Pub. Date : 2020 Oct 5
PMID : 33020580
3 Functional Relationships(s)Download |
Sentence | Compound Name | Protein Name | Organism |
| 1 | Combining structural analyses of cryo-electron microscopy data with molecular dynamic simulations, here we show that the cofactor NADH is a key player in the GDH regulation process. | NAD | glutamate dehydrogenase 1 | Homo sapiens |
| 2 | Our structural analysis indicates that, binding to the regulatory sites in proximity of the antenna region, NADH acts as a positive allosteric modulator by enhancing both the affinity of the inhibitor GTP binding and inhibition of GDH catalytic activity. | NAD | glutamate dehydrogenase 1 | Homo sapiens |
| 3 | We further show that the binding of GTP to the NADH-bound GDH activates a triangular allosteric network, interlinking the inhibitor with regulatory and catalytic sites. | NAD | glutamate dehydrogenase 1 | Homo sapiens |