Evidence map›Paper›PMID 25373400›Full record

ArticleScientific reports2014

Reconstruction of lactate utilization system in Pseudomonas putida KT2440: a novel biocatalyst for l-2-hydroxy-carboxylate production.

Yujiao Wang, Min Lv, Yingxin Zhang, Xieyue Xiao, Tianyi Jiang, Wen Zhang, Chunhui Hu, Chao Gao, Cuiqing Ma, Ping Xu

Abstract read
In one paragraph

Article in Scientific reports, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
–field-weighted citation impact
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

4 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. 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.

Yujiao WangState Key Laboratory of Microbial Technology, Shandong University, Jinan 250100, People's Republic of China.
Min LvState Key Laboratory of Microbial Technology, Shandong University, Jinan 250100, People's Republic of China.
Yingxin ZhangState Key Laboratory of Microbial Technology, Shandong University, Jinan 250100, People's Republic of China.
Xieyue XiaoState Key Laboratory of Microbial Technology, Shandong University, Jinan 250100, People's Republic of China.
Tianyi JiangState Key Laboratory of Microbial Technology, Shandong University, Jinan 250100, People's Republic of China.
Wen ZhangState Key Laboratory of Microbial Technology, Shandong University, Jinan 250100, People's Republic of China.
Chunhui HuState Key Laboratory of Microbial Technology, Shandong University, Jinan 250100, People's Republic of China.
Chao GaoState Key Laboratory of Microbial Technology, Shandong University, Jinan 250100, People's Republic of China.
Cuiqing MaState Key Laboratory of Microbial Technology, Shandong University, Jinan 250100, People's Republic of China.
Ping Xu1] State Key Laboratory of Microbial Technology, Shandong University, Jinan 250100, People's Republic of China [2] State Key Laboratory of Microbial Metabolism, Shanghai Jiao Tong University, Shanghai 200240, People's Republic of China.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

As an important method for building blocks synthesis, whole cell biocatalysis is hindered by some shortcomings such as unpredictability of reactions, utilization of opportunistic pathogen, and side reactions. Due to its biological and extensively studied genetic background, Pseudomonas putida KT2440 is viewed as a promising host for construction of efficient biocatalysts. After analysis and reconstruction of the lactate utilization system in the P. putida strain, a novel biocatalyst that only exhibited NAD-independent D-lactate dehydrogenase activity was prepared and used in L-2-hydroxy-carboxylates production. Since the side reaction catalyzed by the NAD-independent L-lactate dehydrogenase was eliminated in whole cells of recombinant P. putida KT2440, two important L-2-hydroxy-carboxylates (L-lactate and L-2-hydroxybutyrate) were produced in high yield and high optical purity by kinetic resolution of racemic 2-hydroxy carboxylic acids. The results highlight the promise in biocatalysis by the biotechnologically important organism P. putida KT2440 through genomic analysis and recombination.

Indexed as

Gene Expression Regulation, BacterialBacterial ProteinsBiocatalysisHydroxybutyratesKineticsLactate DehydrogenasesLactatesL-Lactate DehydrogenaseMetabolic EngineeringOperonPseudomonas putidaStereoisomerism2-hydroxybutyric acidBacterial ProteinsD-lactate dehydrogenaseHydroxybutyratesLactate DehydrogenasesLactatesL-Lactate Dehydrogenase

Identifiers

PMID25373400
PMCPMC4221787

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.