Evidence map›Paper›PMID 26798500›Full record

ArticleActa naturae

Sulfoxides, Analogues of L-Methionine and L-Cysteine As Pro-Drugs against Gram-Positive and Gram-Negative Bacteria.

N V Anufrieva, E A Morozova, V V Kulikova, N P Bazhulina, I V Manukhov, D I Degtev, E Yu Gnuchikh, A N Rodionov, G B Zavilgelsky, T V Demidkina

Open access · hybridAbstract read
In one paragraph

Article in Acta naturae. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
4.7field-weighted citation impact, top 6% 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

11 citing papers in PubMed, 35 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Review
  6. An unusual bidentate methionine ruthenium(II) complex: photo-uncaging and antimicrobial activity.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2020
    Article
  7. Review
  8. Article
  9. Article
  10. Structure of methionine γ-lyase from Clostridium sporogenes.Acta crystallographica. Section F, Structural biology communications · 2016
    Article
  11. 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

10 authors at 2 institutions in 1 country.

N V AnufrievaEngelhardt Institute of Molecular Biology, Russian Academy of Sciences, Vavilova Str., 32, Moscow, 119991, Russia.
E A MorozovaEngelhardt Institute of Molecular Biology, Russian Academy of Sciences, Vavilova Str., 32, Moscow, 119991, Russia.
V V KulikovaEngelhardt Institute of Molecular Biology, Russian Academy of Sciences, Vavilova Str., 32, Moscow, 119991, Russia.
N P BazhulinaEngelhardt Institute of Molecular Biology, Russian Academy of Sciences, Vavilova Str., 32, Moscow, 119991, Russia.
I V ManukhovState Research Institute of Genetics and Selection of Industrial Microorganisms, 1-st Dorozhniy pr., 1 , Moscow, 117545, Russia.
D I DegtevState Research Institute of Genetics and Selection of Industrial Microorganisms, 1-st Dorozhniy pr., 1 , Moscow, 117545, Russia.
E Yu GnuchikhState Research Institute of Genetics and Selection of Industrial Microorganisms, 1-st Dorozhniy pr., 1 , Moscow, 117545, Russia.
A N RodionovEngelhardt Institute of Molecular Biology, Russian Academy of Sciences, Vavilova Str., 32, Moscow, 119991, Russia.
G B ZavilgelskyState Research Institute of Genetics and Selection of Industrial Microorganisms, 1-st Dorozhniy pr., 1 , Moscow, 117545, Russia.
T V DemidkinaEngelhardt Institute of Molecular Biology, Russian Academy of Sciences, Vavilova Str., 32, Moscow, 119991, Russia.
Engelhardt Institute of Molecular Biology · RUGenetika · RU

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The problem of resistance to antibiotics requires the development of new classes of broad-spectrum antimicrobial drugs. The concept of pro-drugs allows researchers to look for new approaches to obtain effective drugs with improved pharmacokinetic and pharmacodynamic properties. Thiosulfinates, formed enzymatically from amino acid sulfoxides upon crushing cells of genus Allium plants, are known as antimicrobial compounds. The instability and high reactivity of thiosulfinates complicate their use as individual antimicrobial compounds. We propose a pharmacologically complementary pair: an amino acid sulfoxide pro-drug and vitamin B6 - dependent methionine γ-lyase, which metabolizes it in the patient's body. The enzyme catalyzes the γ- and β-elimination reactions of sulfoxides, analogues of L-methionine and L-cysteine, which leads to the formation of thiosulfinates. In the present work, we cloned the enzyme gene from Clostridium sporogenes. Ionic and tautomeric forms of the internal aldimine were determined by lognormal deconvolution of the holoenzyme spectrum and the catalytic parameters of the recombinant enzyme in the γ- and β-elimination reactions of amino acids, and some sulfoxides of amino acids were obtained. For the first time, the possibility of usage of the enzyme for effective conversion of sulfoxides was established and the antimicrobial activity of thiosulfinates against Gram-negative and Gram-positive bacteria in situ was shown.

Indexed as

allicinalliincloning of Clostridium sporogenes methionine γ-lyase geneGram-positive and Gram-negative bacteriaPro-drugssulfoxides of amino acidsvitamin B6-dependent enzymes

Identifiers

PMID26798500
PMCPMC4717258
OpenAlexW2411911916

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.