Evidence map›Paper›PMID 25572294›Full record

ReviewCellular and molecular life sciences : CMLS2015

Laccases of prokaryotic origin: enzymes at the interface of protein science and protein technology.

Lígia O Martins, Paulo Durão, Vânia Brissos, Peter F Lindley

Open access · greenAbstract readReview
In one paragraph

Review in Cellular and molecular life sciences : CMLS, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.

0numbers the graph read from it
0cells of the map it votes in
36citing papers in PubMed
14.5field-weighted citation impact, top 1% 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

36 citing papers in PubMed, 110 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Enzymatic Oxidation of Aflatoxin MFoods (Basel, Switzerland) · 2024
    Article
  5. Review
  6. Article
  7. Catalase-peroxidase StKatG2 fromFrontiers in microbiology · 2024
    Article
  8. Detoxification of aflatoxin B1 by aFrontiers in microbiology · 2024
    Article
  9. Article
  10. Article
  11. Article
  12. Review
  13. Article
  14. Article
  15. Article
  16. Review
  17. Review
  18. Article
  19. Review
  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

4 authors at 1 institution in 1 country.

Lígia O MartinsInstituto de Tecnologia Química e Biológica, Universidade Nova de Lisboa, Av. da República, 2781-901, Oeiras, Portugal, lmartins@itqb.unl.pt.
Paulo Durão
Vânia Brissos
Peter F Lindley
Universidade Nova de Lisboa · PT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The ubiquitous members of the multicopper oxidase family of enzymes oxidize a range of aromatic substrates such as polyphenols, methoxy-substituted phenols, amines and inorganic compounds, concomitantly with the reduction of molecular dioxygen to water. This family of enzymes can be broadly divided into two functional classes: metalloxidases and laccases. Several prokaryotic metalloxidases have been described in the last decade showing a robust activity towards metals, such as Cu(I), Fe(II) or Mn(II) and have been implicated in the metal metabolism of the corresponding microorganisms. Many laccases, with a superior efficiency for oxidation of organic compounds when compared with metals, have also been identified and characterized from prokaryotes, playing roles that more closely conform to those of intermediary metabolism. This review aims to present an update of current knowledge on prokaryotic multicopper oxidases, with a special emphasis on laccases, anticipating their enormous potential for industrial and environmental applications.

Indexed as

BacteriaLaccaseMetalsProkaryotic CellsProtein Structure, TertiaryLaccaseMetals

Identifiers

PMID25572294
PMCPMC11113980
OpenAlexW2012975010

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.