Glutaminase

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== Structural highlights ==
== Structural highlights ==
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The glutamate binding site is in the helical domain of GLN and <scene name='49/497107/Cv/4'>Tyr residue serves as a general acid in the catalysis</scene><ref>PMID:22049910</ref>. <scene name='49/497107/Cv/3'>Whole glutamate binding site</scene>.
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The glutamate binding site is in the helical domain of GLN and <scene name='49/497107/Cv/5'>Tyr residue serves as a general acid in the catalysis</scene><ref>PMID:22049910</ref>. <scene name='49/497107/Cv/6'>Whole glutamate binding site</scene>.
</StructureSection>
</StructureSection>
==3D structures of glutaminase==
==3D structures of glutaminase==

Revision as of 13:35, 1 April 2019

Human glutaminase tetramer complex with glutamate 3unw

Drag the structure with the mouse to rotate

3D structures of glutaminase

Updated on 01-April-2019

References

  1. Curthoys NP. Role of mitochondrial glutaminase in rat renal glutamine metabolism. J Nutr. 2001 Sep;131(9 Suppl):2491S-5S; discussion 2496S-7S. PMID:11533299
  2. Steckel J, Roberts J, Philips FS, Chou TC. Kinetic properties and inhibition of Acinetobacter glutaminase-asparaginase. Biochem Pharmacol. 1983 Mar 15;32(6):971-7. PMID:6838661
  3. Erickson JW, Cerione RA. Glutaminase: a hot spot for regulation of cancer cell metabolism? Oncotarget. 2010 Dec;1(8):734-40. PMID:21234284 doi:http://dx.doi.org/10.18632/oncotarget.208
  4. Curthoys NP, Watford M. Regulation of glutaminase activity and glutamine metabolism. Annu Rev Nutr. 1995;15:133-59. PMID:8527215 doi:http://dx.doi.org/10.1146/annurev.nu.15.070195.001025
  5. Delabarre B, Gross S, Fang C, Gao Y, Jha A, Jiang F, Song J J, Wei W, Hurov JB. Full-Length Human Glutaminase in Complex with an Allosteric Inhibitor. Biochemistry. 2011 Nov 18. PMID:22049910 doi:10.1021/bi201613d

Created with the participation of Lindsey Butler.

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Michal Harel, Alexander Berchansky, Joel L. Sussman

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