Glutaminase
From Proteopedia
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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>. '''K-GLN''' is the kidney isoform | + | '''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. |
| + | *'''K-GLN''' is the kidney isoform | ||
| + | *'''L-GLN''' is the liver isoform. | ||
| + | * '''Glutaminase-asparaginase''' (GLN-ASN) can amidohydrolase both glutamine and asparagine to their corresponding Glu and Asp<ref>PMID:6838661</ref>. For details on GLN-ASN see [[Glutaminase-Asparaginase (Pseudomonas 7A)]]. | ||
==Relevance== | ==Relevance== | ||
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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/ | + | 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== | ==3D structures of glutaminase== | ||
| + | [[Glutaminase 3D structures]] | ||
| - | + | </StructureSection> | |
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| - | **[[1u60]] - YbaS <br /> | ||
| - | **[[3brm]] - YbgJ in a complex with DON <br /> | ||
| - | **[[1mki]] - YbgJ free <br /> | ||
| - | }} | ||
== 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]] | ||
Current revision
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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.
