Zusammenfassung
Thiamindiphosphat, die biologisch aktive Form von Vitamin B1, nimmt als Kofaktor eine bedeutende Rolle ein. Die Aufklärung des Katalysemechanismus und der Struktur-Funktionsbeziehungen dieser Enzyme stellen zentrale Ziele der DFG-Forschergruppe 1296 dar.
Abstract
Thiamine diphosphate, the active form of vitamin B1, serves as a key cofactor in all forms of life. Elucidation of catalytic mechanisms and structure-function relationships of these enzymes are in the focus of the DFG Research Unit FOR 1296.
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Die Teilprojektleiter der DFG-Forschergruppe 1296 „Diversität asymetrischer Thiamin-Katalyse“: Jürgen Pleiss, Georg Sprenger (Stuttgart), Michael Müller (Freiburg), Antje Spiess (Aachen), Kirsten Zeitler (Regensburg), Martina Pohl, Dörte Gocke (Jülich) (v. l. n. r), Kai Tittmann (Göttingen) fehlt.
Die durch die DFG geförderte Forschergruppe FOR 1296 baut auf einer langen Tradition der Thiamin-Forschung in Deutschland auf. Während früher der Vitamincharakter und mechanistische Untersuchungen im Vordergrund standen, wird in der Forschergruppe an einem integrierten Ansatz zu Struktur-Funktionsbeziehungen ThDP-abhängiger Enzymkatalyse gearbeitet. Diese Enzyme dienen in verschiedener Hinsicht als Modell für das Verständnis diversitätsorientierter (Bio-)Katalyse.
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Müller, M. Diversität asymmetrischer Thiamin-Katalyse. Biospektrum 17, 281–283 (2011). https://doi.org/10.1007/s12268-011-0043-1
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DOI: https://doi.org/10.1007/s12268-011-0043-1