This title appears in the Scientific Report :
2016
Please use the identifier:
http://hdl.handle.net/2128/9738 in citations.
Please use the identifier: http://dx.doi.org/10.1038/srep17908 in citations.
Trading off stability against activity in extremophilic aldolases
Trading off stability against activity in extremophilic aldolases
Understanding enzyme stability and activity in extremophilic organisms is of great biotechnological interest, but many questions are still unsolved. Using 2-deoxy-D-ribose-5-phosphate aldolase (DERA) as model enzyme, we have evaluated structural and functional characteristics of different orthologs...
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Personal Name(s): | Dick, Markus |
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Weiergräber, Oliver H. / Classen, Thomas / Bisterfeld, Carolin / Bramski, Julia / Gohlke, Holger (Corresponding author) / Pietruszka, Jörg (Corresponding author) | |
Contributing Institute: |
Institut für Bioorganische Chemie (HHUD); IBOC Strukturbiochemie; ICS-6 Biotechnologie; IBG-1 |
Published in: | Scientific reports, 6 (2016) S. 17908 - |
Imprint: |
London
Nature Publishing Group
2016
|
PubMed ID: |
26783049 |
DOI: |
10.1038/srep17908 |
Document Type: |
Journal Article |
Research Program: |
Biotechnology |
Link: |
OpenAccess OpenAccess |
Publikationsportal JuSER |
Please use the identifier: http://dx.doi.org/10.1038/srep17908 in citations.
Understanding enzyme stability and activity in extremophilic organisms is of great biotechnological interest, but many questions are still unsolved. Using 2-deoxy-D-ribose-5-phosphate aldolase (DERA) as model enzyme, we have evaluated structural and functional characteristics of different orthologs from psychrophilic, mesophilic and hyperthermophilic organisms. We present the first crystal structures of psychrophilic DERAs, revealing a dimeric organization resembling their mesophilic but not their thermophilic counterparts. Conversion into monomeric proteins showed that the native dimer interface contributes to stability only in the hyperthermophilic enzymes. Nevertheless, introduction of a disulfide bridge in the interface of a psychrophilic DERA did confer increased thermostability, suggesting a strategy for rational design of more durable enzyme variants. Constraint network analysis revealed particularly sparse interactions between the substrate pocket and its surrounding α-helices in psychrophilic DERAs, which indicates that a more flexible active center underlies their high turnover numbers. |