Search Results - "Spinka, Michael"

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  1. 1

    Arabidopsis thaliana PECP1 — Enzymatic characterization and structural organization of the first plant phosphoethanolamine/phosphocholine phosphatase by May, Anett, Spinka, Michael, Köck, Margret

    Published in Biochimica et biophysica acta (01-02-2012)
    “…Maintenance of cellular phosphate homeostasis is crucial for primary and energy metabolism. In plants, low exogenous phosphate availability activates adaptive…”
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    Journal Article
  2. 2

    Significance of Individual Residues at the Regulatory Site of Yeast Pyruvate Decarboxylase for Allosteric Substrate Activation by Spinka, Michael, Seiferheld, Sebastian, Zimmermann, Philipp, Bergner, Elena, Blume, Anne-Kathrin, Schierhorn, Angelika, Reichenbach, Tom, Pertermann, Robert, Ehrt, Christiane, König, Stephan

    Published in Biochemistry (Easton) (07-03-2017)
    “…The catalytic activity of the allosteric enzyme pyruvate decarboxylase from yeast is strictly controlled by its own substrate pyruvate via covalent binding at…”
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    Journal Article
  3. 3

    Covalently Bound Substrate at the Regulatory Site of Yeast Pyruvate Decarboxylases Triggers Allosteric Enzyme Activation by Kutter, Steffen, Weiss, Manfred S., Wille, Georg, Golbik, Ralph, Spinka, Michael, König, Stephan

    Published in The Journal of biological chemistry (01-05-2009)
    “…The mechanism by which the enzyme pyruvate decarboxylase from two yeast species is activated allosterically has been elucidated. A total of seven…”
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    Journal Article
  4. 4

    Activation of Thiamin Diphosphate and FAD in the Phosphatedependent Pyruvate Oxidase fromLactobacillus plantarum by Tittmann, Kai, Proske, Daniela, Spinka, Michael, Ghisla, Sandro, Rudolph, Rainer, Hübner, Gerhard, Kern, Gunther

    Published in The Journal of biological chemistry (22-05-1998)
    “…The phosphate- and oxygen-dependent pyruvate oxidase from Lactobacillus plantarum is a homotetrameric enzyme that binds 1 FAD and 1 thiamine diphosphate per…”
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    Journal Article
  5. 5

    Phosphorylation of Serine 264 Impedes Active Site Accessibility in the E1 Component of the Human Pyruvate Dehydrogenase Multienzyme Complex by Seifert, Franziska, Ciszak, Ewa, Korotchkina, Lioubov, Golbik, Ralph, Spinka, Michael, Dominiak, Paulina, Sidhu, Sukhdeep, Brauer, Johanna, Patel, Mulchand S, Tittmann, Kai

    Published in Biochemistry (Easton) (29-05-2007)
    “…At the junction of glycolysis and the Krebs cycle in cellular metabolism, the pyruvate dehydrogenase multienzyme complex (PDHc) catalyzes the oxidative…”
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    Journal Article
  6. 6

    Allosteric activation of pyruvate decarboxylases. A never-ending story? by König, Stephan, Spinka, Michael, Kutter, Steffen

    “…The allosteric substrate activation of pyruvate decarboxylases was studied for more than 30 years using varying techniques and ending up in different…”
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    Journal Article Conference Proceeding
  7. 7

    Catalytically active filaments – pyruvate decarboxylase from Neurospora crassa. pH‐controlled oligomer structure and catalytic function by Hüttl, Stefanie, Fiebig, Juliane, Kutter, Steffen, Hause, Gerd, Lilie, Hauke, Spinka, Michael, König, Stephan

    Published in The FEBS journal (01-01-2012)
    “…Pyruvate decarboxylase is a key enzyme in organisms whose energy metabolism is based on alcoholic fermentation. The enzyme catalyses the nonoxidative…”
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    Journal Article
  8. 8

    Catalytically active filaments - pyruvate decarboxylase from Neurosporacrassa. pH-controlled oligomer structure and catalytic function by Hüttl, Stefanie, Fiebig, Juliane, Kutter, Steffen, Hause, Gerd, Lilie, Hauke, Spinka, Michael, König, Stephan

    Published in The FEBS journal (01-01-2012)
    “…Pyruvate decarboxylase is a key enzyme in organisms whose energy metabolism is based on alcoholic fermentation. The enzyme catalyses the nonoxidative…”
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    Journal Article
  9. 9

    Covalently Bound Substrate at the Regulatory Site of Yeast Pyruvate Decarboxylases Triggers Allosteric Enzyme ActivationS by Kutter, Steffen, Weiss, Manfred S., Wille, Georg, Golbik, Ralph, Spinka, Michael, König, Stephan

    Published in The Journal of biological chemistry (01-05-2009)
    “…The mechanism by which the enzyme pyruvate decarboxylase from two yeast species is activated allosterically has been elucidated. A total of seven…”
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    Journal Article
  10. 10

