Glutamate racemase

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<StructureSection load='2jfq' size='350' side='right' caption='Structure of glutamate racemase dimer complex with D-glutamate (PDB entry [[2jfq]])' scene=''>
<StructureSection load='2jfq' size='350' side='right' caption='Structure of glutamate racemase dimer complex with D-glutamate (PDB entry [[2jfq]])' scene=''>
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== Function ==
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'''Glutamate racemase''' (GR) catalyzes the racemization of L-glutamate to D-glutamate. GR plays a major role in bacterial cell wall biosynthesis and moonlights as gyrase inhibitor. GR inhibition is used as anti-bacterial target.
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'''Glutamate racemase''' (GR) catalyzes the racemization of L-glutamate to D-glutamate. GR plays a major role in bacterial cell wall biosynthesis and moonlights as gyrase inhibitor<ref>PMID:18757813</ref>.
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== Relevance ==
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GR inhibition is used as anti-bacterial target.
</StructureSection>
</StructureSection>
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**[[2ohv]] – SpGR + D-glutamate derivative inhibitor <BR />
**[[2ohv]] – SpGR + D-glutamate derivative inhibitor <BR />
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}}
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== References ==
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<references/>
[[Category:Topic Page]]
[[Category:Topic Page]]

Revision as of 10:23, 8 March 2016

Structure of glutamate racemase dimer complex with D-glutamate (PDB entry 2jfq)

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3D Structures of glutamate racemase

Updated on 08-March-2016

References

  1. 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

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Michal Harel, Alexander Berchansky

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