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

ABSTRACT: The cyclic AMP (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, cAMP receptor protein. A 16S rRNA gene sequence found on the same environmental DNA cosmid as NasP is most closely related to 16S sequences from beta-proteobacteria.

SUBMITTER: Clardy J

PROVIDER: S-EPMC1951892 | biostudies-literature | 2007 Sep

REPOSITORIES: biostudies-literature

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

Clardy Jon J Brady Sean F SF

Journal of bacteriology 20070622 17

The cyclic AMP (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, cAMP receptor protein. A 16S rRNA gene sequence found on the same environmental DNA cosmid as NasP is most closely related to 16S sequences from beta-proteobacteria. ...[more]

PMID: 17586635

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