Michael Spinka

Martin Luther University Halle-Wittenberg — Germany

Biochemistry, Genetics and Molecular Biology · Life Sciences

11h-index378citations17works0.02yr avg
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Research Topics

Biochemical Acid Research Studies(14), Alcoholism and Thiamine Deficiency(10), Metabolism and Genetic Disorders(6), Tryptophan and brain disorders(4), Amino Acid Enzymes and Metabolism(3)

Publications17 total

Significance of Individual Residues at the Regulatory Site of Yeast Pyruvate Decarboxylase for Allosteric Substrate Activation
Biochemistry·2017· 4 cited
Catalytically active filaments – pyruvate decarboxylase from <i>Neurospora crassa</i>. pH‐controlled oligomer structure and catalytic function
FEBS Journal·2011· 3 cited
Arabidopsis thaliana PECP1 — Enzymatic characterization and structural organization of the first plant phosphoethanolamine/phosphocholine phosphatase
Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics·2011· 37 cited
Profiling of Enzymatic Activities Using Peptide Arrays
Mini-Reviews in Organic Chemistry·2011· 6 cited
Covalently Bound Substrate at the Regulatory Site of Yeast Pyruvate Decarboxylases Triggers Allosteric Enzyme Activation
Journal of Biological Chemistry·2009· 46 citedOpen Access
Allosteric activation of pyruvate decarboxylases. A never-ending story?
Journal of Molecular Catalysis B Enzymatic·2009· 18 cited
Covalently bound substrate at the regulatory site triggers allosteric enzyme activation
Nature Precedings·2008· 2 citedOpen Access
Covalently Bound Substrate At The Regulatory Site Triggers Allosteric Enzyme Activation
Zenodo (CERN European Organization for Nuclear Research)·2008Open Access
Amino Acids Allosterically Regulate the Thiamine Diphosphate-dependent α-Keto Acid Decarboxylase from Mycobacterium tuberculosis
Journal of Biological Chemistry·2007· 17 citedOpen Access
The Influence of Protein Concentration on Oligomer Structure and Catalytic Function of Two Pyruvate Decarboxylases
The Protein Journal·2007· 11 cited
Phosphorylation of Serine 264 Impedes Active Site Accessibility in the E1 Component of the Human Pyruvate Dehydrogenase Multienzyme Complex
Biochemistry·2007· 67 cited
Ligand-Induced Conformational Changes in Thiamine Diphosphate–Dependent Enzymes
Oxidative stress and disease·2003
Pyruvate decarboxylase from <i>Kluyveromyces lactis</i>
European Journal of Biochemistry·2002· 30 citedOpen Access
Consequences of a Modified Putative Substrate-Activation Site on Catalysis by Yeast Pyruvate Decarboxylase
Biochemistry·2001· 26 cited
Activation of thiamin diphosphate in enzymes
Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology·1998· 53 citedOpen Access
Activation of Thiamin Diphosphate and FAD in the Phosphatedependent Pyruvate Oxidase fromLactobacillus plantarum
Journal of Biological Chemistry·1998· 39 citedOpen Access
Molecular Mechanism of Regulation of the Pyruvate Dehydrogenase Complex from <i>E. coli</i>
Biochemistry·1997· 19 cited

Frequent Co-authors

Stephan König(10), Ralph Golbik(7), Gerhard Hübner(6), S. Kutter(6), Kai Tittmann(5), G. Wille(4), Günther Kern(3), M.S. Weiss(3), Johanna Brauer(2), Holger Neef(2), Sandro Ghisla(2), Michel H. J. Koch(2), Franziska Seifert(1), Ewa Ciszak(1), Lioubov G. Korotchkina(1), P.M. Dominiak(1), Sukhdeep Sidhu(1), Mulchand S. Patel(1), Margrit Killenberg‐Jabs(1), Jörg Schäffner(1)