ArticleJournal of microbiology (Seoul, Korea)2009
Molecular cloning of the phospholipase D gene from Streptomyces sp. YU100 and its expression in Escherichia coli.
Article in Journal of microbiology (Seoul, Korea), 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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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.
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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.
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Who cites it
4 citing papers in PubMed, 18 citations in OpenAlex.
- A New Phospholipase D-Producing Bacillus cereus: Taxonomy, Mutagenesis, Fermentation Optimization and Enzyme Characterization.Applied biochemistry and biotechnology · 2025Article
- Acyl Chain Specificity of MarineInternational journal of molecular sciences · 2021Article
- Cardiolipin synthetase is involved in antagonistic interaction (reverse CAMP phenomenon) of Mycoplasma species with Staphylococcus aureus beta-hemolysis.Journal of clinical microbiology · 2014Article
- Phospholipase D: enzymology, functionality, and chemical modulation.Chemical reviews · 2011Review
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The gene for phospholipase D (PLD) of Streptomyces sp. YU100 was cloned from lambda phage library and heterologously expressed in Escherichia coli. Using an amplified gene fragment based on the consensus sequences of streptomycetes PLDs, lambda phage library of Streptomyces sp. YU100 chromosomal DNA was screened. The sequencing result of BamHI-digested 3.8 kb fragment in a positive phage clone revealed the presence of an open reading frame of a full sequence of PLD gene encoding a 540-amino acid protein including 33-amino acid signal peptide. The deduced amino acid sequence showed a high homology with other Streptomyces PLDs, having the highly conserved 'HKD' motifs. The PLD gene excluding signal peptide sequence was amplified and subcloned into a pET-32b(+) expression vector in E. coli BL21(DE3). The recombinant PLD was purified by nickel affinity chromatography and compared the enzyme activity with wild-type PLD. The results imply that the recombinant PLD produced by E. coli had the nearly same enzyme activity as PLD from Streptomyces sp. YU100.
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Registered trials
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