Evidence map›Paper›PMID 27956488›Full record

ArticlePlant physiology2017

Structural and Biochemical Characterization of Cinnamoyl-CoA Reductases.

Steven A Sattler, Alexander M Walker, Wilfred Vermerris, Scott E Sattler, ChulHee Kang

Open access · greenAbstract read
In one paragraph

Article in Plant physiology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
1.4field-weighted citation impact, top 17% 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

21 citing papers in PubMed, 43 citations in OpenAlex.

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  18. Metabolite and transcript profiling of Guinea grass (Panicum maximum Jacq) response to elevated [COMetabolomics : Official journal of the Metabolomic Society · 2019
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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

5 authors at 3 institutions in 1 country.

Steven A SattlerSchool of Molecular Biosciences (S.A.S., A.M.W., C.K.) and Department of Chemistry (C.K.), Washington State University, Pullman, Washington 99164.ORCID 0000-0001-7991-1664
Alexander M WalkerSchool of Molecular Biosciences (S.A.S., A.M.W., C.K.) and Department of Chemistry (C.K.), Washington State University, Pullman, Washington 99164.
Wilfred VermerrisSchool of Molecular Biosciences (S.A.S., A.M.W., C.K.) and Department of Chemistry (C.K.), Washington State University, Pullman, Washington 99164.ORCID 0000-0002-4582-3436
Scott E SattlerSchool of Molecular Biosciences (S.A.S., A.M.W., C.K.) and Department of Chemistry (C.K.), Washington State University, Pullman, Washington 99164.ORCID 0000-0002-6814-4073
ChulHee KangSchool of Molecular Biosciences (S.A.S., A.M.W., C.K.) and Department of Chemistry (C.K.), Washington State University, Pullman, Washington 99164; chkang@wsu.edu.ORCID 0000-0002-0693-7860
Agricultural Research Service · USUnited States Department of Agriculture · USWashington State University · US

Funding

Roles of Calsequestrin in the Control of Calcium Signals in Health and DiseaseR01GM111254 · NIGMS · RUSH UNIVERSITY MEDICAL CENTER · PI KANG, CHULHEE, RIOS, EDUARDO · 2014 to 2017
$1.4M
NIGMS NIH HHS R01 GM111254
6 · The paper itself

Abstract

Cinnamoyl-coenzyme A reductase (CCR) catalyzes the reduction of hydroxycinnamoyl-coenzyme A (CoA) esters using NADPH to produce hydroxycinnamyl aldehyde precursors in lignin synthesis. The catalytic mechanism and substrate specificity of cinnamoyl-CoA reductases from sorghum (Sorghum bicolor), a strategic plant for bioenergy production, were deduced from crystal structures, site-directed mutagenesis, and kinetic and thermodynamic analyses. Although SbCCR1 displayed higher affinity for caffeoyl-CoA or p-coumaroyl-CoA than for feruloyl-CoA, the enzyme showed significantly higher activity for the latter substrate. Through molecular docking and comparisons between the crystal structures of the Vitis vinifera dihydroflavonol reductase and SbCCR1, residues threonine-154 and tyrosine-310 were pinpointed as being involved in binding CoA-conjugated phenylpropanoids. Threonine-154 of SbCCR1 and other CCRs likely confers strong substrate specificity for feruloyl-CoA over other cinnamoyl-CoA thioesters, and the T154Y mutation in SbCCR1 led to broader substrate specificity and faster turnover. Through data mining using our structural and biochemical information, four additional putative CCR genes were discovered from sorghum genomic data. One of these, SbCCR2, displayed greater activity toward p-coumaroyl-CoA than did SbCCR1, which could imply a role in the synthesis of defense-related lignin. Taken together, these findings provide knowledge about critical residues and substrate preference among CCRs and provide, to our knowledge, the first three-dimensional structure information for a CCR from a monocot species.

Indexed as

Acyl Coenzyme AAldehyde OxidoreductasesAmino Acid SequenceBinding SitesBiocatalysisCalorimetryKineticsLigandsModels, MolecularMutant ProteinsMutationNADPProtein Structure, SecondaryProtein Structure, TertiarySequence AlignmentSorghumAcyl Coenzyme AAldehyde Oxidoreductasescinnamoyl CoA reductasecinnamoyl-coenzyme Aferuloyl-CoALigandsMutant ProteinsNADP

Identifiers

PMID27956488
PMCPMC5291045
OpenAlexW2566435034

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.