BPTES inhibition of hGA124–551, a truncated form of human kidney-type glutaminase
نویسندگان
چکیده
منابع مشابه
the investigation of the relationship between type a and type b personalities and quality of translation
چکیده ندارد.
Structural Basis for the Active Site Inhibition Mechanism of Human Kidney-Type Glutaminase (KGA)
Glutaminase is a metabolic enzyme responsible for glutaminolysis, a process harnessed by cancer cells to feed their accelerated growth and proliferation. Among the glutaminase isoforms, human kidney-type glutaminase (KGA) is often upregulated in cancer and is thus touted as an attractive drug target. Here we report the active site inhibition mechanism of KGA through the crystal structure of the...
متن کاملStructural basis for exploring the allosteric inhibition of human kidney type glutaminase
Cancer cells employ glutaminolysis to provide a source of intermediates for their upregulated biosynthetic needs. Glutaminase, which catalyzes the conversion of glutamine to glutamate, is gaining increasing attention as a potential drug target. Small-molecule inhibitors such as BPTES and CB-839, which target the allosteric site of glutaminase with high specificity, demonstrate immense promise a...
متن کاملNovel mechanism of inhibition of rat kidney-type glutaminase by bis-2-(5-phenylacetamido-1,2,4-thiadiazol-2-yl)ethyl sulfide (BPTES).
The release of GA (mitochondrial glutaminase) from neurons following acute ischaemia or during chronic neurodegenerative diseases may contribute to the propagation of glutamate excitotoxicity. Thus an inhibitor that selectively inactivates the released GA may limit the accumulation of excess glutamate and minimize the loss of neurological function that accompanies brain injury. The present stud...
متن کاملInhibition by glutamate of phosphate-dependent glutaminase of rat kidney.
A membrane-associated form of phosphate-dependent glutaminase was derived from sonicated mitochondria and purified essentially free of gamma-glutamyl transpeptidase activity. Increasing concentrations of phosphate cause a sigmoidal activation of the membrane-bound glutaminase. Phosphate also causes a similar effect on the rate of glutaminase inactivation by the two affinity labels, L-2-amino-4-...
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ژورنال
عنوان ژورنال: Journal of Enzyme Inhibition and Medicinal Chemistry
سال: 2011
ISSN: 1475-6366,1475-6374
DOI: 10.3109/14756366.2011.622272