Document Type
Article
Publication Date
2-2013
Publication Title
JBIC Journal of Biological Inorganic Chemistry
Volume
18
Issue
2
Pages
155-163
Publisher Name
Springer-Verlag
Abstract
In this review, we summarize the recent literature on dapE-encoded N-succinyl-l,l-diaminopimelic acid desuccinylase (DapE) enzymes, with an emphasis on structure–function studies that provide insight into the catalytic mechanism. Crystallographic data have also provided insight into residues that might be involved in substrate and hence inhibitor recognition and binding. These data have led to the design and synthesis of several new DapE inhibitors, which are described along with what is known about how inhibitors interact with the active site of DapE enzymes, including the efficacy of a moderately strong DapE inhibitor.
Recommended Citation
Gillner, Danuta M.; Becker, Daniel P. Ph.D.; and Holz, Richard C.. Lysine Biosynthesis in Bacteria: A Metallodesuccinylase as a Potential Antimicrobial Target. JBIC Journal of Biological Inorganic Chemistry, 18, 2: 155-163, 2013. Retrieved from Loyola eCommons, Chemistry: Faculty Publications and Other Works, http://dx.doi.org/10.1007/s00775-012-0965-1
Creative Commons License
This work is licensed under a Creative Commons Attribution-Noncommercial-No Derivative Works 3.0 License.
Copyright Statement
© 2012 SBIC
Comments
Author Posting. © 2012 SBIC, 2012. This is the author's version of the work. It is posted here by permission of Springer-Verlag for personal use, not for redistribution. The definitive version was published in JBIC Journal of Biological Inorganic Chemistry. February 2013, Volume 18, Issue 2, pp 155-163 http://link.springer.com/article/10.1007%2Fs00775-012-0965-1.