title: Uncovering the Serine Hydrolytic Landscape of Mycobacterium tuberculosis.
abstract: In this issue of Cell Chemical Biology, Ortega et al. (2016) present a study utilizing a click-chemistry-enabled fluorophosphonate for activity-based identification of serine hydrolases, pinpointing a range of proteins including previously annotated hypotheticals. The application of this technology on both actively replicating and non-replicating Mycobacterium tuberculosis gives us a glimpse of its serine hydrolytic landscape during different stages of metabolic activity.
authors.affiliation: Tuberculosis Research Section, Laboratory of Clinical Infectious Diseases, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, MD 20892, USA. Electronic address: hboshoff@niaid.nih.gov.
authors.forename: Helena I
authors.initials: HI
authors.lastname: Boshoff
mesh_terms: D000995:Antitubercular Agents; D001426:Bacterial Proteins; D006867:Hydrolases / Q000378:metabolism; D006868:Hydrolysis; D009161:Mycobacterium / Q000378:metabolism; D020102:Mycobacterium smegmatis / Q000378:metabolism; D009169:Mycobacterium tuberculosis / Q000378:metabolism*; D009170:Nontuberculous Mycobacteria / Q000378:metabolism; D012694:Serine; D012697:Serine Endopeptidases; D051050:Serine O-Acetyltransferase; D057057:Serine Proteases; D015842:Serine Proteinase Inhibitors; D014376:Tuberculosis
chemical_list: D000995:Antitubercular Agents; D001426:Bacterial Proteins; D015842:Serine Proteinase Inhibitors; D012694:Serine; D051050:Serine O-Acetyltransferase; D006867:Hydrolases; D057057:Serine Proteases; D012697:Serine Endopeptidases