A mutation affecting the association equilibrium of formyltransferase from the 
hyperthermophilic Methanopyrus kandleri and its influence on the enzyme's 
activity and thermostability

Shima, S.; Thauer, R. K.; Ermler, U; Durchschlag, H; Tziatzios, C; Schubert, D

doi:10.1046/j.1432-1327.2000.01756.x

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A mutation affecting the association equilibrium of formyltransferase from the hyperthermophilic Methanopyrus kandleri and its influence on the enzyme's activity and thermostability

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Shima, S.
Department-Independent Research Group Microbial Protein Structure, Max Planck Institute for Terrestrial Microbiology, Max Planck Society;

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Thauer, R. K.
Department of Biochemistry, Alumni, Max Planck Institute for Terrestrial Microbiology, 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 association equilibrium of formyltransferase from the hyperthermophilic Methanopyrus kandleri and its influence on the enzyme's activity and thermostability. EUROPEAN JOURNAL OF BIOCHEMISTRY, 267(22), 6619-6623. doi:10.1046/j.1432-1327.2000.01756.x.

Cite as: https://hdl.handle.net/21.11116/0000-0009-4BB1-B

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.