title: Functional profiling of adenylation domains in nonribosomal peptide synthetases by competitive activity-based protein profiling.
abstract: We describe competitive activity-based protein profiling (ABPP) to accelerate the functional prediction and assessment of adenylation (A) domains in nonribosomal peptide synthetases (NRPSs) in proteomic environments. Using a library of sulfamoyloxy-linked aminoacyl-AMP analogs, the competitive ABPP technique offers a simple and rapid assay system for adenylating enzymes and provides insight into enzyme substrate candidates and enzyme active-site architecture.
authors.affiliation: Department of System Chemotherapy and Molecular Sciences, Division of Bioinformatics and Chemical Genomics, Graduate School of Pharmaceutical Sciences, Kyoto University, Sakyo, Kyoto 606-8501, Japan. fishika@pharm.kyoto-u.ac.jp scseigyo-hisyo@pharm.kyoto-u.ac.jp.
authors.forename: Shota
authors.initials: S
authors.lastname: Kasai
authors.affiliation: Department of System Chemotherapy and Molecular Sciences, Division of Bioinformatics and Chemical Genomics, Graduate School of Pharmaceutical Sciences, Kyoto University, Sakyo, Kyoto 606-8501, Japan. fishika@pharm.kyoto-u.ac.jp scseigyo-hisyo@pharm.kyoto-u.ac.jp.
authors.forename: Sho
authors.initials: S
authors.lastname: Konno
authors.affiliation: Department of System Chemotherapy and Molecular Sciences, Division of Bioinformatics and Chemical Genomics, Graduate School of Pharmaceutical Sciences, Kyoto University, Sakyo, Kyoto 606-8501, Japan. fishika@pharm.kyoto-u.ac.jp scseigyo-hisyo@pharm.kyoto-u.ac.jp.
authors.forename: Fumihiro
authors.initials: F
authors.lastname: Ishikawa
authors.affiliation: Department of System Chemotherapy and Molecular Sciences, Division of Bioinformatics and Chemical Genomics, Graduate School of Pharmaceutical Sciences, Kyoto University, Sakyo, Kyoto 606-8501, Japan. fishika@pharm.kyoto-u.ac.jp scseigyo-hisyo@pharm.kyoto-u.ac.jp.
authors.forename: Hideaki
authors.initials: H
authors.lastname: Kakeya
mesh_terms: D000249:Adenosine Monophosphate / Q000031:analogs & derivatives / Q000138:chemical synthesis; D000591:Amino Acid Isomerases / Q000037:antagonists & inhibitors; D056449:Bacillales; D020134:Catalytic Domain; D004791:Enzyme Inhibitors / Q000138:chemical synthesis; D007700:Kinetics; D015335:Molecular Probes / Q000138:chemical synthesis; D010453:Peptide Synthases / Q000032:analysis* / Q000737:chemistry; D040081:Protein Array Analysis; D017434:Protein Structure, Tertiary; D020543:Proteome; D013379:Substrate Specificity; D013449:Sulfonamides / Q000138:chemical synthesis
chemical_list: D004791:Enzyme Inhibitors; D015335:Molecular Probes; D020543:Proteome; D013449:Sulfonamides; D000249:Adenosine Monophosphate; D000591:Amino Acid Isomerases; D010453:Peptide Synthases; C035180:tyrocidine synthetase