期刊
EUROPEAN JOURNAL OF BIOCHEMISTRY
卷 267, 期 22, 页码 6619-6623出版社
BLACKWELL PUBLISHING LTD
DOI: 10.1046/j.1432-1327.2000.01756.x
关键词
formyltransferase; Methanopyrus kandleri; monomer/dimer/tetramer association equilibrium; site-directed mutagenesis
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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