Evidence map›Paper›PMID 29229855›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2017

Distinct roles of N- and O-glycans in cellulase activity and stability.

Antonella Amore, Brandon C Knott, Nitin T Supekar, Asif Shajahan, Parastoo Azadi, Peng Zhao, Lance Wells, Jeffrey G Linger, Sarah E Hobdey, Todd A Vander Wall and 8 more

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.

0numbers the graph read from it
0cells of the map it votes in
40citing papers in PubMed
5.4field-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

40 citing papers in PubMed, 113 citations in OpenAlex.

  1. Review
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  8. Engineering cellulases for conversion of lignocellulosic biomass.Protein engineering, design & selection : PEDS · 2023
    Review
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  14. Review
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  18. Review
  19. Biochemical properties of a native β-1,4-mannanase fromBiochemistry and biophysics reports · 2021
    Article
  20. 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

18 authors at 3 institutions in 1 country.

Antonella AmoreBiosciences Center, National Renewable Energy Laboratory, Golden, CO 80401.
Brandon C KnottNational Bioenergy Center, National Renewable Energy Laboratory, Golden, CO 80401.
Nitin T SupekarComplex Carbohydrate Research Center, University of Georgia, Athens, GA 30602.ORCID 0000-0002-7006-7177
Asif ShajahanComplex Carbohydrate Research Center, University of Georgia, Athens, GA 30602.
Parastoo AzadiComplex Carbohydrate Research Center, University of Georgia, Athens, GA 30602.
Peng ZhaoComplex Carbohydrate Research Center, University of Georgia, Athens, GA 30602.
Lance WellsComplex Carbohydrate Research Center, University of Georgia, Athens, GA 30602.
Jeffrey G LingerNational Bioenergy Center, National Renewable Energy Laboratory, Golden, CO 80401.
Sarah E HobdeyBiosciences Center, National Renewable Energy Laboratory, Golden, CO 80401.
Todd A Vander WallBiosciences Center, National Renewable Energy Laboratory, Golden, CO 80401.
Todd ShollenbergerBiosciences Center, National Renewable Energy Laboratory, Golden, CO 80401.
John M YarbroughBiosciences Center, National Renewable Energy Laboratory, Golden, CO 80401.
Zhongping TanDepartment of Chemistry and Biochemistry, University of Colorado, Boulder, CO 80303.ORCID 0000-0002-9302-150X
Michael F CrowleyBiosciences Center, National Renewable Energy Laboratory, Golden, CO 80401.
Michael E HimmelBiosciences Center, National Renewable Energy Laboratory, Golden, CO 80401.
Stephen R DeckerBiosciences Center, National Renewable Energy Laboratory, Golden, CO 80401.ORCID 0000-0001-7002-9034
Gregg T BeckhamNational Bioenergy Center, National Renewable Energy Laboratory, Golden, CO 80401; gregg.beckham@nrel.gov.ORCID 0000-0002-3480-212X
Larry E TaylorBiosciences Center, National Renewable Energy Laboratory, Golden, CO 80401.
National Laboratory of the Rockies · USUniversity of Georgia · USUniversity of Colorado Boulder · US

Funding

Orbitrap Fusion Tribrid Mass SpectrometerS10OD018530 · OD · UNIVERSITY OF GEORGIA · PI AZADI, PARASTOO · 2014 to 2014
$750k
NIH HHS S10 OD018530
6 · The paper itself

Abstract

In nature, many microbes secrete mixtures of glycoside hydrolases, oxidoreductases, and accessory enzymes to deconstruct polysaccharides and lignin in plants. These enzymes are often decorated with N- and O-glycosylation, the roles of which have been broadly attributed to protection from proteolysis, as the extracellular milieu is an aggressive environment. Glycosylation has been shown to sometimes affect activity, but these effects are not fully understood. Here, we examine N- and O-glycosylation on a model, multimodular glycoside hydrolase family 7 cellobiohydrolase (Cel7A), which exhibits an O-glycosylated carbohydrate-binding module (CBM) and an O-glycosylated linker connected to an N- and O-glycosylated catalytic domain (CD)-a domain architecture common to many biomass-degrading enzymes. We report consensus maps for Cel7A glycosylation that include glycan sites and motifs. Additionally, we examine the roles of glycans on activity, substrate binding, and thermal and proteolytic stability. N-glycan knockouts on the CD demonstrate that N-glycosylation has little impact on cellulose conversion or binding, but does have major stability impacts. O-glycans on the CBM have little impact on binding, proteolysis, or activity in the whole-enzyme context. However, linker O-glycans greatly impact cellulose conversion via their contribution to proteolysis resistance. Molecular simulations predict an additional role for linker O-glycans, namely that they are responsible for maintaining separation between ordered domains when Cel7A is engaged on cellulose, as models predict α-helix formation and decreased cellulose interaction for the nonglycosylated linker. Overall, this study reveals key roles for N- and O-glycosylation that are likely broadly applicable to other plant cell-wall-degrading enzymes.

Indexed as

CellulaseEnzyme ActivationEnzyme StabilityGlycoside HydrolasesGlycosylationIntrinsically Disordered ProteinsModels, MolecularMolecular ConformationPolysaccharidesProteolysisTransition TemperatureCellulaseGlycoside HydrolasesIntrinsically Disordered ProteinsPolysaccharidescellulaseglycoside hydrolaseglycosylationintrinsically disordered proteinmannosylation

Identifiers

PMID29229855
PMCPMC5748201
OpenAlexW2774296474

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.