ArticleThe protein journal2012
Fluorescence studies on the stability, flexibility and substrate-induced conformational changes of acetate kinases from psychrophilic and mesophilic bacteria.
Article in The protein journal, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
7 citing papers in PubMed, 12 citations in OpenAlex.
- Roles of Active-Site Aromatic Residues in Cold Adaptation ofACS omega · 2017Article
- Bacterial Community Structures in Freshwater Polar Environments of Svalbard.Microbes and environments · 2016Article
- Discovery, Molecular Mechanisms, and Industrial Applications of Cold-Active Enzymes.Frontiers in microbiology · 2016Review
- Cold adaptation: structural and functional characterizations of psychrophilic and mesophilic acetate kinase.The protein journal · 2014Article
- Spectroscopic analyses of manganese ions effects on the conformational changes of inorganic pyrophosphatase from psychrophilic Shewanella sp. AS-11.The protein journal · 2014Article
- Psychrophilic enzymes: from folding to function and biotechnology.Scientifica · 2013Review
- Optimization to low temperature activity in psychrophilic enzymes.International journal of molecular sciences · 2012Review
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The acetate kinase from the Antarctic psychrophilic Shewanella sp. AS-11 (SAK) has a significantly higher catalytic efficiency at low temperatures when compared with that from mesophilic Escherichia coli K-12 (EAK). To examine the stability and conformational flexibility of SAK and EAK, steady state intrinsic fluorescence studies were performed. EAK contains only one Trp at a position 46, while SAK contains two Trps at positions 46 and 388. From the fluorescence emission spectra, quenching with acrylamide, Cs(+) and I(-) at different temperatures and denaturation with guanidine-HCl, it was revealed that the SAK bears more flexible and unstable structure than that of EAK. Substrate-induced conformational changes reflect that SAK reached transition state through more conformational changes than EAK. In combination of our thermodynamic studies on the enzymatic reaction and present research findings, it can be concluded that these structural features of SAK may contribute to its high catalytic efficiency at low temperatures.
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