Evidence map›Paper›PMID 31199579›Full record

ArticleMicrobial biotechnology2019

Chimeric 6-methylsalicylic acid synthase with domains of acyl carrier protein and methyltransferase from Pseudallescheria boydii shows novel biosynthetic activity.

Ji-Long Liao, Ka-Lai Pang, Guang-Huan Sun, Tun-Wen Pai, Pang-Hung Hsu, Jyuan-Siou Lin, Kuang-Hui Sun, Chii-Cheng Hsieh, Shye-Jye Tang

Open access · goldAbstract read
In one paragraph

Article in Microbial biotechnology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing papers in PubMed
0.7field-weighted citation impact, top 29% 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

6 citing papers in PubMed, 5 citations in OpenAlex.

  1. Article
  2. Review
  3. Review
  4. Article
  5. Synthetic biology enabling access to designer polyketides.Current opinion in chemical biology · 2020
    Review
  6. 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

9 authors at 4 institutions in 1 country.

Ji-Long LiaoDepartment of Bioscience and Biotechnology, Center of Excellence for the Oceans, National Taiwan Ocean University, No. 2 Pei-Ning Road, Keelung, 20224, Taiwan.
Ka-Lai PangDepartment of Marine Biology, Center of Excellence for the Oceans, National Taiwan Ocean University, No. 2 Pei-Ning Road, Keelung, 20224, Taiwan.
Guang-Huan SunDivision of Urology, Department of Surgery, National Defense Medical Center, Tri-Service General Hospital, No. 325, Sec. 2, Cheng-gong Rd., Taipei, Taiwan.
Tun-Wen PaiDepartment of Computer Science and Engineering, National Taiwan Ocean University, No. 2 Pei-Ning Road, Keelung, 20224, Taiwan.
Pang-Hung HsuDepartment of Bioscience and Biotechnology, Center of Excellence for the Oceans, National Taiwan Ocean University, No. 2 Pei-Ning Road, Keelung, 20224, Taiwan.
Jyuan-Siou LinDepartment of Bioscience and Biotechnology, Center of Excellence for the Oceans, National Taiwan Ocean University, No. 2 Pei-Ning Road, Keelung, 20224, Taiwan.
Kuang-Hui SunDepartment of Biotechnology and Laboratory Science in Medicine, National Yang-Ming University, No. 155, Sec. 2, Linong Street, Taipei, Taiwan.
Chii-Cheng HsiehSection of Urology, Cheng-Hsin General Hospital, Taipei, 11211, Taiwan.
Shye-Jye TangDepartment of Bioscience and Biotechnology, Center of Excellence for the Oceans, National Taiwan Ocean University, No. 2 Pei-Ning Road, Keelung, 20224, Taiwan.ORCID 0000-0002-4828-7456
National Taiwan Ocean University · TWCheng Hsin General Hospital · TWNational Yang Ming Chiao Tung University · TWTri-Service General Hospital · TW

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Polyketides are important secondary metabolites, many of which exhibit potent pharmacological applications. Biosynthesis of polyketides is carried out by a single polyketide synthase (PKS) or multiple PKSs in successive elongations of enzyme-bound intermediates related to fatty acid biosynthesis. The polyketide gene PKS306 from Pseudallescheria boydii NTOU2362 containing domains of ketosynthase (KS), acyltransferase (AT), dehydratase (DH), acyl carrier protein (ACP) and methyltransferase (MT) was cloned in an attempt to produce novel chemical compounds, and this PKS harbouring green fluorescent protein (GFP) was expressed in Saccharomyces cerevisiae. Although fluorescence of GFP and fusion protein analysed by anti-GFP antibody were observed, no novel compound was detected. 6-methylsalicylic acid synthase (6MSAS) was then used as a template and engineered with PKS306 by combinatorial fusion. The chimeric PKS containing domains of KS, AT, DH and ketoreductase (KR) from 6MSAS with ACP and MT from PKS306 demonstrated biosynthesis of a novel compound. The compound was identified with a deduced chemical formula of C

Indexed as

Acyl Carrier ProteinAcyltransferasesCloning, MolecularGene ExpressionLigasesMethyltransferasesMultienzyme ComplexesOxidoreductasesPolyketidesPolyketide SynthasesPseudallescheriaRecombinant Fusion ProteinsSaccharomyces cerevisiae6-methylsalicylic acid synthetaseAcyl Carrier ProteinAcyltransferasesLigasesMethyltransferasesMultienzyme ComplexesOxidoreductasesPolyketidesPolyketide SynthasesRecombinant Fusion Proteins

Identifiers

PMID31199579
PMCPMC6681407
OpenAlexW2949931089

What OpenQuestion holds

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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.