Title : Allosteric regulation of glutamate dehydrogenase deamination activity.

Pub. Date : 2020 Oct 5

PMID : 33020580

3 Functional Relationships(s)
Compound Name
Protein Name
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