Evidence map›Paper›PMID 25239898›Full record

ArticleApplied and environmental microbiology2014

Cloning and Characterization of a Novel Esterase from Rhodococcus sp. for Highly Enantioselective Synthesis of a Chiral Cilastatin Precursor.

Yan Zhang, Jiang Pan, Zheng-Jiao Luan, Guo-Chao Xu, Sunghoon Park, Jian-He Xu

Open access · bronzeAbstract read
In one paragraph

Article in Applied and environmental microbiology, 2014. 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
0.7field-weighted citation impact, top 31% 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, 22 citations in OpenAlex.

  1. Article
  2. Article
  3. International journal of molecular sciences · 2019
    Review
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

6 authors at 2 institutions in 2 countries.

Yan ZhangState Key Laboratory of Bioreactor Engineering, East China University of Science and Technology, Shanghai, China.
Jiang PanState Key Laboratory of Bioreactor Engineering, East China University of Science and Technology, Shanghai, China.
Zheng-Jiao LuanState Key Laboratory of Bioreactor Engineering, East China University of Science and Technology, Shanghai, China.
Guo-Chao XuState Key Laboratory of Bioreactor Engineering, East China University of Science and Technology, Shanghai, China guochaoxu@163.com jianhexu@ecust.edu.cn.
Sunghoon ParkDepartment of Chemical and Biomolecular Engineering, Pusan National University, Busan, South Korea.
Jian-He XuState Key Laboratory of Bioreactor Engineering, East China University of Science and Technology, Shanghai, China guochaoxu@163.com jianhexu@ecust.edu.cn.
East China University of Science and Technology · CNPusan National University · KR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

A novel nonheme chloroperoxidase (RhEst1), with promiscuous esterase activity for enantioselective hydrolysis of ethyl (S)-2,2-dimethylcyclopropanecarboxylate, was identified from a shotgun library of Rhodococcus sp. strain ECU1013. RhEst1 was overexpressed in Escherichia coli BL21(DE3), purified to homogeneity, and functionally characterized. Fingerprinting analysis revealed that RhEst1 prefers para-nitrophenyl (pNP) esters of short-chain acyl groups. pNP esters with a cyclic acyl moiety, especially that with a cyclobutanyl group, were also substrates for RhEst1. The Km values for methyl 2,2-dimethylcyclopropanecarboxylate (DmCpCm) and ethyl 2,2-dimethylcyclopropane carboxylate (DmCpCe) were 0.25 and 0.43 mM, respectively. RhEst1 could serve as an efficient hydrolase for the bioproduction of optically pure (S)-2,2-dimethyl cyclopropane carboxylic acid (DmCpCa), which is an important chiral building block for cilastatin. As much as 0.5 M DmCpCe was enantioselectively hydrolyzed into (S)-DmCpCa, with a molar yield of 47.8% and an enantiomeric excess (ee) of 97.5%, indicating an extremely high enantioselectivity (E = 240) of this novel and unique biocatalyst for green manufacturing of highly valuable chiral chemicals.

Indexed as

Amino Acid SequenceChloride PeroxidaseCilastatinCloning, MolecularCluster AnalysisDNA, BacterialEscherichia coliGene ExpressionKineticsMolecular Sequence DataPhylogenyProtease InhibitorsRhodococcusSequence Analysis, DNASequence Homology, Amino AcidSubstrate SpecificityChloride PeroxidaseCilastatinDNA, BacterialProtease Inhibitors

Identifiers

PMID25239898
PMCPMC4249170
OpenAlexW1964974165

What OpenQuestion holds

Textmetadata
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.