Cloning and characterization of a phosphopantetheinyl transferase from Streptomyces verticillus ATCC15003, the producer of the hybrid peptide–polyketide antitumor drug bleomycin
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- 作者：Sí ; a Funcional e Instituto Universitario de Oncologí ; a ; Universidad de Oviedo ; 33006 Oviedo ; Spain. ; Cé ; sar ; et. al.
- 关键词：Phosphopantetheinyl transferase ; Bleomycin ; Acyl carrier protein ; Peptidyl carrier protein ; Streptomyces verticillus ; ACP ; acyl carrier protein ; ArCP ; aryl carrier protein ; BLM ; bleomycin ; CoA ; coenzyme A ; FAS ; fatty acid synthase ; MW ; molecular weight ; M
- 刊名：Chemistry & Biology
- 出版年：2001
- 出版时间：July, 2001
- 年：2001
- 卷：8
- 期：7
- 页码：725-738
- 全文大小：801 K
文摘
Background: Phosphopantetheinyl transferases (PPTases) catalyze the posttranslational modification of carrier proteins by the covalent attachment of the 4′-phosphopantetheine (P-pant) moiety of coenzyme A to a conserved serine residue, a reaction absolutely required for the biosynthesis of natural products including fatty acids, polyketides, and nonribosomal peptides. PPTases have been classified according to their carrier protein specificity. In organisms containing multiple P-pant-requiring pathways, each pathway has been suggested to have its own PPTase activity. However, sequence analysis of the bleomycin biosynthetic gene cluster in Streptomyces verticillus ATCC15003 failed to reveal an associated PPTase gene.