Evidence map›Paper›PMID 31482467›Full record

ArticleMolecular biotechnology2019

Heterologous Expression of Sfp-Type Phosphopantetheinyl Transferase is Indispensable in the Biosynthesis of Lipopeptide Biosurfactant.

Abdullahi Adekilekun Jimoh, Johnson Lin

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Article in Molecular biotechnology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
0.6field-weighted citation impact, top 36% 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

2 citing papers in PubMed, 13 citations in OpenAlex.

  1. Review
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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

2 authors at 1 institution in 1 country.

Abdullahi Adekilekun JimohDiscipline of Microbiology, School of Life Sciences, College of Agriculture, Engineering, and Science, University of KwaZulu-Natal (Westville), Private Bag X 54001, Durban, 4000, South Africa. jimohabdullahi1@gmail.com.
Johnson LinDiscipline of Microbiology, School of Life Sciences, College of Agriculture, Engineering, and Science, University of KwaZulu-Natal (Westville), Private Bag X 54001, Durban, 4000, South Africa.
University of KwaZulu-Natal · ZA

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Phosphopantetheinyl transferases are of tremendous enthusiasm inferable from their fundamental parts in activating polyketide, fatty acid, and non-ribosomal peptide synthetase enzymes and additionally an increasing number of biotechnological applications. The present study reports the identification of sfp gene from the Paenibacillus sp. D9, which encompasses 693 bp encoding a 230-amino acid protein with a molecular weight of 25.3 kDa. The amino acid sequence Paenibacillus sp. D9 Sfp revealed more than 90% sequence identity to other Sfp proteins from other Paenibacillus. The sfp gene was cloned and recovered efficiently using affinity chromatography with maximal specific phosphopantetheinyl transferase activity at an optimal pH of 8.0 and temperature of 30 °C. The enzyme also exhibited stability under a wide-ranging pH and temperature. The presence of Zn

Indexed as

Amino Acid SequenceBacterial ProteinsBiotechnologyCloning, MolecularEnzyme StabilityEscherichia coliEsterasesKineticsLipopeptidesMetals, HeavyPaenibacillusPeptide SynthasesPhylogenySurface-Active AgentsTransferases (Other Substituted Phosphate Groups)Bacterial ProteinsEsterasesLipopeptidesMetals, Heavynon-ribosomal peptide synthasePeptide Synthasesphosphopantetheinyl transferaseSurface-Active AgentsTransferases (Other Substituted Phosphate Groups)BiosurfactantCloned recombinantEsterasePaenibacillus sp. D9Phosphopantetheinyl transferase

Identifiers

PMID31482467
OpenAlexW2971468057

What OpenQuestion holds

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Registered trials

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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.