Evidence map›Paper›PMID 38265165›Full record

ArticleMicrobial biotechnology2024

Selective biosynthesis of a rhamnosyl nosiheptide by a novel bacterial rhamnosyltransferase.

Yali Du, Yuan Xia, Lingrui Wu, Lu Chen, Jiale Rong, Junting Fan, Yijun Chen, Xuri Wu

Open access · goldAbstract read
In one paragraph

Article in Microbial biotechnology, 2024. 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
1.3field-weighted citation impact, top 21% 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, 3 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

8 authors at 1 institution in 1 country.

Yali DuDepartment of Biochemistry, College of Life Sciences and Technology, China Pharmaceutical University, Nanjing, Jiangsu Province, China.
Yuan XiaDepartment of Biochemistry, College of Life Sciences and Technology, China Pharmaceutical University, Nanjing, Jiangsu Province, China.
Lingrui WuDepartment of Biochemistry, College of Life Sciences and Technology, China Pharmaceutical University, Nanjing, Jiangsu Province, China.
Lu ChenDepartment of Biochemistry, College of Life Sciences and Technology, China Pharmaceutical University, Nanjing, Jiangsu Province, China.
Jiale RongDepartment of Biochemistry, College of Life Sciences and Technology, China Pharmaceutical University, Nanjing, Jiangsu Province, China.
Junting FanDepartment of Pharmaceutical Analysis, School of Pharmacy, Nanjing Medical University, Nanjing, Jiangsu Province, China.
Yijun ChenLaboratory of Chemical Biology, College of Life Sciences and Technology, China Pharmaceutical University, Nanjing, Jiangsu Province, China.ORCID 0000-0002-4920-152X
Xuri WuDepartment of Biochemistry, College of Life Sciences and Technology, China Pharmaceutical University, Nanjing, Jiangsu Province, China.ORCID 0000-0002-0933-5902
China Pharmaceutical University · CN

Funding

"Double First-Class" University project CPU2022QZ08Key Research and Development Project of Guangdong Province 2022B1111070004National Innovation and Entrepreneurship Training Program for Undergraduate 202310316020ZNational Key Research and Development Program of China 2018YFA0902000National Natural Science Foundation of China 81973214
6 · The paper itself

Abstract

Nosiheptide (NOS) is a thiopeptide antibiotic produced by the bacterium Streptomyces actuosus. The hydroxyl group of 3-hydroxypyridine in NOS has been identified as a promising site for modification, which we therefore aimed to rhamnosylate. After screening, Streptomyces sp. 147326 was found to regioselectively attach a rhamnosyl unit to the 3-hydroxypyridine site in NOS, resulting in the formation of a derivative named NOS-R at a productivity of 24.6%. In comparison with NOS, NOS-R exhibited a 17.6-fold increase in aqueous solubility and a new protective effect against MRSA infection in mice, while maintaining a similar in vitro activity. Subsequently, SrGT822 was identified as the rhamnosyltransferase in Streptomyces sp. 147326 responsible for the biosynthesis of NOS-R using dTDP-L-rhamnose. SrGT822 demonstrated an optimal reaction pH of 10.0 and temperature of 55°C, which resulted in a NOS-R yield of 74.9%. Based on the catalytic properties and evolutionary analysis, SrGT822 is anticipated to be a potential rhamnosyltransferase for use in the modification of various complex scaffolds.

Indexed as

Anti-Bacterial AgentsThiazolesAnimalsMiceAnti-Bacterial AgentsnosiheptideThiazoles

Identifiers

PMID38265165
PMCPMC10832541
OpenAlexW4391174255

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.