{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Fellner M"],"funding":["Marsden Fund","University of Otago","New Zealand Synchrotron Group Ltd","Health Research Council of New Zealand"],"pagination":["2119-2132"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC10644348"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["9(11)"],"pubmed_abstract":["The development of new treatment options for bacterial infections requires access to new targets for antibiotics and antivirulence strategies. Chemoproteomic approaches are powerful tools for profiling and identifying novel druggable target candidates, but their functions often remain uncharacterized. Previously, we used activity-based protein profiling in the opportunistic pathogen <i>Staphylococcus aureus</i> to identify active serine hydrolases termed fluorophosphonate-binding hydrolases (Fph). Here, we provide the first characterization of <i>S. aureus</i> FphH, a conserved, putative carboxylesterase (referred to as <i>yva</i>K in <i>Bacillus subtilis</i>) at the molecular and cellular level. First, phenotypic characterization of <i>fph</i>H-deficient transposon mutants revealed phenot"],"journal":["ACS infectious diseases"],"pubmed_title":["Biochemical and Cellular Characterization of the Function of Fluorophosphonate-Binding Hydrolase H (FphH) in <i>Staphylococcus aureus</i> Support a Role in Bacterial Stress Response."],"pmcid":["PMC10644348"],"funding_grant_id":["23/200/A","MFP-UOO2201"],"pubmed_authors":["Tan EW","Walsh A","Sutherland B","Dela Ahator S","van der Stelt M","Martin NI","Lentz CS","Bakker AT","Aftab N","Fellner M"],"additional_accession":[]},"is_claimable":false,"name":"Biochemical and Cellular Characterization of the Function of Fluorophosphonate-Binding Hydrolase H (FphH) in <i>Staphylococcus aureus</i> Support a Role in Bacterial Stress Response.","description":"The development of new treatment options for bacterial infections requires access to new targets for antibiotics and antivirulence strategies. Chemoproteomic approaches are powerful tools for profiling and identifying novel druggable target candidates, but their functions often remain uncharacterized. Previously, we used activity-based protein profiling in the opportunistic pathogen <i>Staphylococcus aureus</i> to identify active serine hydrolases termed fluorophosphonate-binding hydrolases (Fph). Here, we provide the first characterization of <i>S. aureus</i> FphH, a conserved, putative carboxylesterase (referred to as <i>yva</i>K in <i>Bacillus subtilis</i>) at the molecular and cellular level. First, phenotypic characterization of <i>fph</i>H-deficient transposon mutants revealed phenot","dates":{"release":"2023-01-01T00:00:00Z","publication":"2023 Nov","modification":"2026-05-28T14:45:51.647Z","creation":"2024-11-07T13:54:19.685Z"},"accession":"S-EPMC10644348","cross_references":{"pubmed":["37824340"],"doi":["10.1021/acsinfecdis.3c00246"]}}