Shima, Seigo and Thauer, Rudolf K. and Ermler, Ulrich and Durchschlag, Helmut and Tziatzios, Christos and Schubert, Dieter (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). pp. 6619-6623. ISSN 0014-2956
Full text not available from this repository. (Request a copy)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.
| Item Type: | Article |
|---|---|
| Uncontrolled Keywords: | TETRAHYDROMETHANOPTERIN FORMYLTRANSFERASE; ESCHERICHIA-COLI; SALT-DEPENDENCE; FORMYLMETHANOFURAN; PROTEIN; METHANOGENESIS; 110-DEGREES-C; EXPRESSION; MECHANISM; CLONING; formyltransferase; Methanopyrus kandleri; monomer/dimer/tetramer association equilibrium; site-directed mutagenesis |
| Subjects: | 500 Science > 570 Life sciences |
| Divisions: | Biology, Preclinical Medicine > Institut für Biophysik und physikalische Biochemie |
| Depositing User: | Dr. Gernot Deinzer |
| Date Deposited: | 16 Mar 2022 16:33 |
| Last Modified: | 16 Mar 2022 16:33 |
| URI: | https://pred.uni-regensburg.de/id/eprint/42079 |
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