Author: "König, Stephan" / Journal: journal of biological chemistry - Searchworks@Jio Institute Digital Library Search Results

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Start Over Author "König, Stephan" Journal journal of biological chemistry

Author: Wirtz, Markus, primary, Birke, Hannah, additional, Heeg, Corinna, additional, Müller, Christopher, additional, Hosp, Fabian, additional, Throm, Christian, additional, König, Stephan, additional, Feldman-Salit, Anna, additional, Rippe, Karsten, additional, Petersen, Gabriele, additional, Wade, Rebecca C., additional, Rybin, Vladimir, additional, Scheffzek, Klaus, additional, and Hell, Rüdiger, additional
Published: 2010
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Author: Kutter, Steffen, primary, Weiss, Manfred S., additional, Wille, Georg, additional, Golbik, Ralph, additional, Spinka, Michael, additional, and König, Stephan, additional
Published: 2009
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Author: Werther, Tobias, primary, Spinka, Michael, additional, Tittmann, Kai, additional, Schütz, Anja, additional, Golbik, Ralph, additional, Mrestani-Klaus, Carmen, additional, Hübner, Gerhard, additional, and König, Stephan, additional
Published: 2008
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Author: Fiedler, Erik, primary, Golbik, Ralph, additional, Schneider, Gunter, additional, Tittmann, Kai, additional, Neef, Holger, additional, König, Stephan, additional, and Hübner, Gerhard, additional
Published: 2001
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Author: Svergun, Dmitri I., primary, Petoukhov, Maxim V., additional, Koch, Michel H.J., additional, and König, Stephan, additional
Published: 2000
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Author: Dobritzsch, Doreen, primary, König, Stephan, additional, Schneider, Gunter, additional, and Lu, Guoguang, additional
Published: 1998
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Author: Werther, Tobias, Spinka, Michael, Tittmann, Kai, Schütz, Anja, Golbik, Ralph, Mrestani-Klaus, Carmen, Hübner, Gerhard, and König, Stephan
Subjects: *DECARBOXYLASES, *KETONIC acids, *MICROBIAL enzymes, *MYCOBACTERIUM tuberculosis, *THIAMIN pyrophosphate, *AMINO acids
Abstract: The gene rv0853c from Mycobacterium tuberculosis strain H37Rv codes for a thiamine diphosphate-dependent α-keto acid decarboxylase (MtKDC), an enzyme involved in the amino acid degradation via the Ehrlich pathway. Steady state kinetic experiments were performed to determine the substrate specificity of MtKDC. The mycobacterial enzyme was found to convert a broad spectrum of branched-chain and aromatic α-keto acids, Stopped-flow kinetics showed that MtKDC is allosterically activated by α-keto acids. Even more, we demonstrate that also amino acids are potent activators of this thiamine diphosphate-dependent enzyme. Thus, metabolic flow through the Ehrlich pathway can be directly regulated at the decarboxylation step. The influence of amino acids on MtKDC catalysis was investigated, and implications for other thiamine diphosphate-dependent enzymes are discussed. [ABSTRACT FROM AUTHOR]
Published: 2008
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