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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

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.

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Item Permalink: https://hdl.handle.net/21.11116/0000-0009-4BB1-B Version Permalink: https://hdl.handle.net/21.11116/0000-0009-4BB2-A
Genre: Journal Article

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 Creators:
Shima, S.1, Author           
Thauer, R. K.2, Author           
Ermler, U3, Author
Durchschlag, H3, Author
Tziatzios, C3, Author
Schubert, D3, Author
Affiliations:
1Department-Independent Research Group Microbial Protein Structure, Max Planck Institute for Terrestrial Microbiology, Max Planck Society, ou_3266277              
2Department of Biochemistry, Alumni, Max Planck Institute for Terrestrial Microbiology, Max Planck Society, ou_3266311              
3external, ou_persistent22              

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 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.

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 Dates: 2000
 Publication Status: Issued
 Pages: -
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 Rev. Type: -
 Identifiers: ISI: 000165456600013
DOI: 10.1046/j.1432-1327.2000.01756.x
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Title: EUROPEAN JOURNAL OF BIOCHEMISTRY
Source Genre: Journal
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Pages: - Volume / Issue: 267 (22) Sequence Number: - Start / End Page: 6619 - 6623 Identifier: ISSN: 0014-2956