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'Ascochyta rabiei' in keywords
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1997 (1)
1995 (1)
1Author    Gregor Benning, Wolfgang BarzRequires cookie*
 Title    Accumulation and Biosynthesis of Solanapyrone Phytotoxins by Ascochyta rabiei  
 Abstract    The biosynthesis of the phytotoxins solanapyrone A , B and C produced by the phytopatho-genic fungus Ascochyta rabiei has been investigated. To optimize feeding conditons for the tracer experiments the growth of the fungus and the accumulation of the toxins in submers culture were determined. The accumulation kinetics revealed that formation of the toxins occurs in the stationary phase of the growth indicating that synthesis of solanapyrones follows a typical pattern of secondary metabolism. Incorporation experiments with sodium [1-14C]-and [2-13C]acetate were performed and the NM R-spectroscopically determined labelling pattern of the 13C-enriched solanapyrone A compound confirmed that the carbon skeleton of this compound is formed via the polyketide pathway. The biosynthetic route to solana­ pyrone B is discussed. 
  Reference    Z. Naturforsch. 50c, 181 (1995); received January 9 1995 
  Published    1995 
  Keywords    Biosynthesis, Solanapyrones, Polyketide Phytotoxin, Ascochyta rabiei 
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 TEI-XML for    default:Reihe_C/50/ZNC-1995-50c-0181.pdf 
 Identifier    ZNC-1995-50c-0181 
 Volume    50 
2Author    Raimund Tenhaken, Martin Arnemann, Gabriele Köhler, Wolfgang BarzRequires cookie*
 Title    Characterization and Cloning of Cutinase from Ascochyta rabiei  
 Abstract    Ascochyta rabiei, the causal agent o f Ascochyta blight on chickpea plants, secretes a cu­ tinase in the culture filtrate when it is induced by cutin or hydroxylated fatty acids. This cutinase is the main esterase in the culture fluids. The enzyme was purified to homogeneity by three successive chromatographic steps. It showed an apparent molecular weight of 22 kD in SDS-PAGE and cleaved ester bonds o f 3H-labelled cutin or p-nitrophenylbutyrate with maximal activities around pH 8. A s a serine esterase, cutinase is strongly inhibited by organophosphorous compounds and the most effective inhibitor 2,3,5-trichloropyridine-6-(0-methyl-0-«-butyl)-phosphateester (M A T 9564) shows a K\ value of 0.8 nM. The cutinase gene was cloned from a genomic cosmid library by screening with two oligonucleotides directed against cutinase consensus peptides. The gene was subcloned to a 1.7 Kb Sall/Hindlll-insert and sequenced. The cutinase gene codes for a 223 amino acid protein with strong homology to other fungal cutinase sequences. The purified cutinase is encoded by a single copy gene. 
  Reference    Z. Naturforsch. 52c, 197—208 (1997); received September 11/November 15 1996 
  Published    1997 
  Keywords    Ascochyta rabiei, Cutinase, Cutinase Gene Sequence, Serine Esterase, Organophosphorous Pesticides 
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 TEI-XML for    default:Reihe_C/52/ZNC-1997-52c-0197.pdf 
 Identifier    ZNC-1997-52c-0197 
 Volume    52