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Substrate Activation Of Yeast Pyruvate Decarboxylases

descriptionPublicationkeyboard_double_arrow_right Presentation , Other literature type 29 Sep 2007 English Publisher:Zenodo
Authors: Kutter, Steffen;

doi: 10.5281/zenodo.1313876 , 10.5281/zenodo.1313909 , 10.5281/zenodo.1313875 , 10.5281/zenodo.1313908

Substrate Activation Of Yeast Pyruvate Decarboxylases

Abstract

Short presentation for winning a poster award (Enzymes in motion - substrate activation of yeast pyruvate decarboxylases I. Crystal structures, 10.5281/zenodo.1313834) during the 7th international conference on mechanism and physiology of thiamine, Wittenberg, Germany, 05/29/2008-06/01/2008 Held on 06/01/2018, 11.25 am, https://dechema.de/Veranstaltungen/Archiv/CBT+2008/Lecture+Programme.html The regulatory site of pyruvate decarboxylases has been searched for more than 50 years. We provide the first crystallographic snapshots of yeast pyruvate decarboxylases in the presence of substrates and substrate surrogates, respectively. The ligands form a thiohemiketal bound with C221 of yeast pyruvate decarboxylases.

Related Organizations
Keywords

pyruvate decarboxylase, thiamine diphosphate, methyl acetylphosphonate, pyruvamide, pyruvated decarboxylase, crystallography, substrate activation

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This indicator reflects the "current" impact/attention (the "hype") of an article in the research community at large, based on the underlying citation network.
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