The phosphothreonine lyase class of enzymes represents a recently discovered set of enzymes that catalyze a dephosphorylation reaction. The catalysis is carried out using a unique elimination mechanism without any involvement of cofactors. Crystallographic studies of SpvC, a phosphothreonine lyase, and its mutant show that the mutation of the general catalytic acid does not result in any significant perturbations to the tertiary and the secondary structure of the protein. Using results from the structural studies and a deuterium isotope exchange experiment, we conclude that the reaction catalyzed by SpvC may not involve formation of a carbanion at the active site.
| Identifer | oai:union.ndltd.org:UTAHS/oai:digitalcommons.usu.edu:etd-2414 |
| Date | 01 May 2012 |
| Creators | Shenoy, Alok Gopalkrishna |
| Publisher | DigitalCommons@USU |
| Source Sets | Utah State University |
| Detected Language | English |
| Type | text |
| Format | application/pdf |
| Source | All Graduate Theses and Dissertations |
| Rights | Copyright for this work is held by the author. Transmission or reproduction of materials protected by copyright beyond that allowed by fair use requires the written permission of the copyright owners. Works not in the public domain cannot be commercially exploited without permission of the copyright owner. Responsibility for any use rests exclusively with the user. For more information contact Andrew Wesolek (andrew.wesolek@usu.edu). |
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