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Active site-directed proteomic probes for adenylation domains in nonribosomal peptide synthetases.

ABSTRACT: We describe a general strategy for selective chemical labeling of individual adenylation (A) domains in nonribosomal peptide synthetases (NRPSs) using active site-directed proteomic probes coupled to the 5'-O-N-(aminoacyl)sulfamoyladenosine (AMS) scaffold with a clickable benzophenone functionality. These proteomic tools can greatly facilitate the molecular identification, functional characterization, and profiling of virtually any kind of A domains of NRPS enzymes in complex biological systems.

SUBMITTER: Konno S

PROVIDER: S-EPMC4795001 | biostudies-literature | 2015 Feb

REPOSITORIES: biostudies-literature

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Active site-directed proteomic probes for adenylation domains in nonribosomal peptide synthetases.

Konno Sho S Ishikawa Fumihiro F Suzuki Takehiro T Dohmae Naoshi N Burkart Michael D MD Kakeya Hideaki H

Chemical communications (Cambridge, England) 20150201 12

We describe a general strategy for selective chemical labeling of individual adenylation (A) domains in nonribosomal peptide synthetases (NRPSs) using active site-directed proteomic probes coupled to the 5'-O-N-(aminoacyl)sulfamoyladenosine (AMS) scaffold with a clickable benzophenone functionality. These proteomic tools can greatly facilitate the molecular identification, functional characterization, and profiling of virtually any kind of A domains of NRPS enzymes in complex biological systems. ...[more]

PMID: 25563804

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