Literature DB >> 17367138

Mechanism-based inactivation of benzoylformate decarboxylase, a thiamin diphosphate-dependent enzyme.

Asim K Bera1, Lena S Polovnikova, Juliatek Roestamadji, Theodore S Widlanski, George L Kenyon, Michael J McLeish, Miriam S Hasson.   

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Year:  2007        PMID： 17367138     DOI： 10.1021/ja068636z

Source DB:  PubMed          Journal:  J Am Chem Soc        ISSN： 0002-7863            Impact factor:   15.419


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  3 in total

1.  Covalently bound substrate at the regulatory site of yeast pyruvate decarboxylases triggers allosteric enzyme activation.

Authors:  Steffen Kutter; Manfred S Weiss; Georg Wille; Ralph Golbik; Michael Spinka; Stephan König
Journal:  J Biol Chem       Date:  2009-02-26       Impact factor: 5.157

2.  Probing the active center of benzaldehyde lyase with substitutions and the pseudosubstrate analogue benzoylphosphonic acid methyl ester.

Authors:  Gabriel S Brandt; Natalia Nemeria; Sumit Chakraborty; Michael J McLeish; Alejandra Yep; George L Kenyon; Gregory A Petsko; Frank Jordan; Dagmar Ringe
Journal:  Biochemistry       Date:  2008-06-21       Impact factor: 3.162

3.  Specific inhibition by synthetic analogs of pyruvate reveals that the pyruvate dehydrogenase reaction is essential for metabolism and viability of glioblastoma cells.

Authors:  Victoria I Bunik; Artem Artiukhov; Alexey Kazantsev; Renata Goncalves; Danilo Daloso; Henry Oppermann; Elena Kulakovskaya; Nikolay Lukashev; Alisdair Fernie; Martin Brand; Frank Gaunitz
Journal:  Oncotarget       Date:  2015-11-24
  3 in total

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