Plach, Maximilian G. and Loeffler, Patrick and Merkl, Rainer and Sterner, Reinhard (2015) Conversion of Anthranilate Synthase into Isochorismate Synthase: Implications for the Evolution of Chorismate-Utilizing Enzymes. ANGEWANDTE CHEMIE-INTERNATIONAL EDITION, 54 (38). pp. 11270-11274. ISSN 1433-7851, 1521-3773
Full text not available from this repository. (Request a copy)Abstract
Chorismate-utilizing enzymes play a vital role in the biosynthesis of metabolites in plants as well as free-living and infectious microorganisms. Among these enzymes are the homologous primary metabolic anthranilate synthase (AS) and secondary metabolic isochorismate synthase (ICS). Both catalyze mechanistically related reactions by using ammonia and water as nucleophiles, respectively. We report that the nucleophile specificity of AS can be extended from ammonia to water by just two amino acid exchanges in a channel leading to the active site. The observed ICS/AS bifunctionality demonstrates that a secondary metabolic enzyme can readily evolve from a primary metabolic enzyme without requiring an initial gene duplication event. In a general sense, these findings add to our understanding how nature has used the structurally predetermined features of enzyme superfamilies to evolve new reactions.
| Item Type: | Article |
|---|---|
| Uncontrolled Keywords: | SALICYLATE SYNTHASE; AMINODEOXYCHORISMATE SYNTHASE; SECONDARY METABOLISM; MECHANISM; CHANNELS; PYRUVATE; chorismate; enzyme catalysis; enzyme evolution; nucleophile specificity; protein design |
| Subjects: | 500 Science > 570 Life sciences |
| Divisions: | Biology, Preclinical Medicine > Institut für Biophysik und physikalische Biochemie |
| Depositing User: | Dr. Gernot Deinzer |
| Date Deposited: | 07 Jun 2019 09:35 |
| Last Modified: | 07 Jun 2019 09:35 |
| URI: | https://pred.uni-regensburg.de/id/eprint/4831 |
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