Die Arbeit beschreibt die Reinigung von 4-Hydroxyphenylpyruvat Dioxygenase (4-HPPD) aus Maiskeimlingen, weiterhin die Identifikation, Isolation, Klonierung und heterologe Überexpression von 4-HPPD aus Mais, Reis, Arabidopsis thaliana, Maus und Mensch. Die 4 HPPD aus Arabidopsis thaliana wurde kristllisiert und Röntgenbeugungsdaten aufgenommen. Lösliche anorganische Pyrophosphatase aus Saccharomyces cerevisiae wurde zusammen mit Inhibitoren kristallisiert und die Kristallstruktur der Inhibitorkomplexe bestimmt.     «

Die Arbeit beschreibt die Reinigung von 4-Hydroxyphenylpyruvat Dioxygenase (4-HPPD) aus Maiskeimlingen, weiterhin die Identifikation, Isolation, Klonierung und heterologe Überexpression von 4-HPPD aus Mais, Reis, Arabidopsis thaliana, Maus und Mensch. Die 4 HPPD aus Arabidopsis thaliana wurde kristllisiert und Röntgenbeugungsdaten aufgenommen. Lösliche anorganische Pyrophosphatase aus Saccharomyces cerevisiae wurde zusammen mit Inhibitoren kristallisiert und die Kristallstruktur der Inhibitorkom...     »

1. 4-Hydroxphenylpyruvate Dioxygenase 4-Hydroxyphenylpyruvate dioxygenase (4-HPPD) is a mononuclear, non-heme, iron containing enzyme and belongs to the group of 2-oxoacid dependent dioxygenases. It catalyzes the conversion of 4-hydroxphenylpyruvate to homogentisic acid. In most organisms 4-HPPD is involved in the catabolism of Tyrosin. In plants 4-HPPD is a key enzyme in the synthesis of a-tocopherol and plastoquinone, making it a potential target for herbicide development. In this work different plant and mammalian 4-HPPDs were characterized biochemically, purified, cloned and crystallized. This allowed a detailed a comparison of the protein characteristics from plant and mammalian 4-HPPDs. 2. Soluble inorganic pyrophosphatase Soluble inorganic pyrophosphatase (PPase) catalyzes the hydrolysis of pyrophosphate to two phosphate groups. It is a key enzyme in the metabolism of all living cells. Inhibitors of PPase are used in cancer therapy, in the treatment of osteoporosis and as fungicides in crop protection. In this work PPase from yeast was crystallized in complex with two non hydrolysable substrate analogs. The crystal structure of these complexes was solved at 2.3 A and 2.4 A resolution respectively. A proposed SN2 reaction mechanism was confirmed by the structures.     «

1. 4-Hydroxphenylpyruvate Dioxygenase 4-Hydroxyphenylpyruvate dioxygenase (4-HPPD) is a mononuclear, non-heme, iron containing enzyme and belongs to the group of 2-oxoacid dependent dioxygenases. It catalyzes the conversion of 4-hydroxphenylpyruvate to homogentisic acid. In most organisms 4-HPPD is involved in the catabolism of Tyrosin. In plants 4-HPPD is a key enzyme in the synthesis of a-tocopherol and plastoquinone, making it a potential target for herbicide development. In this work differe...     »