    Amino Acids Allosterically Regulate the Thiamine Diphosphate-dependent α-Keto Acid Decarboxylase from Mycobacterium tuberculosis by Werther, Tobias, Spinka, Michael, Tittmann, Kai, Schütz, Anja, Golbik, Ralph, Mrestani-Klaus, Carmen, Hübner, Gerhard, König, Stephan

    Published in The Journal of biological chemistry (29-02-2008)
    “…The gene rv0853c from Mycobacterium tuberculosis strain H37Rv codes for a thiamine diphosphate-dependent α-keto acid decarboxylase (MtKDC), an enzyme involved…”
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    Journal Article
  11. 11

    Amino Acids Allosterically Regulate the Thiamine Diphosphate-dependent α-Keto Acid Decarboxylase from Mycobacterium tuberculosis by Tobias Werther, Michael Spinka, Kai Tittmann, Anja Schütz, Ralph Golbik, Carmen Mrestani-Klaus, Gerhard Hübner, Stephan König

    Published in The Journal of biological chemistry (29-02-2008)
    “…The gene rv0853c from Mycobacterium tuberculosis strain H37Rv codes for a thiamine diphosphate-dependent α-keto acid decarboxylase ( Mt KDC), an enzyme…”
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    Journal Article
  12. 12

    The influence of protein concentration on oligomer structure and catalytic function of two pyruvate decarboxylases by Kutter, Steffen, Spinka, Michael, Koch, Michel H J, König, Stephan

    Published in The Protein Journal (01-12-2007)
    “…As a general rule protein concentration typical for structural studies differs considerably from that chosen for kinetic investigations. Consequently,…”
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    Journal Article
  13. 13

    Consequences of a Modified Putative Substrate-Activation Site on Catalysis by Yeast Pyruvate Decarboxylase by Wang, Jue, Golbik, Ralph, Seliger, Birgitta, Spinka, Michael, Tittmann, Kai, Hübner, Gerhard, Jordan, Frank

    Published in Biochemistry (Easton) (13-02-2001)
    “…Earlier, it had been proposed in the laboratories at Halle that a cysteine residue is responsible for the hysteretic substrate activation behavior of yeast…”
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    Journal Article
  14. 14

    Activation of Thiamin Diphosphate and FAD in the Phosphate-dependent Pyruvate Oxidase from Lactobacillus plantarum by Tittmann, K, Proske, D, Spinka, M, Ghisla, S, Rudolph, R, Huebner, G, Kern, G

    Published in The Journal of biological chemistry (22-05-1998)
    “…The phosphate- and oxygen-dependent pyruvate oxidase from Lactobacillus plantarum is a homotetrameric enzyme that binds 1 FAD and 1 thiamine diphosphate per…”
    Get full text
    Journal Article
  15. 15

    Pyruvate decarboxylase from Kluyveromyces lactis. An enzyme with an extraordinary substrate activation behaviour by Krieger, Florian, Spinka, Michael, Golbik, Ralph, Hübner, Gerhard, König, Stephan

    Published in European journal of biochemistry (01-07-2002)
    “…Pyruvate decarboxylase (EC 4.1.1.1) was isolated and purified from the yeast Kluyveromyces lactis. The properties of this enzyme relating to the native…”
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    Journal Article
  16. 16

    Molecular Mechanism of Regulation of the Pyruvate Dehydrogenase Complex from E. coli by Hennig, Jana, Kern, Gunther, Neef, Holger, Spinka, Michael, Bisswanger, Hans, Hübner, Gerhard

    Published in Biochemistry (Easton) (16-12-1997)
    “…The pyruvate dehydrogenase multienzyme complex from E. coli shows a sigmoidal dependency of the reaction rate on the substrate concentration when product…”
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    Journal Article
  17. 17

    Pyruvate decarboxylase from Kluyveromyces lactis by Krieger, Florian, Spinka, Michael, Golbik, Ralph, Hübner, Gerhard, König, Stephan

    Published in European journal of biochemistry (01-07-2002)
    “…Pyruvate decarboxylase (EC 4.1.1.1) was isolated and purified from the yeast Kluyveromyces lactis. The properties of this enzyme relating to the native…”
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    Journal Article
  18. 18

    Activation of thiamin diphosphate in enzymes by Hübner, Gerhard, Tittmann, Kai, Killenberg-Jabs, Margrit, Schäffner, Jörg, Spinka, Michael, Neef, Holger, Kern, Dorothee, Kern, Gunther, Schneider, Gunter, Wikner, Christer, Ghisla, Sandro

    “…Activation of the coenzyme ThDP was studied by measuring the kinetics of deprotonation at the C2 carbon of thiamin diphosphate in the enzymes pyruvate…”
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    Book Review Journal Article