MosA is an enzyme from Sinorhizobium meliloti L5-30, a beneficial soil bacterium. Initial investigation into this enzyme categorized it as a methyltransferase. Further investigation revealed that this was incorrect, and that MosA is actually a dihydrodipicolinate synthase, part of the N-acetylneuraminate lyase superfamily. One of the characteristics of enzyme superfamilies is their low sequence identity, but relatively high structural similarity. The structural investigation reported here confirms the high structural similarity between MosA and other superfamily members. <p>Investigation of MosA was carried out by means of x-ray crystallography. It was believed that detailed structural information may shed light into not only the enzymatic mechanism, but also the inhibition of MosA by lysine, the final product of the enzymatic pathway. Insight into enzyme mechanism and inhibition may ultimately prove useful in herbicide or insecticide development, as other dihydrodipicolinate synthases from harmful fungi, bacteria, or plants, make attractive targets for inhibition. Lysine is an essential amino acid for humans, meaning that there is no endogenous lysine production to block the use of these hypothetical inhibitors. Specific inhibitors based on crystal structures have proven to be effective in the past and hopefully, will continue to be useful in the future. <p>Here we report the structure of MosA, solved to 1.95 Å resolution with lysine 161 forming a Schiff-base adduct with pyruvate. This adduct is consistent with the currently accepted dihydrodipicolinate synthase enzyme mechanism.
| Identifer | oai:union.ndltd.org:LACETR/oai:collectionscanada.gc.ca:SSU.etd-04252008-150200 |
| Date | 29 April 2008 |
| Creators | Nienaber, Kurt |
| Contributors | Warrington, Rob C., Moore, Stanley A., Khandelwal, Ramji L., Delbaere, Louis T. J., Yang, Jian |
| Publisher | University of Saskatchewan |
| Source Sets | Library and Archives Canada ETDs Repository / Centre d'archives des thèses électroniques de Bibliothèque et Archives Canada |
| Language | English |
| Detected Language | English |
| Type | text |
| Format | application/pdf |
| Source | http://library.usask.ca/theses/available/etd-04252008-150200/ |
| Rights | unrestricted, I hereby certify that, if appropriate, I have obtained and attached hereto a written permission statement from the owner(s) of each third party copyrighted matter to be included in my thesis, dissertation, or project report, allowing distribution as specified below. I certify that the version I submitted is the same as that approved by my advisory committee. I hereby grant to University of Saskatchewan or its agents the non-exclusive license to archive and make accessible, under the conditions specified below, my thesis, dissertation, or project report in whole or in part in all forms of media, now or hereafter known. I retain all other ownership rights to the copyright of the thesis, dissertation or project report. I also retain the right to use in future works (such as articles or books) all or part of this thesis, dissertation, or project report. |
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