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A mutation affecting the dimer/tetramer association equilibrium of formyltransferase from the hyperthermophilic Methanopyrus kandleri in relation to the activity and thermostability of the enzyme

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Shima,  Seigo
Department-Independent Research Group Microbial Protein Structure, Max Planck Institute for Terrestrial Microbiology, Max Planck Society;
Laboratorium für Mikrobiologie des Fachbereichs Biologie der Philipps‐Universität, Marburg, Germany;

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Thauer,  Rudolf K.
Department of Microbiology, Max Planck Institute for Marine Microbiology, Max Planck Society;

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Ermler,  Ulrich
Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Max Planck Society;

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Citation

Shima, S., Thauer, R. K., Ermler, U., Durchschlag, H., Tziatzios, C., & Schubert, D. (2000). A mutation affecting the dimer/tetramer association equilibrium of formyltransferase from the hyperthermophilic Methanopyrus kandleri in relation to the activity and thermostability of the enzyme. European Journal of Biochemistry, 267(22), 6619-6623. doi:10.1046/j.1432-1327.2000.01756.x.


Cite as: http://hdl.handle.net/21.11116/0000-0007-D2B7-D
Abstract
Formyltransferase from Methanopyrus kandleri is composed of only one type of subunit of molecular mass 32 kDa. The enzyme is in a monomer/dimer/tetramer association equilibrium, the association constant being affected by lyotropic salts. Oligomerization is required for enzyme activity and thermostability. We report here on a subunit interface mutation (R261E) which affects the dimer/tetramer part of the association equilibrium of formyltransferase. With the mutant protein it was shown that tetramerization is not required for activity but is necessary for high thermostability.