Cyclic AMP directly activates NasP, an N-acyl amino acid antibiotic biosynthetic enzyme cloned from an uncultured -Proteobacterium

Laboratory of Genetically Encoded Small Molecules, The Rockefeller University, 1230 York Avenue, New York, NY 10021; Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, 240 Longwood Ave., Boston, MA 02115

^* To whom correspondence should be addressed. Email: sbrady{at}rockefeller.edu.

	Abstract

The cAMP-dependent biosynthesis of N-acylphenylalanine antibiotics by NasP, an environmental DNA-derived N-acyl amino acid synthase, is controlled by an NasP associated cyclic nucleotide binding domain and is independent of the global cAMP signal transducer, CRP. A 16S rDNA sequence found on the same environmental DNA cosmid as NasP is most closely related to 16S sequences from -Proteobacteria.