Matthew D. Clay, Ph.D.
Affiliations: | 2006-2008 | University of Alberta, Edmonton, Alberta, Canada | |
| 2008- | St. Mary's University |
Website:
https://www.stmu.ca/contact-us/dr-matthew-clay/Google:
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Publications
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| Watanabe N, Clay MD, van Belkum MJ, et al. (2011) The structure of LL-diaminopimelate aminotransferase from Chlamydia trachomatis: implications for its broad substrate specificity. Journal of Molecular Biology. 411: 649-60 |
| Fan C, Clay MD, Deyholos MK, et al. (2010) Exploration of inhibitors for diaminopimelate aminotransferase. Bioorganic & Medicinal Chemistry. 18: 2141-51 |
| Fox RJ, Clay MD. (2009) Catalytic effectiveness, a measure of enzyme proficiency for industrial applications. Trends in Biotechnology. 27: 137-40 |
| Watanabe N, Clay MD, van Belkum MJ, et al. (2008) Mechanism of substrate recognition and PLP-induced conformational changes in LL-diaminopimelate aminotransferase from Arabidopsis thaliana. Journal of Molecular Biology. 384: 1314-29 |
| Watanabe N, Cherney M, van Belkum M, et al. (2008) Mechanism of stereospecific substrate recognition by LL-diaminopimelate aminotransferase Acta Crystallographica Section a Foundations of Crystallography. 64: C250-C250 |
| Watanabe N, Cherney MM, van Belkum MJ, et al. (2007) Crystal structure of LL-diaminopimelate aminotransferase from Arabidopsis thaliana: a recently discovered enzyme in the biosynthesis of L-lysine by plants and Chlamydia. Journal of Molecular Biology. 371: 685-702 |