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  3. Functional profiling of adenylation domains in nonribosomal peptide synthetases by competitive activity-based protein profiling

Functional profiling of adenylation domains in nonribosomal peptide synthetases by competitive activity-based protein profiling

  • Chem Commun (Camb). 2015 Nov 11;51(87):15764-7. doi: 10.1039/c5cc04953a.
Shota Kasai 1,  Sho Konno 1,  Fumihiro Ishikawa 1,  Hideaki Kakeya 1
Affiliations

Affiliation

  • 1 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.
PMID: 26365322 DOI: 10.1039/c5cc04953a
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.

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