Evidence map›Paper›PMID 26386069›Full record

ArticleApplied and environmental microbiology2015

Phylogenetic and kinetic characterization of a suite of dehydrogenases from a newly isolated bacterium, strain SG61-1L, that catalyze the turnover of guaiacylglycerol-β-guaiacyl ether stereoisomers.

Shannu Palamuru, Nikki Dellas, Stephen L Pearce, Andrew C Warden, John G Oakeshott, Gunjan Pandey

Open access · hybridAbstract read
In one paragraph

Article in Applied and environmental microbiology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
2.0field-weighted citation impact, top 15% 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

11 citing papers in PubMed, 24 citations in OpenAlex.

  1. Review
  2. The Study of Potentially Lignocellulolytic ActinobacteriaIndian journal of microbiology · 2023
    Article
  3. Aromatic Dimer Dehydrogenases fromApplied and environmental microbiology · 2021
    Article
  4. Article
  5. Article
  6. A heterodimeric glutathioneThe Journal of biological chemistry · 2019
    Article
  7. Article
  8. The Journal of biological chemistry · 2018
    Article
  9. Article
  10. Article
  11. 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

6 authors at 1 institution in 1 country.

Shannu PalamuruCSIRO Land & Water Flagship, Acton, ACT, Australia Research School of Chemistry, Acton, ACT, Australia.
Nikki DellasCSIRO Land & Water Flagship, Acton, ACT, Australia.
Stephen L PearceCSIRO Land & Water Flagship, Acton, ACT, Australia.
Andrew C WardenCSIRO Land & Water Flagship, Acton, ACT, Australia.
John G OakeshottCSIRO Land & Water Flagship, Acton, ACT, Australia.
Gunjan PandeyCSIRO Land & Water Flagship, Acton, ACT, Australia gunjan.pandey@csiro.au.
CSIRO Land and Water · AU

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Lignin is a complex aromatic polymer found in plant cell walls that makes up 15 to 40% of plant biomass. The degradation of lignin substructures by bacteria is of emerging interest because it could provide renewable alternative feedstocks and intermediates for chemical manufacturing industries. We have isolated a bacterium, strain SG61-1L, that rapidly degrades all of the stereoisomers of one lignin substructure, guaiacylglycerol-β-guaiacyl ether (GGE), which contains a key β-O-4 linkage found in most intermonomer linkages in lignin. In an effort to understand the rapid degradation of GGE by this bacterium, we heterologously expressed and kinetically characterized a suite of dehydrogenase candidates for the first known step of GGE degradation. We identified a clade of active GGE dehydrogenases and also several other dehydrogenases outside this clade that were all able to oxidize GGE. Several candidates exhibited stereoselectivity toward the GGE stereoisomers, while others had higher levels of catalytic performance than previously described GGE dehydrogenases for all four stereoisomers, indicating a variety of potential applications for these enzymes in the manufacture of lignin-derived commodities.

Indexed as

Bacterial ProteinsCatalysisGuaifenesinKineticsLigninOxidation-ReductionPhylogenySphingomonadaceaeStereoisomerismSugar Alcohol DehydrogenasesBacterial Proteinsguaiacylglycerol-beta-guaiacyl etherguaiacylglycerol beta-O-4-guaiacyl ether dehydrogenaseGuaifenesinLigninSugar Alcohol Dehydrogenases

Identifiers

PMID26386069
PMCPMC4651090
OpenAlexW1945849808

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.