Glutamate racemase
From Proteopedia
(Difference between revisions)
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== Relevance == | == Relevance == | ||
| - | GR inhibition is used as anti-bacterial target. | + | GR inhibition is used as anti-bacterial target<ref>PMID:22877632</ref>. |
== Structural highlights == | == Structural highlights == | ||
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**[[2jfz]], [[2w4i]], [[4b1f]] – HpGR + D-glutamate + inhibitor <BR /> | **[[2jfz]], [[2w4i]], [[4b1f]] – HpGR + D-glutamate + inhibitor <BR /> | ||
**[[2ohv]] – SpGR + D-glutamate derivative inhibitor <BR /> | **[[2ohv]] – SpGR + D-glutamate derivative inhibitor <BR /> | ||
| + | **[[5hj7]] – GR + D-glutamate – ''Mycobacterium tuberculosis''<BR /> | ||
| + | **[[5ijw]] – GR + D-glutamate – ''Mycobacterium smegmatis''<BR /> | ||
}} | }} | ||
== References == | == References == | ||
<references/> | <references/> | ||
[[Category:Topic Page]] | [[Category:Topic Page]] | ||
Revision as of 08:50, 28 May 2017
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3D Structures of glutamate racemase
Updated on 28-May-2017
References
- ↑ Sengupta S, Ghosh S, Nagaraja V. Moonlighting function of glutamate racemase from Mycobacterium tuberculosis: racemization and DNA gyrase inhibition are two independent activities of the enzyme. Microbiology. 2008 Sep;154(Pt 9):2796-803. doi: 10.1099/mic.0.2008/020933-0. PMID:18757813 doi:http://dx.doi.org/10.1099/mic.0.2008/020933-0
- ↑ Basarab GS, Hill P, Eyermann CJ, Gowravaram M, Kack H, Osimoni E. Design of inhibitors of Helicobacter pylori glutamate racemase as selective antibacterial agents: Incorporation of imidazoles onto a core pyrazolopyrimidinedione scaffold to improve bioavailabilty. Bioorg Med Chem Lett. 2012 Sep 1;22(17):5600-7. Epub 2012 Jul 20. PMID:22877632 doi:http://dx.doi.org/10.1016/j.bmcl.2012.07.004
- ↑ Lundqvist T, Fisher SL, Kern G, Folmer RH, Xue Y, Newton DT, Keating TA, Alm RA, de Jonge BL. Exploitation of structural and regulatory diversity in glutamate racemases. Nature. 2007 Jun 14;447(7146):817-22. PMID:17568739 doi:http://dx.doi.org/10.1038/nature05689
