Evidence map›Paper›PMID 31795104›Full record

ArticleInternational journal of molecular sciences2019

Genetic and Functional Diversity of Nitrilases in Agaricomycotina.

Lenka Rucká, Martin Chmátal, Natalia Kulik, Lucie Petrásková, Helena Pelantová, Petr Novotný, Romana Příhodová, Miroslav Pátek, Ludmila Martínková

Open access · goldAbstract read
In one paragraph

Article in International journal of molecular sciences, 2019. 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
2.1field-weighted citation impact, top 14% 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

6 citing papers in PubMed, 15 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Phe-140 Determines the Catalytic Efficiency of Arylacetonitrilase fromInternational journal of molecular sciences · 2020
    Article
  5. Article
  6. Biocatalysis: "A Jack of all Trades..."International journal of molecular sciences · 2020
    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

9 authors at 1 institution in 1 country.

Lenka RuckáLaboratory of Molecular Genetics of Bacteria, Institute of Microbiology of the Czech Academy of Sciences, Vídeňská 1083, CZ-142 20 Prague, Czech Republic.
Martin ChmátalLaboratory of Biotransformation, Institute of Microbiology of the Czech Academy of Sciences, Vídeňská 1083, CZ-142 20 Prague, Czech Republic.
Natalia KulikCenter for Nanobiology and Structural Biology, Institute of Microbiology of the Czech Academy of Sciences, Zámek 136, CZ-373 33 Nové Hrady, Czech Republic.
Lucie PetráskováLaboratory of Biotransformation, Institute of Microbiology of the Czech Academy of Sciences, Vídeňská 1083, CZ-142 20 Prague, Czech Republic.
Helena PelantováLaboratory of Molecular Structure Characterization, Institute of Microbiology of the Czech Academy of Sciences, Vídeňská 1083, CZ-142 20 Prague, Czech Republic.
Petr NovotnýLaboratory of Biotransformation, Institute of Microbiology of the Czech Academy of Sciences, Vídeňská 1083, CZ-142 20 Prague, Czech Republic.
Romana PříhodováLaboratory of Biotransformation, Institute of Microbiology of the Czech Academy of Sciences, Vídeňská 1083, CZ-142 20 Prague, Czech Republic.
Miroslav PátekLaboratory of Molecular Genetics of Bacteria, Institute of Microbiology of the Czech Academy of Sciences, Vídeňská 1083, CZ-142 20 Prague, Czech Republic.ORCID 0000-0002-9882-0693
Ludmila MartínkováLaboratory of Biotransformation, Institute of Microbiology of the Czech Academy of Sciences, Vídeňská 1083, CZ-142 20 Prague, Czech Republic.
Czech Academy of Sciences · CZ

Funding

Grantová Agentura České Republiky 18-00184S
6 · The paper itself

Abstract

Nitrilases participate in the nitrile metabolism in microbes and plants. They are widely used to produce carboxylic acids from nitriles. Nitrilases were described in bacteria, Ascomycota and plants. However, they remain unexplored in Basidiomycota. Yet more than 200 putative nitrilases are found in this division via GenBank. The majority of them occur in the subdivision Agaricomycotina. In this work, we analyzed their sequences and classified them into phylogenetic clades. Members of clade 1 (61 proteins) and 2 (25 proteins) are similar to plant nitrilases and nitrilases from Ascomycota, respectively, with sequence identities of around 50%. The searches also identified five putative cyanide hydratases (CynHs). Representatives of clade 1 and 2 (NitTv1 from

Indexed as

AminohydrolasesBasidiomycotaBinding SitesFumaratesFungal ProteinsHydrogen CyanideMolecular Docking SimulationPhylogenyProtein BindingPyridinesSubstrate SpecificityAminohydrolasesFumaratesfumaronitrileFungal ProteinsHydrogen CyanidenitrilasePyridinesAgaricomycotinaBasidiomycotacyanide hydratasehomology modelingnitrilasenitrileoverproductionphylogenetic distributionsubstrate dockingsubstrate specificity

Identifiers

PMID31795104
PMCPMC6928751
OpenAlexW2991210673

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.