Glutaminase
From Proteopedia
(Difference between revisions)
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== Function == | == Function == | ||
| - | '''Glutaminase''' (GLN) catalyzes the conversion of glutamine (Gln) to glutamic acid (Glu). GLN is present at the axonal termini of neurons where GA functions as a neurotransmitter. ADP is an activator of GLN. GLN is a homodimer<ref>PMID:11533299</ref>. In human GLN is found as 2 isozymes – GLN and GLN 2. '''Glutaminase-asparaginase''' (GLN-ASN) can amidohydrolase both glutamine and asparagine to their corresponding Glu and Asp<ref>PMID:6838661</ref>. | + | '''Glutaminase''' (GLN) catalyzes the conversion of glutamine (Gln) to glutamic acid (Glu). GLN is present at the axonal termini of neurons where GA functions as a neurotransmitter. ADP is an activator of GLN. GLN is a homodimer<ref>PMID:11533299</ref>. '''K-GLN''' is the kidney isoform; '''L-GLN''' is the liver isoform. In human GLN is found as 2 isozymes – GLN and GLN 2. '''Glutaminase-asparaginase''' (GLN-ASN) can amidohydrolase both glutamine and asparagine to their corresponding Glu and Asp<ref>PMID:6838661</ref>. |
==Relevance== | ==Relevance== | ||
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**[[3agf]] - BsGLN – ''Bacillus subtilis''<br /> | **[[3agf]] - BsGLN – ''Bacillus subtilis''<br /> | ||
**[[3ss3]], [[3ss4]] – mGLN C – mouse<br /> | **[[3ss3]], [[3ss4]] – mGLN C – mouse<br /> | ||
| - | **[[4jkt]] - | + | **[[4jkt]] - mK-GLN<br /> |
| - | **[[3voy]], [[5d3o]] – | + | **[[3voy]], [[5d3o]] – hK-GLN – human<br /> |
| - | **[[4bqm]] - | + | **[[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 /> | **[[3brm]], [[2osu]] – BsGLN + norleucine derivative<br /> | ||
| - | **[[3czd]], [[3unw]] – | + | **[[3czd]], [[3unw]] – hK-GLN + Glu<br /> |
| - | **[[3vp0]] – | + | **[[3vp0]] – hK-GLN + Gln<br /> |
| - | **[[3uo9]], [[3voz]], [[3vp2]], [[3vp3]], [[3vp4]], [[4o7d]], [[5fi2]], [[5fi6]], [[5fi7]], [[5hl1]], [[5i94]], [[5jyo]], [[5jyp]] - | + | **[[3uo9]], [[3voz]], [[3vp2]], [[3vp3]], [[3vp4]], [[4o7d]], [[5fi2]], [[5fi6]], [[5fi7]], [[5hl1]], [[5i94]], [[5jyo]], [[5jyp]], [[5wj6]], [[5uqe]] - hK-GLN + inhibitor<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 + Glu<br /> | ||
| - | **[[3vp1]] - hGLN + inhibitor + Glu<br /> | ||
*GLN-ASN | *GLN-ASN | ||
Revision as of 06:37, 31 May 2018
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3D structures of glutaminase
Updated on 31-May-2018
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.
