Glutaminase

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</StructureSection>
</StructureSection>
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==3D structures of glutaminase==
 
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Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
 
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{{#tree:id=OrganizedByTopic|openlevels=0|
 
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*GLN
 
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**[[3voy]], [[5d3o]] – hK-GLN – human<br />
 
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**[[5u0i]], [[5u0j]] – hK-GLN C-terminal<br />
 
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**[[4bqm]] - hL-GLN catalytic domain<br />
 
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**[[5u0k]] – hL-GLN C-terminal<br />
 
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**[[3ss3]], [[3ss4]] – mGLN C – mouse<br />
 
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**[[4jkt]] - mK-GLN<br />
 
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**[[3if5]], [[3ih8]], [[3ih9]], [[3agd]] – MlGLN – ''Micrococcus luteus''<br />
 
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**[[2pby]] – GLN – ''Geobacillus kaustophilus''<br />
 
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**[[2zk9]] – CpGLN – ''Chryseobacterium proteolyticum''<br />
 
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**[[3a54]], [[3a55]], [[3a56]] – CpGLN (mutant)<br />
 
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**[[2ksv]] – CpGLN - NMR<br />
 
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**[[3agf]] - BsGLN – ''Bacillus subtilis''<br />
 
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*GLN complex
 
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**[[3czd]], [[3unw]] – hK-GLN + Glu<br />
 
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**[[3vp0]] – hK-GLN + Gln<br />
 
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**[[3uo9]], [[3voz]], [[3vp2]], [[3vp3]], [[3vp4]], [[4o7d]], [[5fi2]], [[5fi6]], [[5fi7]], [[5hl1]], [[5i94]], [[5jyo]], [[5jyp]], [[5wj6]], [[5uqe]] - hK-GLN + inhibitor<br />
 
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**[[3vp1]] - hK-GLN + inhibitor + Glu<br />
 
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**[[3iha]], [[3ihb]], [[3age]] - MlGLN + Glu<br />
 
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**[[3ss5]] – mGLN C + Glu<br />
 
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**[[5w2j]] - mK-GLN + peptide<br />
 
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**[[3brm]], [[2osu]] – BsGLN + norleucine derivative<br />
 
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*GLN-ASN
 
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**[[1agx]] – GLN-ASN – ''Acinetobacter glutaminacificans''<br />
 
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**[[3pga]], [[4pga]] – PsGLN-ASN – ''Pseudomonas''<br />
 
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**[[1djo]], [[1djp]] - PsGLN-ASN + norvaline derivative<br />
 
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*Other GLN
 
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**[[1u60]] - YbaS <br />
 
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**[[3brm]] - YbgJ in a complex with DON <br />
 
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**[[1mki]] - YbgJ free <br />
 
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}}
 
== References ==
== References ==
<references/>
<references/>
Created with the participation of [[User:Lindsey Butler|Lindsey Butler]].
Created with the participation of [[User:Lindsey Butler|Lindsey Butler]].
[[Category:Topic Page]]
[[Category:Topic Page]]

Revision as of 09:38, 11 July 2019

Human glutaminase tetramer complex with glutamate 3unw

Drag the structure with the mouse to rotate

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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