Evidence map›Paper›PMID 38003383›Full record

ArticleInternational journal of molecular sciences2023

Expanded Substrate Specificity in D-Amino Acid Transaminases: A Case Study of Transaminase from

Sofia A Shilova, Ilya O Matyuta, Elizaveta S Petrova, Alena Y Nikolaeva, Tatiana V Rakitina, Mikhail E Minyaev, Konstantin M Boyko, Vladimir O Popov, Ekaterina Yu Bezsudnova

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

Article in International journal of molecular sciences, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
0.5field-weighted citation impact, top 44% 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

3 citing papers in PubMed, 5 citations in OpenAlex.

  1. Article
  2. Article
  3. 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 4 institutions in 1 country.

Sofia A ShilovaBach Institute of Biochemistry, Research Centre of Biotechnology, Russian Academy of Sciences, Moscow 119071, Russia.
Ilya O MatyutaBach Institute of Biochemistry, Research Centre of Biotechnology, Russian Academy of Sciences, Moscow 119071, Russia.ORCID 0000-0002-6297-8392
Elizaveta S PetrovaBach Institute of Biochemistry, Research Centre of Biotechnology, Russian Academy of Sciences, Moscow 119071, Russia.
Alena Y NikolaevaBach Institute of Biochemistry, Research Centre of Biotechnology, Russian Academy of Sciences, Moscow 119071, Russia.
Tatiana V RakitinaBach Institute of Biochemistry, Research Centre of Biotechnology, Russian Academy of Sciences, Moscow 119071, Russia.ORCID 0000-0002-3096-8659
Mikhail E MinyaevN. D. Zelinsky Institute of Organic Chemistry, Russian Academy of Sciences, Moscow 119334, Russia.
Konstantin M BoykoBach Institute of Biochemistry, Research Centre of Biotechnology, Russian Academy of Sciences, Moscow 119071, Russia.ORCID 0000-0001-8229-189X
Vladimir O PopovBach Institute of Biochemistry, Research Centre of Biotechnology, Russian Academy of Sciences, Moscow 119071, Russia.
Ekaterina Yu BezsudnovaBach Institute of Biochemistry, Research Centre of Biotechnology, Russian Academy of Sciences, Moscow 119071, Russia.ORCID 0000-0002-4954-7547
A N Bach Institute of Biochemistry · RULomonosov Moscow State University · RUKurchatov Institute · RUN.D. Zelinsky Institute of Organic Chemistry · RU

Funding

Ministry of Science and Higher Education of the Russian Federation no numberRussian Science Foundation 19_14_00164
6 · The paper itself

Abstract

Enzymes with expanded substrate specificity are good starting points for the design of biocatalysts for target reactions. However, the structural basis of the expanded substrate specificity is still elusive, especially in the superfamily of pyridoxal-5'-phosphate-dependent transaminases, which are characterized by a conserved organization of both the active site and functional dimer. Here, we analyze the structure-function relationships in a non-canonical D-amino acid transaminase from

Indexed as

Amino AcidsTransaminasesActinobacteriaKineticsPhenethylaminesSubstrate SpecificityAmino AcidsPhenethylaminesTransaminasesD-amino acidphenylhydrazinestereoselective aminationstructure-function relationshipstransaminase

Identifiers

PMID38003383
PMCPMC10671532
OpenAlexW4388635523

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.