{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"volume":["7(9)"],"submitter":["Schmidl SR"],"pubmed_abstract":["Mycoplasma pneumoniae is a causative agent of atypical pneumonia. The formation of hydrogen peroxide, a product of glycerol metabolism, is essential for host cell cytotoxicity. Phosphatidylcholine is the major carbon source available on lung epithelia, and its utilization requires the cleavage of deacylated phospholipids to glycerol-3-phosphate and choline. M. pneumoniae possesses two potential glycerophosphodiesterases, MPN420 (GlpQ) and MPN566. In this work, the function of these proteins was analyzed by biochemical, genetic, and physiological studies. The results indicate that only GlpQ is an active glycerophosphodiesterase. MPN566 has no enzymatic activity as glycerophosphodiesterase and the inactivation of the gene did not result in any detectable phenotype. Inactivation of the glpQ g"],"journal":["PLoS pathogens"],"pagination":["e1002263"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC3178575"],"repository":["biostudies-literature"],"pubmed_title":["A trigger enzyme in Mycoplasma pneumoniae: impact of the glycerophosphodiesterase GlpQ on virulence and gene expression."],"pmcid":["PMC3178575"],"pubmed_authors":["Busse J","Becher D","Stulke J","Schmidl SR","Otto A","Lluch-Senar M","Pinol J"],"additional_accession":[]},"is_claimable":false,"name":"A trigger enzyme in Mycoplasma pneumoniae: impact of the glycerophosphodiesterase GlpQ on virulence and gene expression.","description":"Mycoplasma pneumoniae is a causative agent of atypical pneumonia. The formation of hydrogen peroxide, a product of glycerol metabolism, is essential for host cell cytotoxicity. Phosphatidylcholine is the major carbon source available on lung epithelia, and its utilization requires the cleavage of deacylated phospholipids to glycerol-3-phosphate and choline. M. pneumoniae possesses two potential glycerophosphodiesterases, MPN420 (GlpQ) and MPN566. In this work, the function of these proteins was analyzed by biochemical, genetic, and physiological studies. The results indicate that only GlpQ is an active glycerophosphodiesterase. MPN566 has no enzymatic activity as glycerophosphodiesterase and the inactivation of the gene did not result in any detectable phenotype. Inactivation of the glpQ g","dates":{"release":"2011-01-01T00:00:00Z","publication":"2011 Sep","modification":"2026-04-15T13:11:57.672Z","creation":"2019-03-27T00:44:13Z"},"accession":"S-EPMC3178575","cross_references":{"pubmed":["21966272"],"doi":["10.1371/journal.ppat.1002263"]}}