Evidence map›Paper›PMID 23344904›Full record

ArticlePlant physiology2013

Monolignol pathway 4-coumaric acid:coenzyme A ligases in Populus trichocarpa: novel specificity, metabolic regulation, and simulation of coenzyme A ligation fluxes.

Hsi-Chuan Chen, Jina Song, Cranos M Williams, Christopher M Shuford, Jie Liu, Jack P Wang, Quanzi Li, Rui Shi, Emine Gokce, Joel Ducoste and 3 more

Open access · greenAbstract read
In one paragraph

Article in Plant physiology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
5.9field-weighted citation impact, top 4% 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

26 citing papers in PubMed, 58 citations in OpenAlex.

  1. PbrMYB14 Enhances Pear Resistance toInternational journal of molecular sciences · 2025
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  7. A High-Throughput Screening System forFrontiers in plant science · 2021
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  19. Isolation and characterization of the 4-coumarate:coenzyme A ligase (4CL1) promoter fromPhysiology and molecular biology of plants : an international journal of functional plant biology · 2016
    Article
  20. 4-Coumarate-CoA Ligase-Like GeneFrontiers in plant science · 2016
    Article
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

13 authors at 1 institution in 1 country.

Hsi-Chuan ChenForest Biotechnology Group, Department of Forestry and Environmental Resources , North Carolina State University, Raleigh, NC 27606, USA.
Jina Song
Cranos M Williams
Christopher M Shuford
Jie Liu
Jack P Wang
Quanzi Li
Rui Shi
Emine Gokce
Joel Ducoste
David C Muddiman
Ronald R Sederoff
Vincent L Chiang
North Carolina State University · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

4-Coumaric acid:coenzyme A ligase (4CL) is involved in monolignol biosynthesis for lignification in plant cell walls. It ligates coenzyme A (CoA) with hydroxycinnamic acids, such as 4-coumaric and caffeic acids, into hydroxycinnamoyl-CoA thioesters. The ligation ensures the activated state of the acid for reduction into monolignols. In Populus spp., it has long been thought that one monolignol-specific 4CL is involved. Here, we present evidence of two monolignol 4CLs, Ptr4CL3 and Ptr4CL5, in Populus trichocarpa. Ptr4CL3 is the ortholog of the monolignol 4CL reported for many other species. Ptr4CL5 is novel. The two Ptr4CLs exhibited distinct Michaelis-Menten kinetic properties. Inhibition kinetics demonstrated that hydroxycinnamic acid substrates are also inhibitors of 4CL and suggested that Ptr4CL5 is an allosteric enzyme. Experimentally validated flux simulation, incorporating reaction/inhibition kinetics, suggested two CoA ligation paths in vivo: one through 4-coumaric acid and the other through caffeic acid. We previously showed that a membrane protein complex mediated the 3-hydroxylation of 4-coumaric acid to caffeic acid. The demonstration here of two ligation paths requiring these acids supports this 3-hydroxylation function. Ptr4CL3 regulates both CoA ligation paths with similar efficiencies, whereas Ptr4CL5 regulates primarily the caffeic acid path. Both paths can be inhibited by caffeic acid. The Ptr4CL5-catalyzed caffeic acid metabolism, therefore, may also act to mitigate the inhibition by caffeic acid to maintain a proper ligation flux. A high level of caffeic acid was detected in stem-differentiating xylem of P. trichocarpa. Our results suggest that Ptr4CL5 and caffeic acid coordinately modulate the CoA ligation flux for monolignol biosynthesis.

Indexed as

Biosynthetic PathwaysComputer SimulationAllosteric RegulationBinding SitesBlotting, WesternCaffeic AcidsCoenzyme ACoenzyme A LigasesCoumaric AcidsKineticsLigninPhenylpropionatesPhosphoproteinsPhosphorylationPlant ExtractsPopulus3-phenylpropionic acidcaffeic acidCaffeic AcidsCoenzyme ACoenzyme A LigasesCoumaric Acidsferulic acidLigninp-coumaric acidPhenylpropionatesPhosphoproteinsPlant ExtractsPropionatesRecombinant Fusion Proteins

Identifiers

PMID23344904
PMCPMC3585612
OpenAlexW2036117077

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.