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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

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.

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 Creators:
Shima, Seigo1, 2, Author           
Thauer, Rudolf K.3, Author           
Ermler, Ulrich4, Author           
Durchschlag, Helmut5, Author
Tziatzios, Christos 6, Author
Schubert, Dieter6, Author
Affiliations:
1Department-Independent Research Group Microbial Protein Structure, Max Planck Institute for Terrestrial Microbiology, Max Planck Society, ou_3266277              
2Laboratorium für Mikrobiologie des Fachbereichs Biologie der Philipps‐Universität, Marburg, Germany, ou_persistent22              
3Department of Microbiology, Max Planck Institute for Marine Microbiology, Max Planck Society, ou_2481695              
4Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Max Planck Society, ou_2068290              
5Institut für Biophysik und Physikalische Biochemie der Universität Regensburg, Regensburg, Germany;, ou_persistent22              
6Institut für Biophysik der Johann Wolfgang Goethe‐Universität, Frankfurt am Main, Germany, ou_persistent22              

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Free keywords: formyltransferase; Methanopyrus kandleri; monomer/dimer/tetramer; association equilibrium; site‐directed mutagenesis
 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.

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Language(s): eng - English
 Dates: 2000-09-082000-06-192000-09-122001-12-252000-11-01
 Publication Status: Published in print
 Pages: 5
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1046/j.1432-1327.2000.01756.x
 Degree: -

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Title: European Journal of Biochemistry
Source Genre: Journal
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Publ. Info: Berlin : Published by Springer-Verlag on behalf of the Federation of European Biochemical Societies
Pages: - Volume / Issue: 267 (22) Sequence Number: - Start / End Page: 6619 - 6623 Identifier: ISSN: 0014-2956
CoNE: https://pure.mpg.de/cone/journals/resource/111097776606040