Glutaminase
From Proteopedia
(Difference between revisions)
| Line 1: | Line 1: | ||
| - | + | <StructureSection load='3unw' size='350' side='right' scene='' caption='Human glutaminase tetramer complex with glutamate [[3unw]]'> | |
| + | |||
== 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>. 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>. | ||
| Line 8: | Line 9: | ||
== Structural highlights == | == Structural highlights == | ||
The glutamate binding site is in the helical domain of GLN and Tyr residue serves as a general acid in the catalysis<ref>PMID:22049910</ref>. | The glutamate binding site is in the helical domain of GLN and Tyr residue serves as a general acid in the catalysis<ref>PMID:22049910</ref>. | ||
| - | + | </StructureSection> | |
==3D structures of glutaminase== | ==3D structures of glutaminase== | ||
Revision as of 12:59, 13 March 2016
| |||||||||||
3D structures of glutaminase
Updated on 13-March-2016
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.
