Evidence map›Paper›PMID 32679618›Full record

ArticleThe FEBS journal2021

R-hydroxynitrile lyase from the cyanogenic millipede, Chamberlinius hualienensis-A new entry to the carrier protein family Lipocalines.

Fumihiro Motojima, Atsushi Izumi, Aem Nuylert, Zhenyu Zhai, Mohammad Dadashipour, Sayaka Shichida, Takuya Yamaguchi, Shogo Nakano, Yasuhisa Asano

Open access · hybridAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in The FEBS journal, 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
1.6field-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, 13 citations in OpenAlex.

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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 2 institutions in 1 country.

Fumihiro MotojimaBiotechnology Research Center and Department of Biotechnology, Toyama Prefectural University, Imizu, Toyama, Japan.ORCID 0000-0003-4461-8673
Atsushi IzumiBiotechnology Research Center and Department of Biotechnology, Toyama Prefectural University, Imizu, Toyama, Japan.
Aem NuylertBiotechnology Research Center and Department of Biotechnology, Toyama Prefectural University, Imizu, Toyama, Japan.ORCID 0000-0002-8312-9592
Zhenyu ZhaiBiotechnology Research Center and Department of Biotechnology, Toyama Prefectural University, Imizu, Toyama, Japan.ORCID 0000-0003-1691-5945
Mohammad DadashipourBiotechnology Research Center and Department of Biotechnology, Toyama Prefectural University, Imizu, Toyama, Japan.ORCID 0000-0002-4842-9282
Sayaka ShichidaBiotechnology Research Center and Department of Biotechnology, Toyama Prefectural University, Imizu, Toyama, Japan.
Takuya YamaguchiBiotechnology Research Center and Department of Biotechnology, Toyama Prefectural University, Imizu, Toyama, Japan.ORCID 0000-0002-7533-430X
Shogo NakanoBiotechnology Research Center and Department of Biotechnology, Toyama Prefectural University, Imizu, Toyama, Japan.ORCID 0000-0002-6614-7158
Yasuhisa AsanoBiotechnology Research Center and Department of Biotechnology, Toyama Prefectural University, Imizu, Toyama, Japan.ORCID 0000-0003-3645-3952
Amano Enzyme (Japan) · JPToyama Prefectural University · JP

Funding

Exploratory Research for Advanced Technology, Japan Science and Technology Agency JPMJER1102Japan Society for the Promotion of Science 17H06169
6 · The paper itself

Abstract

Hydroxynitrile lyases (HNLs) catalyze the cleavage of cyanohydrin into cyanide and the corresponding aldehyde or ketone. Moreover, they catalyze the synthesis of cyanohydrin in the reverse reaction, utilized in industry for preparation of enantiomeric pure pharmaceutical ingredients and fine chemicals. We discovered a new HNL from the cyanogenic millipede, Chamberlinius hualienensis. The enzyme displays several features including a new primary structure, high stability, and the highest specific activity in (R)-mandelonitrile ((R)-MAN) synthesis (7420 U·mg

Indexed as

AcetonitrilesAldehyde-LyasesAmino Acid SequenceAnimalsArthropod ProteinsArthropodsBinding SitesBiocatalysisCloning, MolecularCrystallography, X-RayEnzyme InhibitorsEscherichia coliGene ExpressionGenetic VectorsIodoacetic AcidKineticsAcetonitrilesAldehyde-LyasesArthropod ProteinsEnzyme InhibitorsIodoacetic AcidLipocalinsmandelonitrilemandelonitrile lyaseRecombinant ProteinsthiocyanateThiocyanatescatalytic mechanismChamberlinius hualienensiscrystal structurehydroxynitrile lyaselipocalin familymillipedesite-directed mutagenesis

Identifiers

PMID32679618
PMCPMC7983990
OpenAlexW3043577772

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.