Evidence map›Paper›PMID 34443642›Full record

ArticleMolecules (Basel, Switzerland)2021

The Uncommon Active Site of D-Amino Acid Transaminase from

Alina K Bakunova, Alena Yu Nikolaeva, Tatiana V Rakitina, Tatiana Y Isaikina, Maria G Khrenova, Konstantin M Boyko, Vladimir O Popov, Ekaterina Yu Bezsudnova

Open access · goldAbstract read
In one paragraph

Article in Molecules (Basel, Switzerland), 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing papers in PubMed
3.0field-weighted citation impact, top 9% 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

7 citing papers in PubMed, 27 citations in OpenAlex.

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  6. Diaminopimelic Acid Metabolism byMicrobiology spectrum · 2022
    Article
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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

8 authors at 2 institutions in 1 country.

Alina K BakunovaBach Institute of Biochemistry, Research Center of Biotechnology of the Russian Academy of Sciences, Leninsky Ave. 33, bld. 2, 119071 Moscow, Russia.
Alena Yu NikolaevaBach Institute of Biochemistry, Research Center of Biotechnology of the Russian Academy of Sciences, Leninsky Ave. 33, bld. 2, 119071 Moscow, Russia.
Tatiana V RakitinaBach Institute of Biochemistry, Research Center of Biotechnology of the Russian Academy of Sciences, Leninsky Ave. 33, bld. 2, 119071 Moscow, Russia.
Tatiana Y IsaikinaBach Institute of Biochemistry, Research Center of Biotechnology of the Russian Academy of Sciences, Leninsky Ave. 33, bld. 2, 119071 Moscow, Russia.
Maria G KhrenovaBach Institute of Biochemistry, Research Center of Biotechnology of the Russian Academy of Sciences, Leninsky Ave. 33, bld. 2, 119071 Moscow, Russia.ORCID 0000-0001-7117-3089
Konstantin M BoykoBach Institute of Biochemistry, Research Center of Biotechnology of the Russian Academy of Sciences, Leninsky Ave. 33, bld. 2, 119071 Moscow, Russia.ORCID 0000-0001-8229-189X
Vladimir O PopovBach Institute of Biochemistry, Research Center of Biotechnology of the Russian Academy of Sciences, Leninsky Ave. 33, bld. 2, 119071 Moscow, Russia.
Ekaterina Yu BezsudnovaBach Institute of Biochemistry, Research Center of Biotechnology of the Russian Academy of Sciences, Leninsky Ave. 33, bld. 2, 119071 Moscow, Russia.ORCID 0000-0002-4954-7547
A N Bach Institute of Biochemistry · RULomonosov Moscow State University · RU

Funding

Ministry of Science and Higher Education of the Russian Federation 2021Russian Foundation for Basic Research 18-29-13006Russian Science Foundation 19-14-00164
6 · The paper itself

Abstract

Among industrially important pyridoxal-5'-phosphate (PLP)-dependent transaminases of fold type IV D-amino acid transaminases are the least studied. However, the development of cascade enzymatic processes, including the synthesis of D-amino acids, renewed interest in their study. Here, we describe the identification, biochemical and structural characterization of a new D-amino acid transaminase from

Indexed as

Amino AcidsBacterial ProteinsBacteroidetesCatalytic DomainCrystallography, X-RayModels, MolecularPyridoxal PhosphateSubstrate SpecificityTransaminasesAmino AcidsBacterial ProteinsPyridoxal PhosphateTransaminasesarginine residuesD-amino acid transaminaseenzyme catalysissequence-structure-function relationshipssubstrate specificityX-ray analysis

Identifiers

PMID34443642
PMCPMC8401098
OpenAlexW3195680870

What OpenQuestion holds

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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.