Evidence map›Paper›PMID 34560975›Full record

ArticleCarbohydrate polymers2021

Rational enzyme design for controlled functionalization of acetylated xylan for cell-free polymer biosynthesis.

Hsin-Tzu Wang, Vivek S Bharadwaj, Jeong-Yeh Yang, Thomas M Curry, Kelley W Moremen, Yannick J Bomble, Breeanna R Urbanowicz

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Carbohydrate polymers, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing 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

6 citing papers in PubMed.

  1. Article
  2. Review
  3. Insights into pectinCell surface (Amsterdam, Netherlands) · 2023
    Review
  4. Article
  5. Article
  6. Review
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.

Hsin-Tzu WangComplex Carbohydrate Research Center, University of Georgia, 315 Riverbend Road, Athens, GA 30602, USA; Department of Biochemistry and Molecular Biology, University of Georgia, 315 Riverbend Road, Athens, GA 30602, USA.
Vivek S BharadwajRenewable Resources and Enabling Sciences Center, National Renewable Energy Laboratory, 16253 Denver West Parkway, Golden, CO 80401, USA.
Jeong-Yeh YangComplex Carbohydrate Research Center, University of Georgia, 315 Riverbend Road, Athens, GA 30602, USA; Department of Biochemistry and Molecular Biology, University of Georgia, 315 Riverbend Road, Athens, GA 30602, USA.
Thomas M CurryComplex Carbohydrate Research Center, University of Georgia, 315 Riverbend Road, Athens, GA 30602, USA; Department of Biochemistry and Molecular Biology, University of Georgia, 315 Riverbend Road, Athens, GA 30602, USA.
Kelley W MoremenComplex Carbohydrate Research Center, University of Georgia, 315 Riverbend Road, Athens, GA 30602, USA; Department of Biochemistry and Molecular Biology, University of Georgia, 315 Riverbend Road, Athens, GA 30602, USA.
Yannick J BombleBioscience Center, National Renewable Energy Laboratory, 16253 Denver West Parkway, Golden, CO 80401, USA.
Breeanna R UrbanowiczComplex Carbohydrate Research Center, University of Georgia, 315 Riverbend Road, Athens, GA 30602, USA; Department of Biochemistry and Molecular Biology, University of Georgia, 315 Riverbend Road, Athens, GA 30602, USA. Electronic address: breeanna@uga.edu.

Funding

TR&D3. Approaches to Proteoglycan Function at Biochemical and Cellular LevelsP41GM103390 · NIGMS · UNIVERSITY OF GEORGIA · PI MOREMEN, KELLEY W. · 2012 to 2019
$14.5M
Origin of N-Glycan Site-Specific HeterogeneityR01GM130915 · NIGMS · UNIVERSITY OF GEORGIA · PI KANNAN, NATARAJAN, MOREMEN, KELLEY W. · 2019 to 2022
$3.4M
NIGMS NIH HHS P41 GM103390NIGMS NIH HHS R01 GM130915
6 · The paper itself

Abstract

Xylan O-acetyltransferase 1 (XOAT1) is involved in O-acetylating the backbone of hemicellulose xylan. Recent structural analysis of XOAT1 showed two unequal lobes forming a cleft that is predicted to accommodate and position xylan acceptors into proximity with the catalytic triad. Here, we used docking and molecular dynamics simulations to investigate the optimal orientation of xylan in the binding cleft of XOAT1 and identify putative key residues (Gln445 and Arg444 on Minor lobe & Asn312, Met311 and Asp403 on Major lobe) involved in substrate interactions. Site-directed mutagenesis coupled with biochemical analyses revealed the major lobe of XOAT1 is important for xylan binding. Mutation of single key residues yielded XOAT1 variants with various enzymatic efficiencies that are applicable to one-pot synthesis of xylan polymers with different degrees of O-acetylation. Taken together, our results demonstrate the effectiveness of computational modeling in guiding enzyme engineering aimed at modulating xylan and redesigning plant cell walls.

Indexed as

AcetylationAcetyltransferasesArabidopsisArabidopsis ProteinsCatalytic DomainMembrane ProteinsMolecular Docking SimulationMolecular Dynamics SimulationMutagenesis, Site-DirectedMutationProtein BindingXylansAcetyltransferasesArabidopsis ProteinsAt3g55990 protein, ArabidopsisMembrane ProteinsXylansComputational modelingEnzyme engineeringEnzyme-substrate interactionOne-pot synthesisXylan O-acetylationXylooligosaccharide

Identifiers

PMID34560975
PMCPMC8506904

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Registered trials

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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.