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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Murciano-calles, Javier Buller, Andrew R. Arnold, Frances H. Romney, David K. Herger, Michael Brinkmann-chen, Sabine |
| Description | Author Affiliation: Buller AR ( Division of Chemistry and Chemical Engineering, California Institute of Technology, Pasadena, CA 91125.); Brinkmann-Chen S ( Division of Chemistry and Chemical Engineering, California Institute of Technology, Pasadena, CA 91125.); Romney DK ( Division of Chemistry and Chemical Engineering, California Institute of Technology, Pasadena, CA 91125.); Herger M ( Division of Chemistry and Chemical Engineering, California Institute of Technology, Pasadena, CA 91125.); Murciano-Calles J ( Division of Chemistry and Chemical Engineering, California Institute of Technology, Pasadena, CA 91125.); Arnold FH ( Division of Chemistry and Chemical Engineering, California Institute of Technology, Pasadena, CA 91125 frances@cheme.caltech.edu.); |
| Abstract | Enzymes in heteromeric, allosterically regulated complexes catalyze a rich array of chemical reactions. Separating the subunits of such complexes, however, often severely attenuates their catalytic activities, because they can no longer be activated by their protein partners. We used directed evolution to explore allosteric regulation as a source of latent catalytic potential using the ß-subunit of tryptophan synthase from Pyrococcus furiosus (PfTrpB). As part of its native ßß complex, TrpB efficiently produces tryptophan and tryptophan analogs; activity drops considerably when it is used as a stand-alone catalyst without the -subunit. Kinetic, spectroscopic, and X-ray crystallographic data show that this lost activity can be recovered by mutations that reproduce the effects of complexation with the -subunit. The engineered PfTrpB is a powerful platform for production of Trp analogs and for further directed evolution to expand substrate and reaction scope. |
| ISSN | 00278424 |
| e-ISSN | 10916490 |
| Journal | Proceedings of the National Academy of Sciences of the United States of America |
| Issue Number | 47 |
| Volume Number | 112 |
| Language | English |
| Publisher | National Academy of Sciences |
| Publisher Date | 2015-11-01 |
| Publisher Place | United States |
| Access Restriction | Open |
| Subject Keyword | Directed Molecular Evolution Protein Subunits Metabolism Pyrococcus Furiosus Enzymology Tryptophan Synthase Allosteric Regulation Amino Acids Biocatalysis Crystallography, X-Ray Genetic Engineering Ligands Models, Molecular Mutagenesis, Site-Directed Mutation Genetics Chemistry Salmonella Typhimurium Spectrophotometry, Ultraviolet Substrate Specificity Research Support, N.I.H., Extramural Research Support, Non-U.S. Gov't Multidisciplinary |
| Content Type | Text |
| Resource Type | Article |
| Subject | Multidisciplinary |
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