Cloning and location of a gene governing lysine epsilon-aminotransferase, an enzyme initiating beta-lactam biosynthesis in Streptomyces spp.
AUTOR(ES)
Madduri, K
RESUMO
In actinomycetes that produce beta-lactam antibiotics of the cephem type, lysine epsilon-aminotransferase is the initial enzyme in the conversion of lysine to alpha-aminoadipic acid. We used a two-stage process ("chromosome walking") to screen a lambda library of Streptomyces clavuligerus genomic DNA for fragments that expressed lysine epsilon-aminotransferase activity in S. lividans. Restriction analysis of the cloned DNA confirmed the location of the putative lat gene within the cluster of beta-lactam biosynthesis genes, roughly midway between pcbC, the structural gene for isopenicillin N synthetase, and the putative cefE gene encoding deacetoxycephalosporin C synthetase.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=207215Documentos Relacionados
- Lysine catabolism in Streptomyces spp. is primarily through cadaverine: beta-lactam producers also make alpha-aminoadipate.
- Beta-lactamases and detection of beta-lactam resistance in Enterobacter spp.
- L-lysine epsilon-aminotransferase involved in cephamycin C synthesis in Streptomyces lactamdurans.
- In vitro activities of new beta-lactam antibiotics against Acinetobacter spp.
- Localization of the lysine epsilon-aminotransferase (lat) and delta-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine synthetase (pcbAB) genes from Streptomyces clavuligerus and production of lysine epsilon-aminotransferase activity in Escherichia coli.
