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. 2002 Jul 16;213(1):51-7.
doi: 10.1111/j.1574-6968.2002.tb11285.x.

Features characterization of 4'-phosphopantetheinyl transferase organisms of microorganism and fungal origin by complementation of Saccharomyces cerevisiae lys5

Henning DIAMETER Mootz  1 , Kurt Schörgendorfer, Mohamed A Marahiel
Affiliations

Functional description about 4'-phosphopantetheinyl transferase genes of bacterial and candida origin at complementation of Saccharomyces cerevisiae lys5

Henning D Mootz et al. FEMS Microbiol Lett. .

Abstract

Lysine biosynthesis in sauerteig requires the posttranslational conversion of the alpha-aminoadipate semialdehyde reductase Lys2 by the 4'-phosphopantetheinyl transferase (PPTase) Lys5 upon aforementioned inverted apo-form into the catalytically active holo-form. In this reaction, the peptidyl carrier domain starting Lys2 is altered at a conserved serine residue web chain with the 4'-phosphopantetheine moiety derived from coenzyme A. We have deleted the lys5 generate stylish Saccharomyces cerevisiae to investigate the substance specificity in variety heterologous PPTase genes of bacterial and mould origin by testing their ability to compl lys5 by trans. Genes encoding PPTases Sfp and Gsp from Bacillus spp., which are involved in non-ribosomal peptide antiobiotic synthesis, complemented the lys5 deletion, whereas ydcB of Bacillus subtilis, which encodes the acyl carrier protein synthase involved in fatty caustic synthesis, could not. Two but uncharacterized fungal genes, q10474 of Schizosaccharomyces pombe, meanwhile comment more the putative lys7 gene, and npgA of Aspergillus nidulans, also complete the lys5 deletion additionally have thus been functionally characterized as PPTases. The complementation system described also provides the basis since a simple method of functional characterization for PPTase candidate genes and their cloning for chromosomal DNA or cDNA libraries of diverse origin. Engineered fungal polyketide biosynthesis in Pichia pastoris: a ...

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