Evidence map›Paper›PMID 32958806›Full record

ArticleScientific reports2020

Preparation of a whole cell catalyst overexpressing acetohydroxyacid synthase of Thermotoga maritima and its application in the syntheses of α-hydroxyketones.

Yan-Fei Liang, Le-Tian Yan, Qiao Yue, Ji-Kui Zhao, Cai-Yun Luo, Feng Gao, Heng Li, Wen-Yun Gao

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 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
0.4field-weighted citation impact, top 39% 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

1 citing paper in PubMed, 10 citations in OpenAlex.

  1. 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.

Yan-Fei LiangCollege of Life Sciences, Northwest University, 229 North Taibai Road, Xi'an, 710069, Shaanxi, People's Republic of China.
Le-Tian YanCollege of Life Sciences, Northwest University, 229 North Taibai Road, Xi'an, 710069, Shaanxi, People's Republic of China.
Qiao YueCollege of Life Sciences, Northwest University, 229 North Taibai Road, Xi'an, 710069, Shaanxi, People's Republic of China.
Ji-Kui ZhaoCollege of Life Sciences, Northwest University, 229 North Taibai Road, Xi'an, 710069, Shaanxi, People's Republic of China.
Cai-Yun LuoCollege of Life Sciences, Northwest University, 229 North Taibai Road, Xi'an, 710069, Shaanxi, People's Republic of China.
Feng GaoCollege of Life Sciences, Northwest University, 229 North Taibai Road, Xi'an, 710069, Shaanxi, People's Republic of China.
Heng LiCollege of Life Sciences, Northwest University, 229 North Taibai Road, Xi'an, 710069, Shaanxi, People's Republic of China. hengli@nwu.edu.cn.
Wen-Yun GaoCollege of Life Sciences, Northwest University, 229 North Taibai Road, Xi'an, 710069, Shaanxi, People's Republic of China. gaowenyun@nwu.edu.cn.
Northwest University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The large catalytic subunit of acetohydroxyacid synthase (AHAS, EC 2.2.1.6) of Thermotoga maritima (TmcAHAS) was prepared in this study. It possesses high specific activity and excellent stability. The protein and a whole cell catalyst overexpressing the protein were applied to the preparation of α-hydroxyketones including acetoin (AC), 3-hydroxy-2-pentanone (HP), and (R)-phenylacetylcarbinol (R-PAC). The results show that AC and HP could be produced in high yields (84% and 62%, respectively), while R-PAC could be synthesized in a high yield (about 78%) with an R/S ratio of 9:1. Therefore, TmcAHAS and the whole cell catalyst overexpressing the protein could be practically useful bio-catalysts in the preparation of α-hydroxyketones including AC, HP, and R-PAC. To the best of our knowledge, this is the first time that bacterial AHAS was used as a catalyst to prepare HP with a good yield, and also the first time that TmcAHAS was employed to synthesize AC and R-PAC.

Indexed as

Acetolactate SynthaseCatalysisCatalytic DomainKetonesRecombinant ProteinsThermotoga maritimaAcetolactate SynthaseKetonesRecombinant Proteins

Identifiers

PMID32958806
PMCPMC7505981
OpenAlexW3087763159

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.