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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.

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PubMed ID:: 17586635

PMC ID:: 1951892

DOI:: 10.1128/JB.00457-07

ScienceOpen disciplines: Chemistry

Keywords: Anti-Bacterial Agents,biosynthesis,Bacterial Proteins,genetics,metabolism,Betaproteobacteria,enzymology,Carbon-Nitrogen Ligases,Cyclic AMP,DNA, Bacterial,chemistry,DNA, Ribosomal,Enzyme Activation,Molecular Sequence Data,RNA, Ribosomal, 16S,Sequence Analysis, DNA

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ScienceOpen disciplines: Chemistry

Keywords: Anti-Bacterial Agents, biosynthesis, Bacterial Proteins, genetics, metabolism, Betaproteobacteria, enzymology, Carbon-Nitrogen Ligases, Cyclic AMP, DNA, Bacterial, chemistry, DNA, Ribosomal, Enzyme Activation, Molecular Sequence Data, RNA, Ribosomal, 16S, Sequence Analysis, DNA

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

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