Glutaminase
From Proteopedia
(Difference between revisions)
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== Structural highlights == | == Structural highlights == | ||
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>. | 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>. | ||
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| + | ==3D structures of glutaminase== | ||
| + | [[Glutaminase 3D structures]] | ||
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</StructureSection> | </StructureSection> | ||
==3D structures of glutaminase== | ==3D structures of glutaminase== | ||
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*GLN | *GLN | ||
| + | **[[3voy]], [[5d3o]] – hK-GLN – human<br /> | ||
| + | **[[5u0i]], [[5u0j]] – hK-GLN C-terminal<br /> | ||
| + | **[[4bqm]] - hL-GLN catalytic domain<br /> | ||
| + | **[[5u0k]] – hL-GLN C-terminal<br /> | ||
| + | **[[3ss3]], [[3ss4]] – mGLN C – mouse<br /> | ||
| + | **[[4jkt]] - mK-GLN<br /> | ||
**[[3if5]], [[3ih8]], [[3ih9]], [[3agd]] – MlGLN – ''Micrococcus luteus''<br /> | **[[3if5]], [[3ih8]], [[3ih9]], [[3agd]] – MlGLN – ''Micrococcus luteus''<br /> | ||
**[[2pby]] – GLN – ''Geobacillus kaustophilus''<br /> | **[[2pby]] – GLN – ''Geobacillus kaustophilus''<br /> | ||
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**[[2ksv]] – CpGLN - NMR<br /> | **[[2ksv]] – CpGLN - NMR<br /> | ||
**[[3agf]] - BsGLN – ''Bacillus subtilis''<br /> | **[[3agf]] - BsGLN – ''Bacillus subtilis''<br /> | ||
| - | **[[3ss3]], [[3ss4]] – mGLN C – mouse<br /> | ||
| - | **[[4jkt]] - mK-GLN<br /> | ||
| - | **[[3voy]], [[5d3o]] – hK-GLN – human<br /> | ||
| - | **[[5u0i]], [[5u0j]] – hK-GLN C-terminal<br /> | ||
| - | **[[4bqm]] - hL-GLN catalytic domain<br /> | ||
| - | **[[5u0k]] – hL-GLN C-terminal<br /> | ||
*GLN complex | *GLN complex | ||
| - | **[[3brm]], [[2osu]] – BsGLN + norleucine derivative<br /> | ||
**[[3czd]], [[3unw]] – hK-GLN + Glu<br /> | **[[3czd]], [[3unw]] – hK-GLN + Glu<br /> | ||
**[[3vp0]] – hK-GLN + Gln<br /> | **[[3vp0]] – hK-GLN + Gln<br /> | ||
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**[[3vp1]] - hK-GLN + inhibitor + Glu<br /> | **[[3vp1]] - hK-GLN + inhibitor + Glu<br /> | ||
**[[3iha]], [[3ihb]], [[3age]] - MlGLN + Glu<br /> | **[[3iha]], [[3ihb]], [[3age]] - MlGLN + Glu<br /> | ||
| - | **[[3ss5]] – mGLN + Glu<br /> | + | **[[3ss5]] – mGLN C + Glu<br /> |
| + | **[[5w2j]] - mK-GLN + peptide<br /> | ||
| + | **[[3brm]], [[2osu]] – BsGLN + norleucine derivative<br /> | ||
*GLN-ASN | *GLN-ASN | ||
Revision as of 09:37, 11 July 2019
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3D structures of glutaminase
Updated on 11-July-2019
References
- ↑ 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
- ↑ 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
- ↑ 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
- ↑ 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
- ↑ 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.
