Journal
EUROPEAN JOURNAL OF BIOCHEMISTRY
Volume 267, Issue 22, Pages 6619-6623Publisher
BLACKWELL PUBLISHING LTD
DOI: 10.1046/j.1432-1327.2000.01756.x
Keywords
formyltransferase; Methanopyrus kandleri; monomer/dimer/tetramer association equilibrium; site-directed mutagenesis
Categories
Ask authors/readers for more resources
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.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available