| Electrostatic interactions across the dimer-dimer interface contribute to the pH-dependent stability of a tetrameric malate dehydrogenase. | |
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MedLine Citation:
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PMID: 14572663 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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Malate dehydrogenase (MDH) from the moderately thermophilic bacterium Chloroflexus aurantiacus (CaMDH) is a tetrameric enzyme, while MDHs from mesophilic bacteria usually are dimers. Using site-directed mutagenesis, we show here that a network of electrostatic interactions across the extra dimer-dimer interface in CaMDH is important for thermal stability and oligomeric integrity. Stability effects of single point mutations (E25Q, E25K, D56N, D56K) varied from -1.2 degrees C to -26.8 degrees C, and depended strongly on pH. Gel-filtration experiments indicated that the 26.8 degrees C loss in stability observed for the D56K mutant at low pH was accompanied by a shift towards a lower oligomerization state. |
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Authors:
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Alexandra Bjørk; Dimitrios Mantzilas; Reidun Sirevåg; Vincent G H Eijsink |
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Publication Detail:
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Type: Journal Article; Research Support, Non-U.S. Gov't |
Journal Detail:
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Title: FEBS letters Volume: 553 ISSN: 0014-5793 ISO Abbreviation: FEBS Lett. Publication Date: 2003 Oct |
Date Detail:
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Created Date: 2003-10-23 Completed Date: 2003-12-09 Revised Date: 2008-11-21 |
Medline Journal Info:
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Nlm Unique ID: 0155157 Medline TA: FEBS Lett Country: Netherlands |
Other Details:
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Languages: eng Pagination: 423-6 Citation Subset: IM |
Affiliation:
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Department of Biology, University of Oslo, Box 1031 Blindern, N-0316 Oslo, Norway. alexandra.bjork@bio.uio.no |
Export Citation:
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APA/MLA Format Download EndNote Download BibTex |
| MeSH Terms | |
Descriptor/Qualifier:
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Amino Acid Substitution Bacterial Proteins / chemistry* Chlorobi / enzymology Chromatography, Gel Dimerization Enzyme Stability Hot Temperature Hydrogen-Ion Concentration Malate Dehydrogenase / chemistry* Models, Molecular Mutagenesis, Site-Directed Protein Conformation Protein Denaturation Protein Structure, Quaternary Protein Subunits Recombinant Proteins / chemistry Static Electricity Temperature |
| Chemical | |
Reg. No./Substance:
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0/Bacterial Proteins; 0/Protein Subunits; 0/Recombinant Proteins; EC 1.1.1.37/Malate Dehydrogenase |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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