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.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Adenosine / chemistry*
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Adenosine / metabolism
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Benzophenones / chemistry
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Benzophenones / metabolism
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Catalytic Domain
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Click Chemistry
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Peptide Synthases / chemistry*
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Peptide Synthases / genetics
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Peptide Synthases / metabolism
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Proteomics*
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Recombinant Proteins / biosynthesis
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Recombinant Proteins / chemistry
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Recombinant Proteins / genetics
Substances
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Benzophenones
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Recombinant Proteins
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benzophenone
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Peptide Synthases
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non-ribosomal peptide synthase
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Adenosine