A one-pot chemoenzymatic synthesis for the universal precursor of antidiabetes and antiviral bis-indolylquinones. Export

@article{citeulike:2909577, abstract = {Bis-indolylquinones represent a class of fungal natural products that display antiretroviral, antidiabetes, or cytotoxic bioactivities. Recent advances in Aspergillus genomic mining efforts have led to the discovery of the tdiA-E-gene cluster, which is the first genetic locus dedicated to bis-indolylquinone biosynthesis. We have now genetically and biochemically characterized the enzymes TdiA (bis-indolylquinone synthetase) and TdiD (L-tryptophan:phenylpyruvate aminotransferase), which, together, confer biosynthetic abilities for didemethylasterriquinone D to Aspergillus nidulans. This compound is the universal intermediate for all bis-indolylquinones. In this biochemical study of a bis-indolylquinone synthetase and a fungal natural product transaminase, we present a one-pot chemoenzymatic protocol to generate didemethylasterriquinone D in vitro. As TdiA resembles a nonribosomal peptide synthetase, yet catalyzes carbon-carbon-bond formation, we discuss the implications for peptide synthetase chemistry.}, address = {Pharmaceutical Biology and Biotechnology, Albert-Ludwigs-Universit\"{a}t, Stefan-Meier-Strasse 19, 79104 Freiburg, Germany.}, author = {Schneider, P. and Weber, M. and Rosenberger, K. and Hoffmeister, D.}, citeulike-article-id = {2909577}, citeulike-linkout-0 = {http://dx.doi.org/10.1016/j.chembiol.2007.05.005}, citeulike-linkout-1 = {http://view.ncbi.nlm.nih.gov/pubmed/17584611}, citeulike-linkout-2 = {http://www.hubmed.org/display.cgi?uids=17584611}, doi = {10.1016/j.chembiol.2007.05.005}, issn = {1074-5521}, journal = {Chemistry \& biology}, keywords = {biocatalysis, chemoenzymatic, pptase}, month = {June}, number = {6}, pages = {635--644}, posted-at = {2008-06-20 09:48:15}, priority = {2}, title = {A one-pot chemoenzymatic synthesis for the universal precursor of antidiabetes and antiviral bis-indolylquinones.}, url = {http://dx.doi.org/10.1016/j.chembiol.2007.05.005}, volume = {14}, year = {2007} }

TY - JOUR ID - citeulike:2909577 L3 - citeulike-article-id:2909577 N2 - Bis-indolylquinones represent a class of fungal natural products that display antiretroviral, antidiabetes, or cytotoxic bioactivities. Recent advances in Aspergillus genomic mining efforts have led to the discovery of the tdiA-E-gene cluster, which is the first genetic locus dedicated to bis-indolylquinone biosynthesis. We have now genetically and biochemically characterized the enzymes TdiA (bis-indolylquinone synthetase) and TdiD (L-tryptophan:phenylpyruvate aminotransferase), which, together, confer biosynthetic abilities for didemethylasterriquinone D to Aspergillus nidulans. This compound is the universal intermediate for all bis-indolylquinones. In this biochemical study of a bis-indolylquinone synthetase and a fungal natural product transaminase, we present a one-pot chemoenzymatic protocol to generate didemethylasterriquinone D in vitro. As TdiA resembles a nonribosomal peptide synthetase, yet catalyzes carbon-carbon-bond formation, we discuss the implications for peptide synthetase chemistry. IS - 6 JF - Chemistry & biology SN - 1074-5521 AD - Pharmaceutical Biology and Biotechnology, Albert-Ludwigs-Universität, Stefan-Meier-Strasse 19, 79104 Freiburg, Germany. EP - 644 TI - A one-pot chemoenzymatic synthesis for the universal precursor of antidiabetes and antiviral bis-indolylquinones. VL - 14 SP - 635 KW - biocatalysis KW - chemoenzymatic KW - pptase AU - Schneider, P AU - Weber, M AU - Rosenberger, K AU - Hoffmeister, D PY - 2007/06// UR - http://dx.doi.org/10.1016/j.chembiol.2007.05.005 ER -