutants. Cinnamoyl-coenzyme A (CoA) reductase (CCR) is the first committed gene in the lignin-specific pathway and plays a role in the lignin biosynthesis pathway. In this study, we cloned 11 genes encoding CCR or CCR-like proteins in Populus tomentosa. An enzymatic assay of the purified recombinant P. tomentosa (Pto) CCR and PtoCCR-like proteins indicated that only PtoCCR1 and PtoCCR7 had detectable activities toward hydroxycinnamoyl-CoA esters. PtoCCR1 exhibited specificity for feruloyl-CoA, with no detectable activity for any other hydroxycinnamoyl-CoA esters. However, PtoCCR7 catalyzed p-coumaroyl-CoA, caffeoyl-CoA, feruloyl-CoA, and sinapoyl-CoA with a preference for feruloyl-CoA. Site-directed mutations of selected amino acids divergent between PtoCCR1 and 7, combined with modeling and docking, showed that A132 in CCR7 combined with the catalytic triad might comprise the catalytic center. In CCR7, L192, F155, and H208 were identified as the substrate-binding sites, and site-directed mutations of these amino acids showed obvious changes in catalytic efficiency with respect to both feruloyl-CoA and sinapoyl-CoA. Mutant F155Y exhibited greater catalytic efficiency for sinapoyl-CoA compared with that of wild-type PtoCCR7. Finally, recent genome duplication events provided the foundation for CCR divergence. This study further identified the active sites in CCRs and the evolutionary process of CCRs in terrestrial plants.

Indexed as

Catalytic DomainEvolution, MolecularMultigene FamilyAldehyde OxidoreductasesAmino Acid SequenceChromosomes, PlantConserved SequenceEnzyme AssaysGene DuplicationGenes, PlantHydrogen-Ion ConcentrationKineticsMolecular Docking SimulationMutagenesis, Site-DirectedMutant ProteinsPhylogenyAldehyde Oxidoreductasescinnamoyl CoA reductaseMutant ProteinsRecombinant ProteinsBinding sitesCinnamoyl-coenzyme A reductaseGene familyPopulus tomentosaSite-directed mutations

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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.