Identification of putative multifunctional peptide synthetase genes using highly conserved oligonucleotide sequences derived from known synthetases
Author:
Publisher
Oxford University Press (OUP)
Subject
Genetics,Molecular Biology,Microbiology
Link
http://academic.oup.com/femsle/article-pdf/92/2/175/19091429/92-2-175.pdf
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1. Gramicidin S biosynthesis operon containing the structural genes grsA and grsB has an open reading frame encoding a protein homologous to fatty acid thioesterases
2. Complete nucleotide sequence of the tycA gene coding the tyrocidine synthetase 1 fromBacillus brevis
3. Delta-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine synthetase from Aspergillus nidulans. Molecular characterization of the acvA gene encoding the first enzyme of the penicillin biosynthetic pathway
4. The multifunctional peptide synthetase performing the first step of penicillin biosynthesis in Penicillium chrysogenum is a 421,073 dalton protein similar to Bacillus brevis peptide antibiotic synthetases.
5. The cephamycin biosynthetic genes pcbAB, encoding a large multidomain peptide synthetase, and pcbC of Nocardia lactamdurans are clustered together in an organization different from the same genes in Acremonium chrysogenum and Penicillium chrysogenum
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