Variations in the stability of NCR ene reductase by rational enzyme loop modulation
The engineering of protein stability is of major importance for the application of enzymes in a wide range of industrial applications. Here we study the determinants of the thermo- and solvent stability of the Zymomonas mobilis ene reductase NCR using a rational protein engineering approach based on...
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| Veröffentlicht in: | Journal of structural biology 2014-02, Vol.185 (2), p.228-233 |
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| container_end_page | 233 |
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| container_title | Journal of structural biology |
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| creator | Reich, Sabrina Kress, Nico Nestl, Bettina M. Hauer, Bernhard |
| description | The engineering of protein stability is of major importance for the application of enzymes in a wide range of industrial applications. Here we study the determinants of the thermo- and solvent stability of the Zymomonas mobilis ene reductase NCR using a rational protein engineering approach based on analyses of structural and sequence data. We designed and created two loop mutants with the aim to increase their overall stability. They all retained catalytic activity but exhibited altered thermostability relative to the wild-type enzyme. The modulation of one specific loop segment near the active site of NCR showed an increased tolerance to organic solvents along with an enhanced thermostability. |
| doi_str_mv | 10.1016/j.jsb.2013.04.004 |
| format | Article |
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Here we study the determinants of the thermo- and solvent stability of the Zymomonas mobilis ene reductase NCR using a rational protein engineering approach based on analyses of structural and sequence data. We designed and created two loop mutants with the aim to increase their overall stability. They all retained catalytic activity but exhibited altered thermostability relative to the wild-type enzyme. 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| identifier | ISSN: 1047-8477 |
| ispartof | Journal of structural biology, 2014-02, Vol.185 (2), p.228-233 |
| issn | 1047-8477 1095-8657 |
| language | eng |
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| source | MEDLINE; Access via ScienceDirect (Elsevier) |
| subjects | Amino Acid Motifs Amino Acid Sequence Amino Acid Substitution Bacterial Proteins - chemistry Bacterial Proteins - genetics Cyclohexanones - chemistry Enzyme engineering Enzyme Stability FMN Reductase - chemistry FMN Reductase - genetics Molecular Sequence Data Mutagenesis, Site-Directed Old Yellow Enzyme Oxidation-Reduction Rational loop design Solvent stability Solvents - chemistry ThermoFAD Thermostability Zymomonas - enzymology |
| title | Variations in the stability of NCR ene reductase by rational enzyme loop modulation |
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