jump to searchjump to navigationjump to content

Publications - Cell and Metabolic Biology

Sort by: Year Type of publication

Displaying results 191 to 200 of 409.

Publications

Deepak, S., Shailasree, S., Kini, R.K., Hause, B., Shetty, S.H. & Mithöfer, A. Role of hydroxyproline rich glycoproteins in resistance of pearl millet against downy mildew pathogen Sclerospora graminicola Planta 226, 323-333, (2007)

0
Publications

Schaarschmidt, S., González, M.-C., Roitsch, T., Strack, D., Sonnewald, U. & Hause, B. Regulation of arbuscular mycorrhization by carbon. The symbiotic interaction cannot be improved by increased carbon availability accomplished by root-specifically enhanced invertase activity Plant Physiol 143, 1827-1840, (2007)

0
Publications

Walter, M.H., Floß, D.S., Hans, J., Fester, T. & Strack, D. REVIEW: Apocarotenoid biosynthesis in arbuscular mycorrhizal roots: Contributions from methylerythritol phosphate pathway isogenes and tools for its manipulation Phytochemistry 68, 130-138, (2007)

0
Publications

Stintzing, F. & Schliemann, W. Pigments of Fly Agaric (Amanita muscaria). In: 62c Zeitschrift für Naturforschung 779-785, (2007)

The complex pigment pattern of fly agaric (Amanita muscaria) cap skins has been studied by LC-DAD and mass spectrometry. Among the betaxanthins the corresponding derivatives of serine, threonine, ethanolamine, alanine, Dopa, phenylalanine and tryptophan are reported for the first time to contribute to the pigment pattern of fly agarics. Betalamic acid, the chromophoric precursor of betaxanthins and betacyanins, muscaflavin and seco-dopas were also detected. Furthermore, the red-purple muscapurpurin and the red muscarubrin were tentatively assigned while further six betacyanin-like components could not be structurally allocated. Stability studies indicated a high susceptibility of pigment extracts to degradation which led to rapid colour loss thus rendering a complete characterization of betacyaninlike compounds impossible at present. Taking into account these difficulties the presented results may be a starting point for a comprehensive characterization of the pigment composition of fly agarics.
Publications

Textor, S., De Kraker, J.-W., Hause, B., Gershenzon, J. & Tokuhisa, J.G. MAM3 catalyzes the formation of all aliphatic glucosinolate chain lengths in Arabidopsis thaliana Plant Physiol 144, 60-71, (2007)

0
Publications

Hause, B., Mrosk, C., Isayenkov, S. & Strack, D. Jasmonates in arbuscular mycorrhizal interactions Phytochemistry 68, 101-110, (2007)

0
Publications

Cenzano, A., Abdala, G. & Hause, B. Cytochemical immuno-localization of allene oxide cy-clase, a jasmonic acid biosynthetic enzyme, in developing potato stolons J. Plant Physiol 164, 1449-1456, (2007)

0
Publications

Burow, M., Rice, M., Hause, B., Gershenzon, J. & Wittstock, U. Cell- and tissue-specific localization and regulation of the epithiospecifier protein in Arabidopsis thaliana Plant Mol. Biol 64, 173-185, (2007)

0
Publications

Fester, T., Lohse, S. & Halfmann, K. Chromoplast development in arbuscular mycorrhizal roots Phytochemistry 68, 92-100, (2007)

0
Publications

Ziegler, J., Voigtländer, S., Schmidt, J., Kramell, R., Miersch, O., Ammer, C., Gesell, A. & Kutchan, T.M. Comparative transcript and alkaloid profiling in Papaver species identifies a short chain dehydrogenase/reductase involved in morphine biosynthesis Plant J. 48, 177-192, (2006) DOI: 10.1111/j.1365-313X.2006.02860.x

Plants of the order Ranunculales, especially members of the species Papaver, accumulate a large variety of benzylisoquinoline alkaloids with about 2500 structures, but only the opium poppy (Papaver somniferum) and Papaver setigerum are able to produce the analgesic and narcotic morphine and the antitussive codeine. In this study, we investigated the molecular basis for this exceptional biosynthetic capability by comparison of alkaloid profiles with gene expression profiles between 16 different Papaver species. Out of 2000 expressed sequence tags obtained from P. somniferum, 69 show increased expression in morphinan alkaloid-containing species. One of these cDNAs, exhibiting an expression pattern very similar to previously isolated cDNAs coding for enzymes in benzylisoquinoline biosynthesis, showed the highest amino acid identity to reductases in menthol biosynthesis. After overexpression, the protein encoded by this cDNA reduced the keto group of salutaridine yielding salutaridinol, an intermediate in morphine biosynthesis. The stereoisomer 7-epi-salutaridinol was not formed. Based on its similarities to a previously purified protein from P. somniferum with respect to the high substrate specificity, molecular mass and kinetic data, the recombinant protein was identified as salutaridine reductase (SalR; EC 1.1.1.248). Unlike codeinone reductase, an enzyme acting later in the pathway that catalyses the reduction of a keto group and which belongs to the family of the aldo-keto reductases, the cDNA identified in this study as SalR belongs to the family of short chain dehydrogenases/reductases and is related to reductases in monoterpene metabolism.

IPB Mainnav Search