Evidence map›Paper›PMID 37634202›Full record

ArticleThe FEBS journal2023

Structural and biochemical characterisation of the N-carbamoyl-β-alanine amidohydrolase from Rhizobium radiobacter MDC 8606.

Ani Paloyan, Armen Sargsyan, Mariam D Karapetyan, Artur Hambardzumyan, Sergei Kocharov, Henry Panosyan, Karine Dyukova, Marina Kinosyan, Anna Krueger, Cecilia Piergentili and 5 more

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

Article in The FEBS journal, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
0.2field-weighted citation impact, top 40% 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

1 citing paper in PubMed, 1 citations in OpenAlex.

  1. 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

15 authors at 6 institutions in 3 countries.

Ani PaloyanScientific and Production Center "Armbiotechnology" of NAS RA, Yerevan, Armenia.ORCID 0000-0003-0279-2104
Armen SargsyanScientific and Production Center "Armbiotechnology" of NAS RA, Yerevan, Armenia.
Mariam D KarapetyanScientific and Production Center "Armbiotechnology" of NAS RA, Yerevan, Armenia.
Artur HambardzumyanScientific and Production Center "Armbiotechnology" of NAS RA, Yerevan, Armenia.
Sergei KocharovThe Scientific Technological Centre of Organic and Pharmaceutical Chemistry SNPO of NAS RA, Yerevan, Armenia.
Henry PanosyanThe Scientific Technological Centre of Organic and Pharmaceutical Chemistry SNPO of NAS RA, Yerevan, Armenia.
Karine DyukovaScientific and Production Center "Armbiotechnology" of NAS RA, Yerevan, Armenia.
Marina KinosyanScientific and Production Center "Armbiotechnology" of NAS RA, Yerevan, Armenia.
Anna KruegerAuthority for the Environment, Climate, Energy and Agriculture in Hamburg, Hamburg, Germany.
Cecilia PiergentiliSchool of Natural and Environmental Sciences, Newcastle University, Newcastle upon Tyne, UK.
Will A StanleySchool of Natural and Environmental Sciences, Newcastle University, Newcastle upon Tyne, UK.
Karrera Y DjokoDepartment of Biosciences, Durham University, Durham, UK.
Arnaud BasléNewcastle University Biosciences Institute, Faculty of Medical Sciences, Newcastle University, Newcastle upon Tyne, UK.
Jon Marles-WrightSchool of Natural and Environmental Sciences, Newcastle University, Newcastle upon Tyne, UK.ORCID 0000-0002-9156-3284
Garabed AntranikianCenter for Biobased Solutions TUHH, Hamburg, Germany.
Scientific Center of Zoology and Hydroecology · AMNewcastle University · GBInstitute of Fine Organic Chemistry of Scientific - Technological Center of Organic and Pharmaceutical Chemistry · AMBiobase (Germany) · DEDurham University · GBHamburg Institut (Germany) · DE

Funding

Biotechnology and Biological Sciences Research Council BB/N005570/1
6 · The paper itself

Abstract

N-carbamoyl-β-alanine amidohydrolase (CβAA) constitutes one of the most important groups of industrially relevant enzymes used in the production of optically pure amino acids and derivatives. In this study, a CβAA-encoding gene from Rhizobium radiobacter strain MDC 8606 was cloned and overexpressed in Escherichia coli. The purified recombinant enzyme (RrCβAA) showed a specific activity of 14 U·mg

Indexed as

Agrobacterium tumefaciensAmino AcidsAmidohydrolasesbeta-AlanineSubstrate SpecificityAmidohydrolasesAmino Acidsbeta-AlanineN-carbamoyl-beta-alaninecarbamoylasemetalloproteinN-carbamoyl-β-alanineX-ray crystallographyβ-ureidopropionase

Identifiers

PMID37634202
PMCPMC10952681
OpenAlexW4386204040

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.