Chemoproteomic identification of a DPP4 homolog in Bacteroides thetaiotaomicron

• Published in: Nature chemical biology Vol. 19; no. 12; pp. 1469 - 1479
• Main Authors: Keller, Laura J., Nguyen, Taylor H., Liu, Lawrence J., Hurysz, Brianna M., Lakemeyer, Markus, Guerra, Matteo, Gelsinger, Danielle J., Chanin, Rachael, Ngo, Nhi, Lum, Kenneth M., Faucher, Franco, Ipock, Phillip, Niphakis, Micah J., Bhatt, Ami S., O’Donoghue, Anthony J., Huang, Kerwyn Casey, Bogyo, Matthew
• Format: Journal Article
• Language: English
• Published: New York Nature Publishing Group US 01.12.2023; Nature Publishing Group
• Subjects: 631/114/129; 631/326/41; 631/92/475; 631/92/607/468; Bacteria; Bacteroides thetaiotaomicron; Biochemical Engineering; Biochemistry; Bioinformatics; Biology; Bioorganic Chemistry; Cell Biology; Chemistry; Chemistry and Materials Science; Chemistry/Food Science; Diabetes mellitus (non-insulin dependent); Diabetes Mellitus, Type 2; Dipeptidyl Peptidase 4 - genetics; Drugs; Enzymes; FDA approval; Homology; Humans; Integrity; Medicine; Metabolism; Metabolites; Microbiota; Peptidases; Peptides; Proteins; Proteolysis; Scaffolding; Serine

Serine hydrolases have important roles in signaling and human metabolism, yet little is known about their functions in gut commensal bacteria. Using bioinformatics and chemoproteomics, we identify serine hydrolases in the gut commensal Bacteroides thetaiotaomicron that are specific to the Bacteroide...