Eine Semipinakol‐Umlagerung – katalysiert durch ein Enzymsystem mit difunktioneller FAD‐abhängiger Monooxygenase

[1]  Robert M. Williams,et al.  Biochemical characterization of NotB as an FAD-dependent oxidase in the biosynthesis of notoamide indole alkaloids. , 2012, Journal of the American Chemical Society.

[2]  Robert M. Williams,et al.  Study on the biosynthesis of the notoamides: Pinacol-type rearrangement of the isoprenyl unit in deoxybrevianamide E and 6-hydroxydeoxybrevianamide E. , 2011, Tetrahedron letters.

[3]  Y. Tu,et al.  Semipinacol rearrangement in natural product synthesis. , 2011, Chemical reviews.

[4]  R. Müller,et al.  AuaA, a Membrane‐Bound Farnesyltransferase from Stigmatella aurantiaca, Catalyzes the Prenylation of 2‐Methyl‐4‐hydroxyquinoline in the Biosynthesis of Aurachins , 2011, Chembiochem : a European journal of chemical biology.

[5]  R. Müller,et al.  Unprecedented anthranilate priming involving two enzymes of the acyl adenylating superfamily in aurachin biosynthesis. , 2011, Journal of the American Chemical Society.

[6]  R. Müller,et al.  Completing the puzzle of aurachin biosynthesis in Stigmatella aurantiaca Sg a15. , 2011, Molecular bioSystems.

[7]  K. Noguchi,et al.  Crystal structure of 1-deoxy-d-xylulose 5-phosphate reductoisomerase from the hyperthermophile Thermotoga maritima for insights into the coordination of conformational changes and an inhibitor binding. , 2010, Journal of structural biology.

[8]  B. Kunze,et al.  Biosynthesis of aurachins A-L in Stigmatella aurantiaca: a feeding study. , 2008, Journal of natural products.

[9]  G. Höfle,et al.  Isolation and biosynthesis of aurachin P and 5-nitroresorcinol from Stigmatella erecta. , 2008, Journal of natural products.

[10]  B. Kunze,et al.  Semisynthesis and antiplasmodial activity of the quinoline alkaloid aurachin E. , 2008, Journal of natural products.

[11]  B. Shen,et al.  Characterization of the two-component, FAD-dependent monooxygenase SgcC that requires carrier protein-tethered substrates for the biosynthesis of the enediyne antitumor antibiotic C-1027. , 2008, Journal of the American Chemical Society.

[12]  Gunter Schneider,et al.  Crystal structures of two aromatic hydroxylases involved in the early tailoring steps of angucycline biosynthesis. , 2007, Journal of molecular biology.

[13]  Jens Carlsson,et al.  Structures of Mycobacterium tuberculosis 1-Deoxy-D-xylulose-5-phosphate Reductoisomerase Provide New Insights into Catalysis* , 2007, Journal of Biological Chemistry.

[14]  E. Dittmann,et al.  Aurachin‐Biosynthese im Gram‐negativen Bakterium Stigmatella aurantiaca: Beteiligung einer Typ‐II‐Polyketidsynthase , 2007 .

[15]  Jeroen S. Dickschat,et al.  A Type II polyketide synthase from the gram-negative Bacterium Stigmatella aurantiaca is involved in Aurachin alkaloid biosynthesis. , 2007, Angewandte Chemie.

[16]  L. Guddat,et al.  Probing the mechanism of the bifunctional enzyme ketol‐acid reductoisomerase by site‐directed mutagenesis of the active site , 2005, The FEBS journal.

[17]  Shiou-Chuan Tsai,et al.  Structural Analysis of Actinorhodin Polyketide Ketoreductase: Cofactor Binding and Substrate Specificity , 2004, Biochemistry.

[18]  C Richard Hutchinson,et al.  A model of structure and catalysis for ketoreductase domains in modular polyketide synthases. , 2003, Biochemistry.

[19]  Shunji Takahashi,et al.  Characterization of 1-Deoxy-d-xylulose 5-Phosphate Reductoisomerase, an Enzyme Involved in Isopentenyl Diphosphate Biosynthesis, and Identification of Its Catalytic Amino Acid Residues* , 2000, The Journal of Biological Chemistry.

[20]  M. Eppink,et al.  Identification of a novel conserved sequence motif in flavoprotein hydroxylases with a putative dual function in FAD/NAD(P)H binding , 1997, Protein science : a publication of the Protein Society.

[21]  P. Rich,et al.  New inhibitors of the quinol oxidation sites of bacterial cytochromes bo and bd. , 1995, Biochemistry.

[22]  H. Reichenbach,et al.  Two binding sites of inhibitors in NADH: ubiquinone oxidoreductase (complex I). Relationship of one site with the ubiquinone-binding site of bacterial glucose:ubiquinone oxidoreductase. , 1994, European journal of biochemistry.

[23]  R. Dumas,et al.  Branched-chain-amino-acid biosynthesis in plants: molecular cloning and characterization of the gene encoding acetohydroxy acid isomeroreductase (ketol-acid reductoisomerase) from Arabidopsis thaliana (thale cress). , 1993, The Biochemical journal.

[24]  K. Calvo,et al.  The pH dependence of the kinetic parameters of ketol acid reductoisomerase indicates a proton shuttle mechanism for alkyl migration. , 1992, Archives of biochemistry and biophysics.

[25]  H. Reichenbach,et al.  The Aurachins, Naturally Occurring Inhibitors of Photosvnthetic Electron Flow through Photosystem II and the Cytochrome b6/f-Complex , 1990 .

[26]  H. Reichenbach,et al.  The aurachins, new quinoline antibiotics from myxobacteria: production, physico-chemical and biological properties. , 1987, The Journal of antibiotics.

[27]  G. Wittig,et al.  Über die o-Benzidin-Umlagerung des 3-Methyl-4-phenylhydrazo-5-phenyl-isoxazols , 1929 .