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  1. Azila N, Othman I
    Biochem. Int., 1990;20(2):291-9.
    PMID: 1969267
    An extract prepared from the tentacle of Catostylus mosaicus was shown to lyse erythrocytes from rat, rabbit and human to a different extent; those from the rat being most susceptible followed by those from rabbit and human. The haemolytic activity was dependent on the concentration of crude extract protein exhibiting a sigmoidal curve. Only 60% of the haemolytic activity was retained after treament with heat and proteolytic enzyme. The extract was devoid of hydrolytic enzymes normally present in venoms except for phospholipase A activity, which resulted in the hydrolysis of membrane phospholipids with concomittant appearance of their lyso-derivatives.
    Matched MeSH terms: Membrane Lipids/metabolism
  2. Khalifa M, Few LL, See Too WC
    Biomed Res Int, 2020;2020:1823485.
    PMID: 32695809 DOI: 10.1155/2020/1823485
    Novel antimicrobial agents are crucial to combat antibiotic resistance in pathogenic bacteria. Choline kinase (ChoK) in bacteria catalyzes the synthesis of phosphorylcholine, which is subsequently incorporated into the cell wall or outer membrane. In certain species of bacteria, phosphorylcholine is also used to synthesize membrane phosphatidylcholine. Numerous human ChoK inhibitors (ChoKIs) have been synthesized and tested for anticancer properties. Inhibition of S. pneumoniae ChoK by human ChoKIs showed a promising effect by distorting the cell wall and retarded the growth of this pathogen. Comparison of amino acid sequences at the catalytic sites of putative choline kinases from pathogenic bacteria and human enzymes revealed striking sequence conservation that supports the potential application of currently available ChoKIs for inhibiting bacterial enzymes. We also propose the combined use of ChoKIs and nanoparticles for targeted delivery to the pathogen while shielding the human host from any possible side effects of the inhibitors. More research should focus on the verification of putative bacterial ChoK activities and the characterization of ChoKIs with active enzymes. In conclusion, the presence of ChoK in a wide range of pathogenic bacteria and the distinct function of this enzyme has made it an attractive drug target. This review highlighted the possibility of "choking" bacterial ChoKs by using human ChoKIs.
    Matched MeSH terms: Membrane Lipids/metabolism
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