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SLAC National Accelerator Laboratory

Enzyme Created in Test Tube Promises Biocatalysts for a Range of Uses
December 2012 SSRL Science Summary by Lori Ann White, SLAC Office of Communications

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In recent years, enzymes have gained an important role in industry as cheap and environmentally friendly alternatives to traditional chemical catalysts. Learning to create such enzymes from scratch is necessary in order to provide biocatalysts for the wealth of non-natural reaction chemistries and substrates that have emerged over the last century.

Until now this has been achieved only when extensive knowledge of the mechanism of the reaction is available. Recently, however, researchers have used a clever in vitro strategy to synthesize an artificial RNA ligase enzyme capable of a previously unknown catalytic activity, and to do so they began with a protein not associated with catalysis. A team of scientists led by Burckhard Seelig of the University of Minnesota have now determined the unique structure of this novel biocatalyst using NMR and synchrotron-based Zn K-edge EXAFS at SSRL's Beam Line 9-3. As this new structure has not been subjected to the billions of years of natural evolution that shaped contemporary enzymes it can therefore be considered an early or primordial catalytic fold. In effect, the simplified environment of in vitro evolution allows the generation of model systems and the study of basic principles of complex natural evolution.

This in vitro directed evolution method has the potential to generate novel biocatalysts for a multitude of applications, and the unique structure of the artificial ligase enzyme demonstrates that this methodology can successfully generate artificial enzymes without being limited to known biological folds.


Primary Citation

Chao, F.-A., Morelli, A., Haugner III, J. C., Churchfield, L., Hagmann, L. N., Shi, L., Masterson, L. R., Sarangi, R., Veglia, G. & Seelig, B., "Structure and dynamics of a primordial catalytic fold generated by in vitro evolution" Nat. Chem. Biol. published online: 9 Dec. 2012
[DOI: 10.1038/nchembio.1138]

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Burckhard Seelig, University of Minnesota and Ritimukta Sarangi, SSRL

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