Evidence map›Paper›PMID 32913258›Full record

ArticleScientific reports2020

Catalytic specificity of the Lactobacillus plantarum cystathionine γ-lyase presumed by the crystallographic analysis.

Yasuyuki Matoba, Masafumi Noda, Tomoki Yoshida, Kosuke Oda, Yuka Ezumi, Chiaki Yasutake, Hisae Izuhara-Kihara, Narandarai Danshiitsoodol, Takanori Kumagai, Masanori Sugiyama

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
2.6field-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

13 citing papers in PubMed, 27 citations in OpenAlex.

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  10. An insight into gut microbiota and metabolites in the mice with adenomyosis.Frontiers in cellular and infection microbiology · 2023
    Article
  11. Role of Hydrogen Sulfide in Oral Disease.Oxidative medicine and cellular longevity · 2022
    Review
  12. Review
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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

10 authors at 2 institutions in 1 country.

Yasuyuki MatobaFaculty of Pharmacy, Yasuda Women's University, Yasuhigashi 6-13-1, Asaminami-ku, Hiroshima, 731-0153, Japan. matoba@yasuda-u.ac.jp.
Masafumi NodaGraduate School of Biomedical and Health Sciences, Hiroshima University, Kasumi 1-2-3, Minami-ku, Hiroshima, 734-8551, Japan.
Tomoki YoshidaGraduate School of Biomedical and Health Sciences, Hiroshima University, Kasumi 1-2-3, Minami-ku, Hiroshima, 734-8551, Japan.
Kosuke OdaGraduate School of Biomedical and Health Sciences, Hiroshima University, Kasumi 1-2-3, Minami-ku, Hiroshima, 734-8551, Japan.
Yuka EzumiFaculty of Pharmacy, Yasuda Women's University, Yasuhigashi 6-13-1, Asaminami-ku, Hiroshima, 731-0153, Japan.
Chiaki YasutakeFaculty of Pharmaceutical Sciences, Hiroshima University, Kasumi 1-2-3, Minami-ku, Hiroshima, 734-8551, Japan.
Hisae Izuhara-KiharaGraduate School of Biomedical and Health Sciences, Hiroshima University, Kasumi 1-2-3, Minami-ku, Hiroshima, 734-8551, Japan.
Narandarai DanshiitsoodolGraduate School of Biomedical and Health Sciences, Hiroshima University, Kasumi 1-2-3, Minami-ku, Hiroshima, 734-8551, Japan.
Takanori KumagaiGraduate School of Biomedical and Health Sciences, Hiroshima University, Kasumi 1-2-3, Minami-ku, Hiroshima, 734-8551, Japan.
Masanori SugiyamaGraduate School of Biomedical and Health Sciences, Hiroshima University, Kasumi 1-2-3, Minami-ku, Hiroshima, 734-8551, Japan. sugi@hiroshima-u.ac.jp.
Hiroshima University · JPYasuda Women's University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The reverse transsulfuration pathway, which is composed of cystathionine β-synthase (CBS) and cystathionine γ-lyase (CGL), plays a role to synthesize L-cysteine using L-serine and the sulfur atom in L-methionine. A plant-derived lactic acid bacterium Lactobacillus plantarum SN35N has been previously found to harbor the gene cluster encoding the CBS- and CGL-like enzymes. In addition, it has been demonstrated that the L. plantarum CBS can synthesize cystathionine from O-acetyl-L-serine and L-homocysteine. The aim of this study is to characterize the enzymatic functions of the L. plantarum CGL. We have found that the enzyme has the high γ-lyase activity toward cystathionine to generate L-cysteine, together with the β-lyase activity toward L-cystine to generate L-cysteine persulfide. By the crystallographic analysis of the inactive CGL K194A mutant complexed with cystathionine, we have found the residues which recognize the distal amino and carboxyl groups of cystathionine or L-cystine. The PLP-bound substrates at the active site may take either the binding pose for the γ- or β-elimination reaction, with the former being the major reaction in the case of cystathionine.

Indexed as

CatalysisCrystallography, X-RayCystathionineCystathionine gamma-LyaseHomocysteineLactiplantibacillus plantarumSerineSubstrate SpecificityCystathionineCystathionine gamma-LyaseHomocysteineO-acetylserineSerine

Identifiers

PMID32913258
PMCPMC7483736
OpenAlexW3084057161

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.