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

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 thermostab...

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Veröffentlicht in:European journal of biochemistry 2000-11, Vol.267 (22), p.6619-6623
Hauptverfasser: Shima, Seigo, Thauer, Rudolf K., Ermler, Ulrich, Durchschlag, Helmut, Tziatzios, Christos, Schubert, Dieter
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Sprache:eng
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